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Science 18 December 1998:
Vol. 282. no. 5397, pp. 2266 - 2269
DOI: 10.1126/science.282.5397.2266
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Reports

A Receptor/Cytoskeletal Movement Triggered by Costimulation During T Cell Activation

Christoph Wülfing, Mark M. Davis *

During T cell activation, the engagement of costimulatory molecules is often crucial to the development of an effective immune response, but the mechanism by which this is achieved is not known. Here, it is shown that beads attached to the surface of a T cell translocate toward the interface shortly after the start of T cell activation. This movement appears to depend on myosin motor proteins and requires the engagement of the major costimulatory receptor pairs, B7-CD28 and ICAM-1-LFA-1. This suggests that the engagement of costimulatory receptors triggers an active accumulation of molecules at the interface of the T cell and the antigen-presenting cell, which then increases the overall amplitude and duration of T cell signaling.

Howard Hughes Medical Institute and Department of Microbiology and Immunology, Stanford University School of Medicine, Stanford, CA 94305, USA.
*   To whom correspondence should be addressed.

The central event in T cell activation is the interaction of the T cell receptor (TCR) with the antigenic peptide presented by the major histocompatibility complex (MHC) of the antigen-presenting cell (APC). However, because the number of agonist peptide-MHC complexes can be very low, in the range of 10 to 100 per APC (1), and because the TCR is continuously modulated from the T cell surface (2), sustained T cell activation is likely to require signal amplification (3, 4). An important component of this amplification is thought to be provided by costimulatory molecules on the T cell, although the mechanism by which they accomplish it is unclear (5). The most important of the costimulatory receptors on T cells and their ligand on APCs are CD28-B7 (6) and LFA-1-ICAM-1 (7). Many different receptor couples, including TCR-peptide-MHC and LFA-1-ICAM-1, accumulate at the T cell-APC interface (8, 9). This accumulation has been assumed to be a passive, diffusion-limited cocapping mechanism (10). Here, we describe an active, cytoskeletal mechanism that appears to drive receptor accumulation at the T cell-APC interface. This mechanism requires the APC to express B7 and ICAM-1 and is independent of TCR signaling. We suggest that this mechanism is a central part of costimulation, as it would effectively amplify any TCR-mediated signals.

To study whether receptor accumulation at the T cell-APC interface could be actively driven by the T cell cytoskeleton, we monitored the general movement of the cortical actin cytoskeleton and linked receptors (11) using the classical technique of attaching large beads to the surfaces of antigen-specific T cells. We coated 4.5-µm beads with an antibody to the T cell surface antigen ICAM-1 (12). Cross-linking ICAM-1 by beads in this way is not expected to influence T cell function (13). As has been observed with fibroblasts (11, 14), we find that in migrating 5C.C7 transgenic T cells (9, 15) the beads translocate from the anterior to the posterior end of the cell (16). We then mixed bead-loaded 5C.C7 T cells with B cell lymphoma cells that express the appropriate MHC molecule (I-Ek) and have been pulsed with the moth cytochrome c peptide 88-103. After contact with the APC, the T cells rapidly become activated (9, 17) and the beads move from the posterior end of the T cell to the newly formed interface with the B cells (Fig. 1, movie 1) beginning 4 ± 1 min after the first rise in intracellular calcium (n = 13). This suggests that the T cell cortical actin cytoskeleton reorients toward the T cell-APC interface soon after the start of T cell activation. The ensuing cytoskeletal flow would allow receptors that are linked to the actin cytoskeleton to be transported to the newly formed T cell-APC interface.

Fig. 1. Bead movement toward the interface. Single frames of a video microscopy experiment (36) of the interaction of 5C.C7 T cells, loaded with 4.5-µm anti-ICAM-1 (YN1) beads, with peptide-loaded CH27 B cell lymphoma cells (35) are shown. The CH27 cell is substantially larger than the T cells. The T cell intracellular calcium concentration is overlaid in a false color scale from blue (low concentration) to red (high concentration) to mark the onset of T cell activation, set to time 0:00 min. Although the beads, one of which is marked with an arrow, are bound to the posterior end of the central T cell before and at the time of its activation, they can be seen to move toward the T cell-B cell interface in subsequent frames. The still frames have been excerpted from movie 1 (37), which can be viewed at Science Online (http://www.sciencemag.org/feature/data/984937.shl). [View Larger Version of this Image (80K GIF file)]

To rule out ICAM-1-specific effects, we also attached beads to T cells in two other ways. First, we surface-biotinylated the 5C.C7 T cells with an amine-reactive form of biotin and used 2.8-µm streptavidin beads (18). Second, we exchanged a lipid that is biotinylated at its head into the cell surface of the T cells from liposomes (19) and used the same 2.8-µm streptavidin beads (20). In both cases, we found a behavior identical to that of the antibody-coated beads (Table 1). This confirms that the beads monitor the movement of the cortical actin cytoskeleton and not that of a specific receptor. We have also obtained identical results using monocytes and dendritic cells prepared directly ex vivo as APCs (16). The time to travel half a cell circumference is 6 ± 2 min (n = 14). Given that the diameter of our activated T cells is ~10 µm, this speed of ~3 µm/min is similar to that reported in comparable studies on migrating fibroblasts (1 to 5 µm/min) (21). This behavior is independent of the peptide concentration on the APC as long as enough peptide is presented to activate the T cell (16). Beads bound to the B cell do not move, consistent with the lack of involvement of the B cell actin cytoskeleton in the redistribution of specific receptors (9, 22).

Table 1. Occurrence of different types of T cell bead movement (39) during the interaction of a 5C.C7 T cell with APCs loaded with an activating peptide. Unless mentioned, the APCs were CH27 B cell lymphomas. Bead movement was analyzed using three different types of beads (12, 18, 20); only two of these bead types (12, 18) were used for the rest of the experiments. Blocking antibodies and pharmacological agents were used under standard conditions. (40). The number of cells analyzed during wortmannin treatment was small because the majority of the T cells did not establish a polarized phenotype (41). When transfected CHO cells were used as APCs, we found that GFP fusion did not inhibit the function of its fusion partner (9, 22). In the last row, an activating antibody to CD28 was present during the interaction of the T cell and APC; n indicates the number of cells studied (34).

Type of beads/treatment/APC Movement toward interface Movement away from interface No movement n
Type of beads
Anti-ICAM 74% 0% 26% 81
Streptavidin (surface biotin) 83% 7% 10% 29
Streptavidin (lipid biotin) 64% 5% 32% 22
Antibody blocking
anti-ICAM 11% 5% 84% 37
anti-B7 8% 0% 92% 24
anti-VCAM 62% 0% 38% 21
anti-CD48 75% 0% 25% 20
Pharmacological agents
Wortmannin 13% 0% 78% 8
Ni/BAPTA 23% 0% 77% 26
Transfected CHO cells as APCs
CHO/I-Ek 4% 0% 96% 47
CHO/I-Ek/ICAM-1-GFP 27% 7% 67% 45
CHO/I-Ek/B7-2-GFP 34% 2% 64% 47
CHO/I-Ek/ICAM-1-GFP (anti-CD28) 59% 0% 41% 27

To study the role of costimulatory receptor pairs in the regulation of the cytoskeletal movement, we added antibodies that block a number of accessory interactions to this system. We found that blocking ICAM-1 or B7-1 together with B7-2 abolishes bead movement while leaving undisturbed other aspects of T cell activation, such as the formation of a tight interface and the elevation of intracellular calcium (Table 1) (16). Antibodies to CD48 or VCAM had no effect (Table 1). To determine whether the interactions of ICAM-1 with LFA-1 or of B7 with CD28 are sufficient to trigger bead movement, we used transfected CHO cells as APCs. When transfected with I-Ek, the CHO cells were not able to induce bead movement (Table 1). When the CHO cells were transfected with I-Ek and either ICAM-1 or B7-2 gene constructs, we observed a partial restoration of the bead movement (Table 1). The best results were obtained by transfecting ICAM-1 and engaging CD28 on the T cell with an activating antibody, which allows bead movement to near B cell levels (Table 1). Preliminary experiments with CHO cells expressing all three molecules (I-Ek, ICAM-1, and B7-2) showed that 7 of 10 T-CHO couples examined moved beads toward the T cell-APC interface (16). These experiments show that the interactions of LFA-1-ICAM-1 and CD28-B7 are both necessary and sufficient to induce movement of the T cell cortical actin cytoskeleton toward the newly formed T cell-APC interface.

We have also characterized second messengers that are synergistically activated by the TCR and the accessory interactions that are important for bead movement, namely the intracellular calcium concentration for ICAM-1-LFA-1 (9, 23) and the phosphatidylinositol 3-kinase (PI 3-kinase) for B7-CD28 (24). Blocking the rise in the intracellular calcium concentration with 1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid (BAPTA) and Ni2+ blocks bead movement (Table 1) while leaving the formation of a tight interface intact (9). Using the PI 3-kinase inhibitor wortmannin (25) at 100 nM leads to a distinct phenotype in that most T cells do not establish a polarized phenotype before activation. For the minority of T cells that display a polarized phenotype, bead movement is abolished. These results are consistent with both PI 3-kinase and intracellular calcium being necessary for bead movement.

The cortical actin cytoskeleton moves either by controlled assembly and disassembly of actin filaments or by sliding actin filaments past each other using myosin motor proteins (11, 26). In particular, myosin motor proteins are thought to be involved in actin cytoskeleton movement at the cell body (21). Previously, we and others have shown that blocking actin filament assembly in the T cell (but not B cell APCs) with cytochalasin D severely disrupts many aspects of T cell activation (3, 9). Inhibiting the myosin motors with butanedione monoxime (BDM) (27) gives a more specific phenotype in this system, as shown in Fig. 2 (movie 2) and Table 2. At high concentrations of BDM, the diameter of the T cell-B cell interface is reduced, the calcium signal is less sustained, the redistribution of ICAM-1 to the T cell-B cell interface is impaired, the redistribution of I-Ek is inhibited (22), and bead movement is partially blocked (Table 2). At low BDM concentrations (2 mM), the reduction in interface diameter and the impairment of bead movement remain (Table 2), suggesting that myosin motors are most involved in these two processes. Because BDM has also been reported to block T cell potassium uptake (28), we inhibited voltage-gated potassium channels specifically with noxius toxin (29) and found no inhibition of bead movement (Table 2). The small effect we see on early T cell activation is consistent with the moderate effects reported for specific potassium channel blockers on later activation events (30). We conclude that the receptor/cytoskeletal movement that we describe here is dependent on myosin motor proteins.

Fig. 2. T cell-APC interaction with blocked myosin motor proteins. (A) Single frames of a video microscopy experiment (36) of the interaction of 5C.C7 T cells, loaded with 4.5-µm anti-ICAM-1 (YN1) beads, with peptide-loaded, ICAM-1-GFP-transfected CH27 cells are shown. The bright-field image has been duplicated. In the top panels, the T cell intracellular calcium concentration is overlaid in a false color scale as in Fig. 1. In the bottom panels, the ICAM-1-GFP fluorescence is overlaid in a false color scale from green (low fluorescence) to blue (high fluorescence) to allow the simultaneous investigation of the additional cellular parameter. The accumulation of ICAM-1 at the T cell-APC interface in the absence of all pharmacological agents was described in (9); here, such an interaction is shown in the presence of 2 µM BDM. Although the calcium signal is elevated in a stable manner and ICAM-1-GFP accumulates at the interface, this interface is narrow (as most easily seen by the tightly concentrated ICAM-1-GFP accumulation), and a bead that is bound to an activating T cell, marked with an arrow, does not move. The still frames were excerpted from movie 2 (38), which can be viewed at Science Online (http://www.sciencemag.org/feature/data/984937.shl). (B) An even narrower interface at 20 µM BDM, excerpted from a movie of a different experiment. [View Larger Version of this Image (54K GIF file)]

Table 2. Effects of blocking myosin motor proteins. The analysis of T cell activation by peptide loaded CH27 cells in the presence of BDM or noxius toxin (NTX) is shown (42). Narrow interface form denotes activated T cells having a T cell-B cell interface diameter that is smaller than the diameter of the T cell (Fig. 2). Calcium signal back to baseline denotes activated T cells whose intracellular calcium concentration returns to preactivation levels during an observation period of at least 5 min. ICAM cluster formation denotes CH27 cells that show accumulation of ICAM-1-GFP at the T cell-B cell interface after T cell activation (9) (Fig. 2). Bead movement toward the interface (39) refers to activated T cells that show anti-ICAM-1 bead movement. In all cases, n denotes the number of cells analyzed (43).

Pharmacol. agent Interface form
 Calcium signal
 ICAM clustering
 Bead movement
Narrow n Back to baseline n Cluster formation n Toward interface n
BDM (20 mM) 93% 55 68% 108 36% 33 19% 27
BDM (10 mM) 79% 58 45% 83 51% 35 27% 15
BDM (2 mM) 70% 46 23% 73 85% 32 25% 28
Buffer alone 14% 56 2% 102 90% 38 62% 21
NTX (100 nM) 23% 47 9% 76 85% 40 63% 27

In vivo, costimulation is usually required for efficient T cell activation, probably because TCR signaling is limited by small numbers of agonist peptide-MHC complexes and continuous internalization of the TCR-CD3 complex. Previously, we have shown that the accumulation of MHC-peptide-TCR and accessory receptor couples at the T cell-APC interface after T cell activation can amplify the weak TCR signal efficiently (9, 22). Here, we have described an active movement of the cortical actin cytoskeleton toward the interface, involving myosin motor proteins, that would move all molecules linked to the actin cytoskeleton toward the T cell-APC interface. In support of this possibility, we find that the increase in concentration of LFA-1-ICAM-1 and other (TCR-peptide-I-Ek and CD2-CD48) receptor couples at the interface and the movement of the cortical cytoskeleton are regulated similarly. Both processes are sensitive to the myosin inhibitor BDM, to anti-B7, and to the choice of APC (9, 22) (Table 2). Furthermore, we have shown that this movement of the actin cytoskeleton is regulated by the two most important costimulatory receptor pairs, CD28-B7 and LFA-1-ICAM-1. We suggest that this active accumulation of receptor pairs and other cytoskeleton-linked molecules at the T cell-APC interface, and the signal amplification that would result from these increased receptor densities, could be the principal basis of the costimulatory effect. This is in contrast to models in which a costimulatory signal integrates with TCR signals in the nucleus to affect gene expression.

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  34. The results are derived from a composite analysis of at least seven experiments (11 on average) performed on at least two different days (four on average) for each condition. We show a composite analysis because on average only three or four cells per experiment could be analyzed. To ensure consistency within the data set, at least one positive control experiment was included during each day of experiments.
  35. The CH27 cells used in this particular experiment were ICAM-1-GFP transfected. ICAM-1-GFP transfection of the CH27 cells has no effect on the bead movement (16). The ICAM-1-GFP fluorescence is not shown.
  36. Peptide loading of APCs using 10 µM moth cytochrome c peptide 82-103, Fura-2 loading of T cells, and microscopy (using the Zeiss/Attofluor system) were performed as in (9).
  37. Movie 1: Bead movement toward the interface. The interaction of 5C.C7 T cells, loaded with 4.5-µm anti-ICAM-1 (YN1) beads, with peptide-loaded CH27 B cell lymphoma cells (35) is shown. The CH27 cell is substantially larger than the T cells. Although the beads are bound to the posterior end of the top T cell before and at the time of its activation, they can be seen to move toward the T cell-B cell interface in subsequent frames. The T cell intracellular calcium concentration is overlaid in a false color scale. Two closely related calcium-sensitive dyes that differ in their calcium dissociation constant, Fura-PE in movie 1 and Fura-2 in movie 2, have been used. Therefore, blue indicates low calcium concentration in both movies, whereas high calcium concentration is encoded in yellow in movie 1 and in red in movie 2. For reasons of simplicity, in Fig. 1 the calcium color scale has been changed from the original one of movie 1 to match that of movie 2/Fig. 2. The movie compresses 20 min of experiment into 1 min of movie.
  38. Movie 2: T cell-APC interaction with blocked myosin motor proteins. The interaction of 5C.C7 T cells, loaded with 4.5-µm anti-ICAM-1 (YN1) beads, with peptide-loaded, ICAM-1-GFP-transfected CH27 B cell lymphoma in the presence of 2 mM BDM is shown. A bright-field series of images has been duplicated and is overlaid with false-color encoded fluorescence information. The top panel is overlaid with a false-color representation of the intracellular calcium concentration of the T cell, ranging from blue (low concentration) to red (high concentration). In the bottom panel, the ICAM-1-GFP fluorescence of the B cell lymphoma is overlaid in a false color scale from green (low fluorescence) to blue (high fluorescence) to allow the simultaneous investigation of an additional cellular parameter. The movie shows that in the presence of 2 µM BDM, although the calcium signal is elevated in a stable manner and ICAM-1-GFP accumulates at the T cell-B cell interface, this interface is narrow (as most easily seen by the tightly concentrated ICAM-1-GFP accumulation) and no bead movement is seen. The movie compresses 20 min of experiment into 1 min of movie.
  39. Three categories of bead movement were observed. Movement toward the interface was defined as bead movement at least one-fourth of a T cell circumference toward the interface (as shown in Fig. 1). Movement away from the interface was defined as bead movement at least one-fourth of a T cell circumference away from the interface, indicative of random bead movement. Beads located at the interface at the moment of T cell activation constituted <25% of all beads bound to T cells, consistent with the observation that migrating T cells move the beads toward their posterior. The only exception occurs after treatment with the PI 3-kinase inhibitor wortmannin, when 75% of the beads are already at the interface at the time of T cell activation, indicative of a lack of polarization. In this case, the beads are likely to initiate the cell-cell interaction by binding to ICAM-1 on both cells simultaneously. Beads that started at the interface stay there without exception. Beads that are scored "no movement" are those that move less than one-fourth of a T cell circumference in at least 5 min (Fig. 2).
  40. Blocking antibodies were used at 10 µg/ml. We used YN1 as anti-ICAM-1 (31), 16-10A1 (Pharmingen) as anti-B7-1, GL1 (Pharmingen) as anti-B7-2, HM48-1 (Pharmingen) as anti-CD48, 37.51 (Pharmingen) as anti-CD28, and MK2.7 as anti-VCAM (33). Wortmannin was used at 100 nM, Ni2+ at 5 mM, and both were added directly to the microscopy dish. T cells were preloaded with BAPTA in parallel with Fura-2 at 20 µM. The ICAM-1-GFP construct has been described (9); the B7-2-GFP construct is strictly analogous, with the GFP attached to the cytoplasmic tail. Stable transfectants were selected for GFP expression using flow cytometry, and single cells were cloned.
  41. Lack of T cell polarization is indicated by the fact that few activated cells had beads at the interface, by the lack of uropods and extended lamellipodia, and by the failure to migrate (16).
  42. BDM (Sigma) was added to the T cells at the indicated concentrations 5 min before the start of the microscopy experiment from a fresh 200 µM stock in PBS. Noxius toxin (Alomone Labs, Jerusalem, Israel) was added to the T cells at 100 nM, that is, a 100-fold excess over the apparent dissociation concentration of blocking peak potassium channels 5 min before the start of the microscopy experiment.
  43. The results were derived from a composite analysis of at least five experiments (nine on average) performed on at least three different days for each condition. As discussed in (34), composite data sets are shown because of the small number of cells per experiment that could be analyzed for some parameters. Positive controls were run on each day of the experiments to ensure uniformity.
  44. We thank M. D. Sjaastad, W. J. Nelson, R. S. Lewis, and D. A. Lauffenberger for helpful discussions. Supported by the Howard Hughes Medical Institute and the European Molecular Biology Organization (C.W.).
31 August 1998; accepted 10 November 1998


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   Abstract »    Full Text »    PDF »
Engagement of the CD4 Receptor Affects the Redistribution of Lck to the Immunological Synapse in Primary T Cells: Implications for T-Cell Activation during Human Immunodeficiency Virus Type 1 Infection.
A. M. Nyakeriga, C. J. Fichtenbaum, J. Goebel, S. A. Nicolaou, L. Conforti, and C. A. Chougnet (2009)
J. Virol. 83, 1193-1200
   Abstract »    Full Text »    PDF »
Expression of CD86 on Human Islet Endothelial Cells Facilitates T Cell Adhesion and Migration.
B. Lozanoska-Ochser, N. J. Klein, G. C. Huang, R. A. Alvarez, and M. Peakman (2008)
J. Immunol. 181, 6109-6116
   Abstract »    Full Text »    PDF »
Protein Kinase C{theta} Regulates Stability of the Peripheral Adhesion Ring Junction and Contributes to the Sensitivity of Target Cell Lysis by CTL.
A. M. Beal, N. Anikeeva, R. Varma, T. O. Cameron, P. J. Norris, M. L. Dustin, and Y. Sykulev (2008)
J. Immunol. 181, 4815-4824
   Abstract »    Full Text »    PDF »
Cholera Toxin B Accelerates Disease Progression in Lupus-Prone Mice by Promoting Lipid Raft Aggregation.
G.-M. Deng and G. C. Tsokos (2008)
J. Immunol. 181, 4019-4026
   Abstract »    Full Text »    PDF »
LFA-1 decreases the antigen dose for T cell activation in vivo.
Y. Wang, K. Shibuya, Y. Yamashita, J. Shirakawa, K. Shibata, H. Kai, T. Yokosuka, T. Saito, S.-i. Honda, S. Tahara-Hanaoka, et al. (2008)
Int. Immunol. 20, 1119-1127
   Abstract »    Full Text »    PDF »
CD44 mobilization in allogeneic dendritic cell-T cell immunological synapse plays a key role in T cell activation.
V. L. Hegde, N. P. Singh, P. S. Nagarkatti, and M. Nagarkatti (2008)
J. Leukoc. Biol. 84, 134-142
   Abstract »    Full Text »    PDF »
Rab35 and Its GAP EPI64C in T Cells Regulate Receptor Recycling and Immunological Synapse Formation.
G. Patino-Lopez, X. Dong, K. Ben-Aissa, K. M. Bernot, T. Itoh, M. Fukuda, M. J. Kruhlak, L. E. Samelson, and S. Shaw (2008)
J. Biol. Chem. 283, 18323-18330
   Abstract »    Full Text »    PDF »
SWAP-70 deficiency causes high-affinity plasma cell generation despite impaired germinal center formation.
L. Quemeneur, V. Angeli, M. Chopin, and R. Jessberger (2008)
Blood 111, 2714-2724
   Abstract »    Full Text »    PDF »
Mechanisms for segregating T cell receptor and adhesion molecules during immunological synapse formation in Jurkat T cells.
Y. Kaizuka, A. D. Douglass, R. Varma, M. L. Dustin, and R. D. Vale (2007)
PNAS 104, 20296-20301
   Abstract »    Full Text »    PDF »
Myosin IIA is required for cytolytic granule exocytosis in human NK cells.
M. M. Andzelm, X. Chen, K. Krzewski, J. S. Orange, and J. L. Strominger (2007)
J. Exp. Med. 204, 2285-2291
   Abstract »    Full Text »    PDF »
LFA-1-Mediated T Cell Costimulation through Increased Localization of TCR/Class II Complexes to the Central Supramolecular Activation Cluster and Exclusion of CD45 from the Immunological Synapse.
B. Graf, T. Bushnell, and J. Miller (2007)
J. Immunol. 179, 1616-1624
   Abstract »    Full Text »    PDF »
Forces and Bond Dynamics in Cell Adhesion.
E. A. Evans and D. A. Calderwood (2007)
Science 316, 1148-1153
   Abstract »    Full Text »    PDF »
CTLA-4 Differentially Regulates the Immunological Synapse in CD4 T Cell Subsets.
R. P. Jackman, F. Balamuth, and K. Bottomly (2007)
J. Immunol. 178, 5543-5551
   Abstract »    Full Text »    PDF »
Role of human neutrophil peptides in the initial interaction between lung epithelial cells and CD4+ lymphocytes.
R. Vaschetto, J. Grinstein, L. Del Sorbo, A. A. Khine, S. Voglis, E. Tullis, A. S. Slutsky, and H. Zhang (2007)
J. Leukoc. Biol. 81, 1022-1031
   Abstract »    Full Text »    PDF »
Association of CD38 with Nonmuscle Myosin Heavy Chain IIA and Lck Is Essential for the Internalization and Activation of CD38.
S.-Y. Rah, K.-H. Park, T.-S. Nam, S.-J. Kim, H. Kim, M.-J. Im, and U.-H. Kim (2007)
J. Biol. Chem. 282, 5653-5660
   Abstract »    Full Text »    PDF »
Interaction of the Wiskott-Aldrich syndrome protein with sorting nexin 9 is required for CD28 endocytosis and cosignaling in T cells.
K. Badour, M. K. H. McGavin, J. Zhang, S. Freeman, C. Vieira, D. Filipp, M. Julius, G. B. Mills, and K. A. Siminovitch (2007)
PNAS 104, 1593-1598
   Abstract »    Full Text »    PDF »
The actin cloud induced by LFA-1-mediated outside-in signals lowers the threshold for T-cell activation.
J.-i. Suzuki, S. Yamasaki, J. Wu, G. A. Koretzky, and T. Saito (2007)
Blood 109, 168-175
   Abstract »    Full Text »    PDF »
Specific Patterns of Cdc42 Activity Are Related to Distinct Elements of T Cell Polarization.
I. Tskvitaria-Fuller, A. Seth, N. Mistry, H. Gu, M. K. Rosen, and C. Wulfing (2006)
J. Immunol. 177, 1708-1720
   Abstract »    Full Text »    PDF »
Filamin A Is Required for T Cell Activation Mediated by Protein Kinase C-{theta}.
K. Hayashi and A. Altman (2006)
J. Immunol. 177, 1721-1728
   Abstract »    Full Text »    PDF »
p300/Cyclic AMP-Responsive Element Binding-Binding Protein Mediates Transcriptional Coactivation by the CD28 T Cell Costimulatory Receptor.
S. L. Nandiwada, W. Li, R. Zhang, and D. L. Mueller (2006)
J. Immunol. 177, 401-413
   Abstract »    Full Text »    PDF »
Transient accumulation of human mature thymocytes and regulatory T cells with CD28 superagonist in "human immune system" Rag2-/-{gamma}c-/- mice.
N. Legrand, T. Cupedo, A. U. van Lent, M. J. Ebeli, K. Weijer, T. Hanke, and H. Spits (2006)
Blood 108, 238-245
   Abstract »    Full Text »    PDF »
Role of Fyn in the Rearrangement of Tubulin Cytoskeleton Induced through TCR.
N. B. Martin-Cofreces, D. Sancho, E. Fernandez, M. Vicente-Manzanares, M. Gordon-Alonso, M. C. Montoya, F. Michel, O. Acuto, B. Alarcon, and F. Sanchez-Madrid (2006)
J. Immunol. 176, 4201-4207
   Abstract »    Full Text »    PDF »
Suicide gene therapy of graft-versus-host disease induced by central memory human T lymphocytes.
A. Bondanza, V. Valtolina, Z. Magnani, M. Ponzoni, K. Fleischhauer, M. Bonyhadi, C. Traversari, F. Sanvito, S. Toma, M. Radrizzani, et al. (2006)
Blood 107, 1828-1836
   Abstract »    Full Text »    PDF »
CD80 Cytoplasmic Domain Controls Localization of CD28, CTLA-4, and Protein Kinase C{theta} in the Immunological Synapse.
S.-Y. Tseng, M. Liu, and M. L. Dustin (2005)
J. Immunol. 175, 7829-7836
   Abstract »    Full Text »    PDF »
Activation of p21-Activated Kinase 2 by Human Immunodeficiency Virus Type 1 Nef Induces Merlin Phosphorylation.
B. L. Wei, V. K. Arora, A. Raney, L. S. Kuo, G.-H. Xiao, E. O'Neill, J. R. Testa, J. L. Foster, and J. V. Garcia (2005)
J. Virol. 79, 14976-14980
   Abstract »    Full Text »    PDF »
Identification of the Surfactant Protein A Receptor 210 as the Unconventional Myosin 18A.
C.-H. Yang, J. Szeliga, J. Jordan, S. Faske, Z. Sever-Chroneos, B. Dorsett, R. E. Christian, R. E. Settlage, J. Shabanowitz, D. F. Hunt, et al. (2005)
J. Biol. Chem. 280, 34447-34457
   Abstract »    Full Text »    PDF »
Lack of ICAM-1 on APCs during T Cell Priming Leads to Poor Generation of Central Memory Cells.
N. Parameswaran, R. Suresh, V. Bal, S. Rath, and A. George (2005)
J. Immunol. 175, 2201-2211
   Abstract »    Full Text »    PDF »
Transient Loss of MHC Class I Tetramer Binding after CD8+ T Cell Activation Reflects Altered T Cell Effector Function.
D. R. Drake III, R. M. Ream, C. W. Lawrence, and T. J. Braciale (2005)
J. Immunol. 175, 1507-1515
   Abstract »    Full Text »    PDF »
A Theoretical Framework for Quantitative Analysis of the Molecular Basis of Costimulation.
A. Jansson, E. Barnes, P. Klenerman, M. Harlen, P. Sorensen, S. J. Davis, and P. Nilsson (2005)
J. Immunol. 175, 1575-1585
   Abstract »    Full Text »    PDF »
Orally Tolerized T Cells Can Form Conjugates with APCs but Are Defective in Immunological Synapse Formation.
W. Ise, K. Nakamura, N. Shimizu, H. Goto, K. Fujimoto, S. Kaminogawa, and S. Hachimura (2005)
J. Immunol. 175, 829-838
   Abstract »    Full Text »    PDF »
The CD3{epsilon} Proline-Rich Sequence, and Its Interaction with Nck, Is Not Required for T Cell Development and Function.
A. L. Szymczak, C. J. Workman, D. Gil, S. Dilioglou, K. M. Vignali, E. Palmer, and D. A. A. Vignali (2005)
J. Immunol. 175, 270-275
   Abstract »    Full Text »    PDF »
Expression of Class II Major Histocompatibility Complex Molecules on Thyrocytes Does Not Cause Spontaneous Thyroiditis but Mildly Increases Its Severity after Immunization.
H. Kimura, M. Kimura, S.-C. Tzou, Y.-C. Chen, K. Suzuki, N. R. Rose, and P. Caturegli (2005)
Endocrinology 146, 1154-1162
   Abstract »    Full Text »    PDF »
T cell receptor (TCR) clustering in the immunological synapse integrates TCR and costimulatory signaling in selected T cells.
B. Purtic, L. A. Pitcher, N. S. C. van Oers, and C. Wulfing (2005)
PNAS 102, 2904-2909
   Abstract »    Full Text »    PDF »
Differential Control of CD28-Regulated In Vivo Immunity by the E3 Ligase Cbl-b.
C. M. Krawczyk, R. G. Jones, A. Atfield, K. Bachmaier, S. Arya, B. Odermatt, P. S. Ohashi, and J. M. Penninger (2005)
J. Immunol. 174, 1472-1478
   Abstract »    Full Text »    PDF »
CD45 Signals outside of Lipid Rafts to Promote ERK Activation, Synaptic Raft Clustering, and IL-2 Production.
M. Zhang, M. Moran, J. Round, T. A. Low, V. P. Patel, T. Tomassian, J. D. Hernandez, and M. C. Miceli (2005)
J. Immunol. 174, 1479-1490
   Abstract »    Full Text »    PDF »
Regulated Recruitment of MHC Class II and Costimulatory Molecules to Lipid Rafts in Dendritic Cells.
C. O. Meyer zum Bueschenfelde, J. Unternaehrer, I. Mellman, and K. Bottomly (2004)
J. Immunol. 173, 6119-6124
   Abstract »    Full Text »    PDF »
Differential Regulation of Th1/Th2 Cytokine Responses by Placental Protein 14.
G. Mishan-Eisenberg, Z. Borovsky, M. C. Weber, R. Gazit, M. L. Tykocinski, and J. Rachmilewitz (2004)
J. Immunol. 173, 5524-5530
   Abstract »    Full Text »    PDF »
The Actin Cytoskeleton Controls the Efficiency of Killer Ig-Like Receptor Accumulation at Inhibitory NK Cell Immune Synapses.
L. J. Standeven, L. M. Carlin, P. Borszcz, D. M. Davis, and D. N. Burshtyn (2004)
J. Immunol. 173, 5617-5625
   Abstract »    Full Text »    PDF »
Chronic Immune Activation Associated with Chronic Helminthic and Human Immunodeficiency Virus Infections: Role of Hyporesponsiveness and Anergy.
G. Borkow and Z. Bentwich (2004)
Clin. Microbiol. Rev. 17, 1012-1030
   Abstract »    Full Text »    PDF »
T cell receptor antagonism interferes with MHC clustering and integrin patterning during immunological synapse formation.
C. Sumen, M. L. Dustin, and M. M. Davis (2004)
J. Cell Biol. 166, 579-590
   Abstract »    Full Text »    PDF »
Tec Kinase Migrates to the T Cell-APC Interface Independently of Its Pleckstrin Homology Domain.
F. Garcon, G. Bismuth, D. Isnardon, D. Olive, and J. A. Nunes (2004)
J. Immunol. 173, 770-775
   Abstract »    Full Text »    PDF »
Formation of a central supramolecular activation cluster is not required for activation of naive CD8+ T cells.
J. P. O'Keefe, K. Blaine, M.-L. Alegre, and T. F. Gajewski (2004)
PNAS 101, 9351-9356
   Abstract »    Full Text »    PDF »
Extensive Replicative Capacity of Human Central Memory T Cells.
M. V. Maus, B. Kovacs, W. W. Kwok, G. T. Nepom, K. Schlienger, J. L. Riley, D. Allman, T. H. Finkel, and C. H. June (2004)
J. Immunol. 172, 6675-6683
   Abstract »    Full Text »    PDF »
CD28 Signals in the Immature Immunological Synapse.
P. G. Andres, K. C. Howland, D. Dresnek, S. Edmondson, A. K. Abbas, and M. F. Krummel (2004)
J. Immunol. 172, 5880-5886
   Abstract »    Full Text »    PDF »
CD28 delivers a unique signal leading to the selective recruitment of RelA and p52 NF-{kappa}B subunits on IL-8 and Bcl-xL gene promoters.
B. Marinari, A. Costanzo, V. Marzano, E. Piccolella, and L. Tuosto (2004)
PNAS 101, 6098-6103
   Abstract »    Full Text »    PDF »
Recruitment of the Actin-binding Protein HIP-55 to the Immunological Synapse Regulates T Cell Receptor Signaling and Endocytosis.
S. Le Bras, I. Foucault, A. Foussat, C. Brignone, O. Acuto, and M. Deckert (2004)
J. Biol. Chem. 279, 15550-15560
   Abstract »    Full Text »    PDF »
Induction of various immune modulatory molecules in CD34+ hematopoietic cells.
O. Umland, H. Heine, M. Miehe, K. Marienfeld, K. H. Staubach, and A. J. Ulmer (2004)
J. Leukoc. Biol. 75, 671-679
   Abstract »    Full Text »    PDF »
PKC{theta} Signals Activation versus Tolerance In Vivo.
N. N. Berg-Brown, M. A. Gronski, R. G. Jones, A. R. Elford, E. K. Deenick, B. Odermatt, D. R. Littman, and P. S. Ohashi (2004)
J. Exp. Med. 199, 743-752
   Abstract »    Full Text »    PDF »
Cofilin peptide homologs interfere with immunological synapse formation and T cell activation.
S. M. Eibert, K.-H. Lee, R. Pipkorn, U. Sester, G. H. Wabnitz, T. Giese, S. C. Meuer, and Y. Samstag (2004)
PNAS 101, 1957-1962
   Abstract »    Full Text »    PDF »
Actin Cytoskeleton Regulates Calcium Dynamics and NFAT Nuclear Duration.
F. V. Rivas, J. P. O'Keefe, M.-L. Alegre, and T. F. Gajewski (2004)
Mol. Cell. Biol. 24, 1628-1639
   Abstract »    Full Text »    PDF »
Association of CD26 with CD45RA outside lipid rafts attenuates cord blood T-cell activation.
S. Kobayashi, K. Ohnuma, M. Uchiyama, K. Iino, S. Iwata, N. H. Dang, and C. Morimoto (2004)
Blood 103, 1002-1010
   Abstract »    Full Text »    PDF »
Fyn and PTP-PEST-mediated Regulation of Wiskott-Aldrich Syndrome Protein (WASp) Tyrosine Phosphorylation Is Required for Coupling T Cell Antigen Receptor Engagement to WASp Effector Function and T Cell Activation.
K. Badour, J. Zhang, F. Shi, Y. Leng, M. Collins, and K. A. Siminovitch (2004)
J. Exp. Med. 199, 99-112
   Abstract »    Full Text »    PDF »
CD40-Induced Aggregation of MHC Class II and CD80 on the Cell Surface Leads to an Early Enhancement in Antigen Presentation.
A. Clatza, L. C. Bonifaz, D. A. A. Vignali, and J. Moreno (2003)
J. Immunol. 171, 6478-6487
   Abstract »    Full Text »    PDF »
Leishmania-Induced Inhibition of Macrophage Antigen Presentation Analyzed at the Single-Cell Level.
C. L. Meier, M. Svensson, and P. M. Kaye (2003)
J. Immunol. 171, 6706-6713
   Abstract »    Full Text »    PDF »
The Immunological Synapse Balances T Cell Receptor Signaling and Degradation.
K.-H. Lee, A. R. Dinner, C. Tu, G. Campi, S. Raychaudhuri, R. Varma, T. N. Sims, W. R. Burack, H. Wu, J. Wang, et al. (2003)
Science 302, 1218-1222
   Abstract »    Full Text »    PDF »
Cutting Edge: Dendritic Cell Actin Cytoskeletal Polarization during Immunological Synapse Formation Is Highly Antigen-Dependent.
M. M. Al-Alwan, R. S. Liwski, S. M. M. Haeryfar, W. H. Baldridge, D. W. Hoskin, G. Rowden, and K. A. West (2003)
J. Immunol. 171, 4479-4483
   Abstract »    Full Text »    PDF »
Modeling TCR Signaling Complex Formation in Positive Selection.
K. J. Hare, J. Pongracz, E. J. Jenkinson, and G. Anderson (2003)
J. Immunol. 171, 2825-2831
   Abstract »    Full Text »    PDF »
TCR Comodulation of Nonengaged TCR Takes Place by a Protein Kinase C and CD3{gamma} Di-Leucine-Based Motif-Dependent Mechanism.
C. M. Bonefeld, A. B. Rasmussen, J. P. H. Lauritsen, M. von Essen, N. Odum, P. S. Andersen, and C. Geisler (2003)
J. Immunol. 171, 3003-3009
   Abstract »    Full Text »    PDF »
Regulation of Sustained Actin Dynamics by the TCR and Costimulation as a Mechanism of Receptor Localization.
I. Tskvitaria-Fuller, A. L. Rozelle, H. L. Yin, and C. Wulfing (2003)
J. Immunol. 171, 2287-2295
   Abstract »    Full Text »    PDF »
Incomplete Activation of CD4 T Cells by Antigen-Presenting Transitional Immature B Cells: Implications for Peripheral B and T Cell Responsiveness.
J. B. Chung, A. D. Wells, S. Adler, A. Jacob, L. A. Turka, and J. G. Monroe (2003)
J. Immunol. 171, 1758-1767
   Abstract »    Full Text »    PDF »
LFA-1-induced T cell migration on ICAM-1 involves regulation of MLCK-mediated attachment and ROCK-dependent detachment.
A. Smith, M. Bracke, B. Leitinger, J. C. Porter, and N. Hogg (2003)
J. Cell Sci. 116, 3123-3133
   Abstract »    Full Text »    PDF »
Linker for Activation of T Cells, {zeta}-Associated Protein-70, and Src Homology 2 Domain-Containing Leukocyte Protein-76 are Required for TCR-Induced Microtubule-Organizing Center Polarization.
M. R. Kuhne, J. Lin, D. Yablonski, M. N. Mollenauer, L. I. R. Ehrlich, J. Huppa, M. M. Davis, and A. Weiss (2003)
J. Immunol. 171, 860-866
   Abstract »    Full Text »    PDF »
Composition of MHC class II-enriched lipid microdomains is modified during maturation of primary dendritic cells.
N. Setterblad, C. Roucard, C. Bocaccio, J.-P. Abastado, D. Charron, and N. Mooney (2003)
J. Leukoc. Biol. 74, 40-48
   Abstract »    Full Text »    PDF »
T Cell Glycolipid-Enriched Membrane Domains Are Constitutively Assembled as Membrane Patches That Translocate to Immune Synapses.
S. Jordan and W. Rodgers (2003)
J. Immunol. 171, 78-87
   Abstract »    Full Text »    PDF »
Topological Requirements and Signaling Properties of T Cell-activating, Anti-CD28 Antibody Superagonists.
F. Luhder, Y. Huang, K. M. Dennehy, C. Guntermann, I. Muller, E. Winkler, T. Kerkau, S. Ikemizu, S. J. Davis, T. Hanke, et al. (2003)
J. Exp. Med. 197, 955-966
   Abstract »    Full Text »    PDF »
Low T cell receptor expression and thermal fluctuations contribute to formation of dynamic multifocal synapses in thymocytes.
S.-J. E. Lee, Y. Hori, and A. K. Chakraborty (2003)
PNAS 100, 4383-4388
   Abstract »    Full Text »    PDF »
Coxiella burnetii Avoids Macrophage Phagocytosis by Interfering with Spatial Distribution of Complement Receptor 3.
C. Capo, A. Moynault, Y. Collette, D. Olive, E. J. Brown, D. Raoult, and J.-L. Mege (2003)
J. Immunol. 170, 4217-4225
   Abstract »    Full Text »    PDF »
The Size of the Synaptic Cleft and Distinct Distributions of Filamentous Actin, Ezrin, CD43, and CD45 at Activating and Inhibitory Human NK Cell Immune Synapses.
F. E. McCann, B. Vanherberghen, K. Eleme, L. M. Carlin, R. J. Newsam, D. Goulding, and D. M. Davis (2003)
J. Immunol. 170, 2862-2870
   Abstract »    Full Text »    PDF »
Vav-1 and the IKK{alpha} Subunit of I{kappa}B Kinase Functionally Associate to Induce NF-{kappa}B Activation in Response to CD28 Engagement.
E. Piccolella, F. Spadaro, C. Ramoni, B. Marinari, A. Costanzo, M. Levrero, L. Thomson, R. T. Abraham, and L. Tuosto (2003)
J. Immunol. 170, 2895-2903
   Abstract »    Full Text »    PDF »
The EphB6 Receptor Inhibits JNK Activation in T Lymphocytes and Modulates T Cell Receptor-mediated Responses.
A. Freywald, N. Sharfe, C. Rashotte, T. Grunberger, and C. M. Roifman (2003)
J. Biol. Chem. 278, 10150-10156
   Abstract »    Full Text »    PDF »
Involvement of CD70 and CD80 intracytoplasmic domains in the co-stimulatory signal required to provide an antitumor immune response.
V. Douin-Echinard, J.-M. Peron, V. Lauwers-Cances, G. Favre, and B. Couderc (2003)
Int. Immunol. 15, 359-372
   Abstract »    Full Text »    PDF »
T Cell Receptor Can Be Recruited to a Subset of Plasma Membrane Rafts, Independently of Cell Signaling and Attendantly to Raft Clustering.
E. Giurisato, D. P. McIntosh, M. Tassi, A. Gamberucci, and A. Benedetti (2003)
J. Biol. Chem. 278, 6771-6778
   Abstract »    Full Text »    PDF »
Naturally Occurring Human IgM Antibody That Binds B7-DC and Potentiates T Cell Stimulation by Dendritic Cells.
S. Radhakrishnan, L. T. Nguyen, B. Ciric, D. R. Ure, B. Zhou, K. Tamada, H. Dong, S.-Y. Tseng, T. Shin, D. M. Pardoll, et al. (2003)
J. Immunol. 170, 1830-1838
   Abstract »    Full Text »    PDF »
Regulation of Lymphocyte Apoptosis by Interferon Regulatory Factor 4 (IRF-4).
J. C. Fanzo, C.-M. Hu, S. Y. Jang, and A. B. Pernis (2003)
J. Exp. Med. 197, 303-314
   Abstract »    Full Text »    PDF »
MHC Class II-Peptide Complexes and APC Lipid Rafts Accumulate at the Immunological Synapse.
E. M. Hiltbold, N. J. Poloso, and P. A. Roche (2003)
J. Immunol. 170, 1329-1338
   Abstract »    Full Text »    PDF »
Actin cytoskeletal dynamics in T lymphocyte activation and migration.
Y. Samstag, S. M. Eibert, M. Klemke, and G. H. Wabnitz (2003)
J. Leukoc. Biol. 73, 30-48
   Abstract »    Full Text »    PDF »
Live-Cell Dynamics and the Role of Costimulation in Immunological Synapse Formation.
S. A. Wetzel, T. W. McKeithan, and D. C. Parker (2002)
J. Immunol. 169, 6092-6101
   Abstract »    Full Text »    PDF »
Cutting Edge: Association of the Motor Protein Nonmuscle Myosin Heavy Chain-IIA with the C Terminus of the Chemokine Receptor CXCR4 in T Lymphocytes.
M. Rey, M. Vicente-Manzanares, F. Viedma, M. Yanez-Mo, A. Urzainqui, O. Barreiro, J. Vazquez, and F. Sanchez-Madrid (2002)
J. Immunol. 169, 5410-5414
   Abstract »    Full Text »    PDF »
Quantifying signaling-induced reorientation of T cell receptors during immunological synapse formation.
W. C. Moss, D. J. Irvine, M. M. Davis, and M. F. Krummel (2002)
PNAS 99, 15024-15029
   Abstract »    Full Text »    PDF »
Neural and Immunological Synaptic Relations.
M. L. Dustin and D. R. Colman (2002)
Science 298, 785-789
   Abstract »    Full Text »    PDF »
T cell receptor ligation induces the formation of dynamically regulated signaling assemblies.
S. C. Bunnell, D. I. Hong, J. R. Kardon, T. Yamazaki, C. J. McGlade, V. A. Barr, and L. E. Samelson (2002)
J. Cell Biol. 158, 1263-1275
   Abstract »    Full Text »    PDF »
Engagement of the inhibitory receptor CD158a interrupts TCR signaling, preventing dynamic membrane reorganization in CTL/tumor cell interaction.
N. Guerra, F. Michel, A. Gati, C. Gaudin, Z. Mishal, B. Escudier, O. Acuto, S. Chouaib, and A. Caignard (2002)
Blood 100, 2874-2881
   Abstract »    Full Text »    PDF »
Cutting Edge: Quantitative Imaging of Raft Accumulation in the Immunological Synapse.
W. R. Burack, K.-H. Lee, A. D. Holdorf, M. L. Dustin, and A. S. Shaw (2002)
J. Immunol. 169, 2837-2841
   Abstract »    Full Text »    PDF »
Genomic expression programs and the integration of the CD28 costimulatory signal in T cell activation.
M. Diehn, A. A. Alizadeh, O. J. Rando, C. L. Liu, K. Stankunas, D. Botstein, G. R. Crabtree, and P. O. Brown (2002)
PNAS 99, 11796-11801
   Abstract »    Full Text »    PDF »
Essential Role of NF-{kappa}B-Inducing Kinase in T Cell Activation Through the TCR/CD3 Pathway.
M. Matsumoto, T. Yamada, S. K. Yoshinaga, T. Boone, T. Horan, S. Fujita, Y. Li, and T. Mitani (2002)
J. Immunol. 169, 1151-1158
   Abstract »    Full Text »    PDF »
TCR Engagement Induces Proline-Rich Tyrosine Kinase-2 (Pyk2) Translocation to the T Cell-APC Interface Independently of Pyk2 Activity and in an Immunoreceptor Tyrosine-Based Activation Motif-Mediated Fashion.
D. Sancho, M. C. Montoya, A. Monjas, M. Gordon-Alonso, T. Katagiri, D. Gil, R. Tejedor, B. Alarcon, and F. Sanchez-Madrid (2002)
J. Immunol. 169, 292-300
   Abstract »    Full Text »    PDF »
Polar Redistribution of the Sialoglycoprotein CD43: Implications for T Cell Function.
N. D. L. Savage, S. L. Kimzey, S. K. Bromley, K. G. Johnson, M. L. Dustin, and J. M. Green (2002)
J. Immunol. 168, 3740-3746
   Abstract »    Full Text »    PDF »
Intercellular transfer of antigen-presenting cell determinants onto T cells: molecular mechanisms and biological significance.
D. HUDRISIER and P. BONGRAND (2002)
FASEB J 16, 477-486
   Abstract »    Full Text »    PDF »
Cutting Edge: Differential Segregation of the Src Homology 2-Containing Protein Tyrosine Phosphatase-1 Within the Early NK Cell Immune Synapse Distinguishes Noncytolytic from Cytolytic Interactions.
Y. M. Vyas, H. Maniar, and B. Dupont (2002)
J. Immunol. 168, 3150-3154
   Abstract »    Full Text »    PDF »
CD43 polarization in unprimed T cells can be dissociated from raft coalescence by inhibition of HMG CoA reductase.
E. Gubina, T. Chen, L. Zhang, E. F. Lizzio, and S. Kozlowski (2002)
Blood 99, 2518-2525
   Abstract »    Full Text »    PDF »
Focal Localization of Placental Protein 14 Toward Sites of TCR Engagement.
J. Rachmilewitz, Z. Borovsky, G. Mishan-Eisenberg, E. Yaniv, G. J. Riely, and M. L. Tykocinski (2002)
J. Immunol. 168, 2745-2750
   Abstract »    Full Text »    PDF »
A Novel Serine-rich Motif in the Intercellular Adhesion Molecule 3 Is Critical for Its Ezrin/Radixin/Moesin-directed Subcellular Targeting.
J. M. Serrador, M. Vicente-Manzanares, J. Calvo, O. Barreiro, M. C. Montoya, R. Schwartz-Albiez, H. Furthmayr, F. Lozano, and F. Sanchez-Madrid (2002)
J. Biol. Chem. 277, 10400-10409
   Abstract »    Full Text »    PDF »
The role of lipid rafts in signalling and membrane trafficking in T lymphocytes.
M. A. Alonso and J. Millan (2002)
J. Cell Sci. 114, 3957-3965
   Abstract »    Full Text »    PDF »
How and Why Does the Immunological Synapse Form? Physical Chemistry Meets Cell Biology.
A. K. Chakraborty (2002)
Sci. STKE 2002, pe10
   Abstract »    Full Text »    PDF »
Rho GTPases link cytoskeletal rearrangements and activation processes induced via the tetraspanin CD82 in T lymphocytes.
A. Delaguillaumie, C. Lagaudriere-Gesbert, M. R. Popoff, and H. Conjeaud (2002)
J. Cell Sci. 115, 433-443
   Abstract »    Full Text »    PDF »
Cutting Edge: Negative Regulation of Immune Synapse Formation by Anchoring Lipid Raft to Cytoskeleton Through Cbp-EBP50-ERM Assembly.
K. Itoh, M. Sakakibara, S. Yamasaki, A. Takeuchi, H. Arase, M. Miyazaki, N. Nakajima, M. Okada, and T. Saito (2002)
J. Immunol. 168, 541-544
   Abstract »    Full Text »    PDF »


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Science. ISSN 0036-8075 (print), 1095-9203 (online)