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Article

The endoplasmic reticulum stress protein GRP94, in addition to BiP, associates with unassembled immunoglobulin chains.

The Journal of biological chemistry - 25 Oct 1992

Melnick J, Aviel S, Argon Y

Abstract excerpt

The molecular chaperone BiP/GRP78 associates with various polypeptides in the endoplasmic reticulum, including immunoglobulin chains. We now show, using chemical cross-linking, that another endoplasmic reticulum stress protein, GRP94, associates with newly synthesized immunoglobulin light and heavy chains. We demonstrate the presence of ternary complexes composed of immunoglobulin chains, BiP and GRP94. Because...

Topics

Carrier Proteins
Cross-Linking Reagents
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum
Endoplasmic Reticulum Chaperone BiP
HSP70 Heat-Shock Proteins
Heat-Shock Proteins
Immunoglobulins
Membrane Proteins
Molecular Chaperones

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Plasmids

Precipitin Tests

Tumor Cells, Cultured

Source

Identifiers

PMID: 1400441

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1400441-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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