Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 3 May 1991:
Vol. 252. no. 5006, pp. 712 - 715
DOI: 10.1126/science.1708917
Prev | Table of Contents | Next

Articles

Science, Vol 252, Issue 5006, 712-715
Copyright © 1991 by American Association for the Advancement of Science

articles

Presence of an SH2 domain in the actin-binding protein tensin

S Davis, ML Lu, SH Lo, S Lin, JA Butler, BJ Druker, TM Roberts, Q An, and LB Chen

Division of Cellular and Molecular Biology, Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.

The molecular cloning of the complementary DNA coding for a 90-kilodalton fragment of tensin, an actin-binding component of focal contacts and other submembraneous cytoskeletal structures, is reported. The derived amino acid sequence revealed the presence of a Src homology 2 (SH2) domain. This domain is shared by a number of signal transduction proteins including nonreceptor tyrosine kinases such as Abl, Fps, Src, and Src family members, the transforming protein Crk, phospholipase C-gamma 1, PI-3 (phosphatidylinositol) kinase, and guanosine triphosphatase-activating protein (GAP). Like the SH2 domain found in Src, Crk, and Abl, the SH2 domain of tensin bound specifically to a number of phosphotyrosine-containing proteins from v-src-transformed cells. Tensin was also found to be phosphorylated on tyrosine residues. These findings suggest that by possessing both actin-binding and phosphotyrosine-binding activities and being itself a target for tyrosine kinases, tensin may link signal transduction pathways with the cytoskeleton.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
An arrestin-dependent multi-kinase signaling complex mediates MIP-1{beta}/CCL4 signaling and chemotaxis of primary human macrophages.
R. Cheung, M. Malik, V. Ravyn, B. Tomkowicz, A. Ptasznik, and R. G. Collman (2009)
J. Leukoc. Biol. 86, 833-845
   Abstract »    Full Text »    PDF »
Association of the Tensin N-terminal Protein-tyrosine Phosphatase Domain with the {alpha} Isoform of Protein Phosphatase-1 in Focal Adhesions.
M. Eto, J. Kirkbride, E. Elliott, S. H. Lo, and D. L. Brautigan (2007)
J. Biol. Chem. 282, 17806-17815
   Abstract »    Full Text »    PDF »
The phosphotyrosine-independent interaction of DLC-1 and the SH2 domain of cten regulates focal adhesion localization and growth suppression activity of DLC-1.
Y.-C. Liao, L. Si, R. W. deVere White, and S. H. Lo (2007)
J. Cell Biol. 176, 43-49
   Abstract »    Full Text »    PDF »
Tensin Is Expressed in Glomerular Mesangial Cells and Is Related to Their Attachment to Surrounding Extracellular Matrix.
H. Takahara, I. Shirato, K. Asanuma, M. Yamashita, Y. Takeda, and Y. Tomino (2004)
J. Histochem. Cytochem. 52, 683-692
   Abstract »    Full Text »    PDF »
Epidermal Growth Factor Modulates Tyrosine Phosphorylation of a Novel Tensin Family Member, Tensin3.
Y. Cui, Y.-C. Liao, and S. H. Lo (2004)
Mol. Cancer Res. 2, 225-232
   Abstract »    Full Text »    PDF »
blistery encodes Drosophila tensin protein and interacts with integrin and the JNK signaling pathway during wing development.
S. B. Lee, K. S. Cho, E. Kim, and J. Chung (2003)
Development 130, 4001-4010
   Abstract »    Full Text »    PDF »
Cten, a COOH-Terminal Tensin-like Protein with Prostate Restricted Expression, Is Down-Regulated in Prostate Cancer.
S. H. Lo and T. B. Lo (2002)
Cancer Res. 62, 4217-4221
   Abstract »    Full Text »    PDF »
Indomethacin Delays Gastric Restitution: Association with the Inhibition of Focal Adhesion Kinase and Tensin Phosphorylation and Reduced Actin Stress Fibers.
I. L. Szabo, R. Pai, M. K. Jones, G. R. Ehring, H. Kawanaka, and A. S. Tarnawski (2002)
Experimental Biology and Medicine 227, 412-424
   Abstract »    Full Text »    PDF »
Molecular Cloning and Characterization of Human Trabeculin-alpha , a Giant Protein Defining a New Family of Actin-binding Proteins.
Y. Sun, J. Zhang, S.-K. Kraeft, D. Auclair, M.-S. Chang, Y. Liu, R. Sutherland, R. Salgia, J. D. Griffin, L. H. Ferland, et al. (1999)
J. Biol. Chem. 274, 33522-33530
   Abstract »    Full Text »    PDF »
PTEN Gene and Integrin Signaling in Cancer.
M. Tamura, J. Gu, H. Tran, and K. M. Yamada (1999)
J Natl Cancer Inst 91, 1820-1828
   Abstract »    Full Text »    PDF »
Independent SH2-binding Sites Mediate Interaction of Dok-related Protein with RasGTPase-activating Protein and Nck.
P. Lock, F. Casagranda, and A. R. Dunn (1999)
J. Biol. Chem. 274, 22775-22784
   Abstract »    Full Text »    PDF »
A Novel Human Cytomegalovirus Glycoprotein, gpUS9, Which Promotes Cell-to-Cell Spread in Polarized Epithelial Cells, Colocalizes with the Cytoskeletal Proteins E-Cadherin and F-Actin.
E. Maidji, S. Tugizov, G. Abenes, T. Jones, and L. Pereira (1998)
J. Virol. 72, 5717-5727
   Abstract »    Full Text »    PDF »
Signal Transduction and Signal Modulation by Cell Adhesion Receptors: The Role of Integrins, Cadherins, Immunoglobulin-Cell Adhesion Molecules, and Selectins.
A. E. Aplin, A. Howe, S. K. Alahari, and R. L. Juliano (1998)
Pharmacol. Rev. 50, 197-264
   Abstract »    Full Text »    PDF »
SMART, a simple modular architecture research tool: Identification of signaling domains.
J. Schultz, F. Milpetz, P. Bork, and C. P. Ponting (1998)
PNAS 95, 5857-5864
   Abstract »    Full Text »    PDF »
Role of Ion Channels and Exchangers in Mechanical Stretch–Induced Cardiomyocyte Hypertrophy.
T. Yamazaki, I. Komuro, S. Kudoh, Y. Zou, R. Nagai, R. Aikawa, H. Uozumi, and Y. Yazaki (1998)
Circ. Res. 82, 430-437
   Abstract »    Full Text »    PDF »
Progressive Kidney Degeneration in Mice Lacking Tensin.
S. H. Lo, Q.-C. Yu, L. Degenstein, L. B. Chen, and E. Fuchs (1997)
J. Cell Biol. 136, 1349-1361
   Abstract »    Full Text »    PDF »
Platelet-derived Growth Factor-induced Formation of Tensin and Phosphoinositide 3-Kinase Complexes.
K. R. Auger, Z. Songyang, S. H. Lo, T. M. Roberts, and L. B. Chen (1996)
J. Biol. Chem. 271, 23452-23457
   Abstract »    Full Text »    PDF »
p80/85 Cortactin Associates with the Src SH2 Domain and Colocalizes with v-Src in Transformed Cells.
H. Okamura and M. D. Resh (1995)
J. Biol. Chem. 270, 26613-26618
   Abstract »    Full Text »    PDF »
Molecular Cloning Of Human Paxillin, a Focal Adhesion Protein Phosphorylated by P210[IMAGE].
R. Salgia, J.-L. Li, S. H. Lo, B. Brunkhorst, G. S. Kansas, E. S. Sobhany, Y. Sun, E. Pisick, M. Hallek, T. Ernst, et al. (1995)
J. Biol. Chem. 270, 5039-5047
   Abstract »    Full Text »    PDF »
Cell Spreading in Colo 201 by Staurosporin Is alpha3beta1 Integrin-mediated with Tyrosine Phosphorylation of Src and Tensin.
M. Yoshimura, A. Nishikawa, T. Nishiura, Y. Ihara, Y. Kanayama, Y. Matsuzawa, and N. Taniguchi (1995)
J. Biol. Chem. 270, 2298-2304
   Abstract »    Full Text »    PDF »
The RhoA-dependent assembly of focal adhesions in Swiss 3T3 cells is associated with increased tyrosine phosphorylation and the recruitment of both pp125FAK and protein kinase C-delta to focal adhesions.
S. T. Barry and D. R. Critchley (1994)
J. Cell Sci. 107, 2033-2045
   Abstract »    PDF »
Talin, vinculin and DRP (utrophin) concentrations are increased at mdx myotendinous junctions following onset of necrosis.
D. Law, D. Allen, and J. Tidball (1994)
J. Cell Sci. 107, 1477-1483
   Abstract »    PDF »
Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak-binding region.
C. Turner and J. Miller (1994)
J. Cell Sci. 107, 1583-1591
   Abstract »    PDF »
On the crawling of animal cells.
T. Stossel (1993)
Science 260, 1086-1094
   Abstract »    PDF »
Alpha 7 beta 1 integrin is a component of the myotendinous junction on skeletal muscle.
Z. Bao, M Lakonishok, S Kaufman, and A. Horwitz (1993)
J. Cell Sci. 106, 579-589
   Abstract »    PDF »
Cytoskeleton--plasma membrane interactions.
E. Luna and A. Hitt (1992)
Science 258, 955-964
   Abstract »    PDF »
Signaling between the Extracellular Matrix and the Cytoskeleton: Tyrosine Phosphorylation and Focal Adhesion Assembly.
L.H. Romer, K. Burridge, and C.E. Turner (1992)
Cold Spring Harb Symp Quant Biol 57, 193-202
   Abstract »    PDF »
SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins.
C. Koch, D Anderson, M. Moran, C Ellis, and T Pawson (1991)
Science 252, 668-674
   Abstract »    PDF »
Tensin1 and a previously undocumented family member, tensin2, positively regulate cell migration.
H. Chen, I. C. Duncan, H. Bozorgchami, and S. H. Lo (2002)
PNAS 99, 733-738
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

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