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Retention of Unassembled Components of Integral Membrane Proteins by Calnexin
Abstract
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 ε 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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Citations
Cited by
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Hammond, C., & Helenius, A. (1995) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(95)80009-3 · Cited by 673
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Parodi, A. J. (2000) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.69.1.69 · Cited by 658
Protein Folding in the Endoplasmic Reticulum
Braakman, I., & Hebert, D. N. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a013201 · Cited by 571
Role of Heat Shock Proteins in Protection from and Pathogenesis of Infectious Diseases
Zügel, U., & Kaufmann, S. H. E. (1999) · Clinical Microbiology Reviews · doi:10.1128/cmr.12.1.19 · Cited by 559
Hebert, D. N., Foellmer, B., & Helenius, A. (1995) · Cell · doi:10.1016/0092-8674(95)90395-x · Cited by 552
Metadata
- Authors
- Rajagopalan, S., Xu, Y., & Brenner, M. B.
- Venue
- Science
- Published
- 1994-01-21
- Volume
- 263
- Issue
- 5145
- Pages
- 387-390
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1994947913
- Cited by
- 243
- References
- 0
- FWCI
- 12.05
- Type
- journal article
- Language
- en
- Open access
- closed
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