Cited by 340Endoplasmic Reticulum Stress and DiseaseCellular transport and secretionHeat shock proteins research

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Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein.

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Hendershot, L, Bole, D, Köhler, G, Kearney, J F·1987·The Journal of cell biology

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Abstract

Heavy chain-binding protein (BiP) associates posttranslationally with nascent Ig heavy chains in the endoplasmic reticulum (ER) and remains associated with these heavy chains until they assemble with light chains. The heavy chain-BiP complex can be precipitated by antibody reagents against either component. To identify sites on heavy chain molecules that are important for association with BiP, we have examined 30 mouse myelomas and hybridomas that synthesize Ig heavy chains with well characterized deletions. Mutant Ig heavy chains that lack the CH1 domain could not be demonstrated to associate with BiP, whereas mutant Ig heavy chains with deletions of the CH2 or CH3 domain were still able to associate with BiP. In two light chain negative cell lines that produced heavy chains with deletions of the CH1 domain, free heavy chains were secreted. When Ig assembly and secretion were examined in mutants that did not associate with BiP, and were compared with normal parental lines, it was found that the rate of Ig secretion was increased in the mutant lines and that the Ig molecules were secreted in various stages of assembly. In one mutant line (CH1-) approximately one-third of the secreted Ig molecules were incompletely assembled, whereas the Ig molecules secreted by the parental line were completely assembled. Our data show the CH1 domain to be important for association with BiP and that when this association does not occur, incompletely assembled heavy chains can be secreted. This implies a role for BiP in preventing the transport of unassembled Ig molecules from the ER.

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Authors: Hendershot, L., Bole, D., Köhler, G., & Kearney, J. F.
Affiliations: University of Alabama at Birmingham (US)
Max Planck Society (DE)
ORCID: Hendershot, L
Kearney, J F
Venue: The Journal of cell biology
Publisher: Rockefeller University Press
Published: 1987-03-01
Volume: 104
Issue: 3
Pages: 761-767
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.104.3.761
PMC: PMC2114523
OpenAlex: W2002164494
Cited by: 340
References: 32
Citations by year: 2026: 3 · 2025: 3 · 2024: 7 · 2023: 5 · 2022: 2 · 2021: 1 · 2020: 8 · 2019: 5 · 2018: 4 · 2017: 8 · 2016: 5 · 2015: 7 · 2014: 6 · 2013: 7 · 2012: 12
FWCI: 9.67
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: The Journal of Cell Biology (publishedVersion)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Funders: U.S. Public Health Service (A 16673)
National Cancer Institute (CA-13 148)
National Institute of Allergy and Infectious Diseases (R01AI014782, AI 23526-01)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords: immunoglobulin heavy chain, BiP, endoplasmic reticulum, protein secretion, antibody assembly, CH1 domain, CH2 domain, CH3 domain, myeloma cells, hybridoma
MeSH terms: Endoplasmic Reticulum Chaperone BiP, Animals, Carrier Proteins, Cell Line, Heat-Shock Proteins, Immunoglobulin A, Immunoglobulin Heavy Chains, Kinetics, Mutation, Protein Processing, Post-Translational, Molecular Chaperones

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Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein.

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