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Science 21 January 1994:
Vol. 263. no. 5145, pp. 387 - 390
DOI: 10.1126/science.8278814
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Articles

Science, Vol 263, Issue 5145, 387-390
Copyright © 1994 by American Association for the Advancement of Science

articles

Retention of unassembled components of integral membrane proteins by calnexin

S Rajagopalan, Y Xu, and MB Brenner

Department of Rheumatology and Immunology, Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115.

Quality control mechanisms prevent the cell surface expression of incompletely assembled multisubunit receptors such as the T cell receptor (TCR). The molecular chaperone function of calnexin (IP90, p88), a 90-kilodalton protein that resides in the endoplasmic reticulum (ER), in the retention of representative chains of the TCR-CD3 complex in the ER was tested. Truncation mutants of calnexin, when transiently expressed in COS cells, were exported from the ER and either accumulated in the Golgi or progressed to the cell surface. CD3 epsilon chains cotransfected with the forms of calnexin that were not retained in the ER exited the ER and colocalized with calnexin. Since engineered calnexin determined the intracellular localization of the proteins associated with it, it is concluded that calnexin interacts with incompletely assembled TCR components and retains them in the ER.


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   Abstract »    Full Text »    PDF »
The Related Molecular Chaperones Calnexin and Calreticulin Differentially Associate with Nascent T Cell Antigen Receptor Proteins within the Endoplasmic Reticulum.
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   Abstract »    Full Text »    PDF »
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S. Roy, A. Sun, and C. Redman (1996)
J. Biol. Chem. 271, 24544-24550
   Abstract »    Full Text »    PDF »
Involvement of the Chaperone Protein Calnexin and the Acetylcholine Receptor beta -Subunit in the Assembly and Cell Surface Expression of the Receptor.
S. H. Keller, J. Lindstrom, and P. Taylor (1996)
J. Biol. Chem. 271, 22871-22877
   Abstract »    Full Text »    PDF »
Interactions between Microsomal Triglyceride Transfer Protein and Apolipoprotein B within the Endoplasmic Reticulum in a Heterologous Expression System.
S. B. Patel and S. M. Grundy (1996)
J. Biol. Chem. 271, 18686-18694
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Glycan-dependent and -independent Association of Vesicular Stomatitis Virus G Protein with Calnexin.
K. S. Cannon, D. N. Hebert, and A. Helenius (1996)
J. Biol. Chem. 271, 14280-14284
   Abstract »    Full Text »    PDF »
The Glut 1Glucose Transporter Interacts with Calnexin and Calreticulin.
J. D. Oliver, R. C. Hresko, M. Mueckler, and S. High (1996)
J. Biol. Chem. 271, 13691-13696
   Abstract »    Full Text »    PDF »
Calnexin Associates Exclusively with Individual CD3[IMAGE] and T Cell Antigen Receptor (TCR) alpha Proteins Containing Incompletely Trimmed Glycans That Are Not Assembled into Multisubunit TCR Complexes.
J. E. M. van Leeuwen and K. P. Kearse (1996)
J. Biol. Chem. 271, 9660-9665
   Abstract »    Full Text »    PDF »
Unique Expression of Major Histocompatibility Complex Class I Proteins in the Absence of Glucose Trimming and Calnexin Association.
J. P. Balow, J. D. Weissman, and K. P. Kearse (1995)
J. Biol. Chem. 270, 29025-29029
   Abstract »    Full Text »    PDF »
Calnexin Fails to Associate with Substrate Proteins in Glucosidase-deficient Cell Lines.
A. Ora and A. Helenius (1995)
J. Biol. Chem. 270, 26060-26062
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Cytotoxic T Lymphocyte-associated Molecule-4, a High Avidity Receptor for CD80 and CD86, Contains an Intracellular Localization Motif in Its Cytoplasmic Tail.
H. T. Leung, J. Bradshaw, J. S. Cleaveland, and P. S. Linsley (1995)
J. Biol. Chem. 270, 25107-25114
   Abstract »    Full Text »    PDF »
P-glycoprotein.
T. W. Loo and D. M. Clarke (1995)
J. Biol. Chem. 270, 21839-21844
   Abstract »    Full Text »    PDF »
Chaperone Function of Calreticulin When Expressed in the Endoplasmic Reticulum as the Membrane-anchored and Soluble Forms.
I. Wada, S.-i. Imai, M. Kai, F. Sakane, and H. Kanoh (1995)
J. Biol. Chem. 270, 20298-20304
   Abstract »    Full Text »    PDF »
Conformational Changes Induced in the Endoplasmic Reticulum Luminal Domain of Calnexin by Mg-ATP and Ca[IMAGE].
W.-J. Ou, J. J. M. Bergeron, Y. Li, C. Y. Kang, and D. Y. Thomas (1995)
J. Biol. Chem. 270, 18051-18059
   Abstract »    Full Text »    PDF »
Role of the Endoplasmic Reticulum Chaperone Calnexin in Subunit Folding and Assembly of Nicotinic Acetylcholine Receptors.
M. S. Gelman, W. Chang, D. Y. Thomas, J. J. M. Bergeron, and J. M. Prives (1995)
J. Biol. Chem. 270, 15085-15092
   Abstract »    Full Text »    PDF »
Transient Aggregation of Major Histocompatibility Complex Class II Chains during Assembly in Normal Spleen Cells.
M. S. Marks, R. N. Germain, and J. S. Bonifacino (1995)
J. Biol. Chem. 270, 10475-10481
   Abstract »    Full Text »    PDF »
The Molecular Chaperone Calnexin Binds Glc(1)Man(9)GlcNAc(2) Oligosaccharide as an Initial Step in Recognizing Unfolded Glycoproteins.
F. E. Ware, A. Vassilakos, P. A. Peterson, M. R. Jackson, M. A. Lehrman, and D. B. Williams (1995)
J. Biol. Chem. 270, 4697-4704
   Abstract »    Full Text »    PDF »
Calnexin Recognizes Carbohydrate and Protein Determinants of Class I Major Histocompatibility Complex Molecules.
Q. Zhang, M. Tector, and R. D. Salter (1995)
J. Biol. Chem. 270, 3944-3948
   Abstract »    Full Text »    PDF »
Molecular Requirements for the Interaction of Class II Major Histocompatibility Complex Molecules and Invariant Chain with Calnexin.
B. Arunachalam and P. Cresswell (1995)
J. Biol. Chem. 270, 2784-2790
   Abstract »    Full Text »    PDF »
Saccharomyces cerevisiae CNE1 Encodes an Endoplasmic Reticulum (ER) Membrane Protein with Sequence Similarity to Calnexin and Calreticulin and Functions as a Constituent of the ER Quality Control Apparatus.
F. Parlati, M. Dominguez, J. J. M. Bergeron, and D. Y. Thomas (1995)
J. Biol. Chem. 270, 244-253
   Abstract »    Full Text »    PDF »
Assembly and Intracellular Transport of MHC Class I and Class II Molecules.
M.R. Jackson, K. Fruh, L. Karlsson, L. Teyton, Y. Yang, and P.A. Peterson (1995)
Cold Spring Harb Symp Quant Biol 60, 249-261
   Abstract »    PDF »
Assembly, Peptide Loading, and Transport of MHC Class I Molecules in a Calnexin-negative Cell Line.
B.K. Sadasivan, A. Cariappa, G.L. Waneck, and P. Cresswell (1995)
Cold Spring Harb Symp Quant Biol 60, 267-275
   Abstract »    PDF »
Calnexin, Calreticulin, and Bip/Kar2p in Protein Folding.
D.N. Hebert, J.F. Simons, J.R. Peterson, and A. Helenius (1995)
Cold Spring Harb Symp Quant Biol 60, 405-415
   Abstract »    PDF »
Folding of VSV G protein: sequential interaction with BiP and calnexin.
C Hammond and A Helenius (1994)
Science 266, 456-458
   Abstract »    PDF »
Cell Surface Expression of Calnexin, a Molecular Chaperone in the Endoplasmic Reticulum.
Y. Okazaki, H. Ohno, K. Takase, T. Ochiai, and T. Saito (2000)
J. Biol. Chem. 275, 35751-35758
   Abstract »    Full Text »    PDF »
Translation Rate of Human Tyrosinase Determines Its N-Linked Glycosylation Level.
A. Ujvari, R. Aron, T. Eisenhaure, E. Cheng, H. A. Parag, Y. Smicun, R. Halaban, and D. N. Hebert (2001)
J. Biol. Chem. 276, 5924-5931
   Abstract »    Full Text »    PDF »
The Lectin Chaperone Calnexin Utilizes Polypeptide-based Interactions to Associate with Many of Its Substrates in Vivo.
U. G. Danilczyk and D. B. Williams (2001)
J. Biol. Chem. 276, 25532-25540
   Abstract »    Full Text »    PDF »


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