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

The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

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
DOI 10.1083/jcb.104.3.761PMC PMC2114523
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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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Metadata

Authors
Hendershot, L., Bole, D., Köhler, G., & Kearney, J. F.
Affiliations
  • University of Alabama at Birmingham (US)
  • Max Planck Society (DE)
ORCID
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
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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