Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP.

doi:10.1083/jcb.114.2.189

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Article

Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP.

The Journal of cell biology - 1 Jul 1991

Suzuki C K, Bonifacino J S, Lin A Y, Davis M M, Klausner R D

Abstract excerpt

Immunoglobulin heavy chain binding protein (BiP, GRP 78) coprecipitates with soluble and membrane-associated variants of the T-cell antigen receptor alpha chain (TCR-alpha) which are stably retained within the ER. Chelation of Ca2+ during solubilization of cells leads to the dissociation of BiP from the TCR-alpha variants, which is dependent upon the availability of Mg2+ and hydrolyzable ATP; this suggests that...

Topics

Animals
Calcimycin
Calcium
Carcinogens
Carrier Proteins
Cell Line
Cricetinae
Cricetulus
Dose-Response Relationship, Drug
Endoplasmic Reticulum
Endoplasmic Reticulum Chaperone BiP

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Female

Fluorescent Antibody Technique

Gene Rearrangement, alpha-Chain T-Cell Antigen Receptor

Genetic Variation

Heat-Shock Proteins

Immunoblotting

Immunoglobulin alpha-Chains

Source

Open in PubMed Open full text

Identifiers

PMID: 1649196
DOI: 10.1083/jcb.114.2.189
PMCID: PMC2289081

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1649196-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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