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PMID: 3141786 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Identity of the immunoglobulin heavy-chain-binding protein with the 78,000-dalton glucose-regulated protein and the role of posttranslational modifications in its binding function.

Molecular and cellular biology ·Vol. 8 ·No. 10 ·1988-10-00 ·Pages 4250-6

Hendershot LM, Ting J, Lee AS

Abstract

The 78,000-dalton glucose-regulated protein (GRP78) and the immunoglobulin heavy-chain-binding protein (BiP) were shown to be the same protein by NH2-terminal sequence comparison. Immunoprecipitation of GRP78-BiP induced by glucose starvation and a temperature-sensitive mutation in a hamster fibroblast cell line demonstrated the association of GRP78-BiP with other cellular proteins. In both fibroblasts and lymphoid cells, GRP78-BiP was found to label with 32Pi and [3H]adenosine. Phosphoamino acid analysis demonstrated that GRP78-BiP is phosphorylated on serine and threonine residues. Conditions which induce increased production of GRP78-BiP resulted in decreased incorporation of 32Pi and [3H]adenosine into GRP78-BiP. Furthermore, we report here that the phosphorylated form of BiP resides in the endoplasmic reticulum and that BiP which is associated with heavy chains is not phosphorylated or labeled with [3H]adenosine, whereas free BiP is. This suggests that posttranslational modifications may be important in regulating the synthesis and binding of BiP.

MeSH Terms

Adenosine/metabolism Amino Acid Sequence Animals Carrier Proteins/physiology Cricetinae Endoplasmic Reticulum/metabolism Endoplasmic Reticulum Chaperone BiP Fibroblasts/metabolism HSP70 Heat-Shock Proteins Heat-Shock Proteins Immunoglobulin Heavy Chains/metabolism,physiology Lymphocytes/metabolism Membrane Proteins/physiology Mice Molecular Chaperones Molecular Sequence Data Phosphoproteins/metabolism Phosphorylation Protein Binding Protein Processing, Post-Translational

Chemicals

Carrier Proteins Endoplasmic Reticulum Chaperone BiP HSP70 Heat-Shock Proteins Heat-Shock Proteins Hspa5 protein, mouse Immunoglobulin Heavy Chains Membrane Proteins Molecular Chaperones Phosphoproteins glucose-regulated proteins Adenosine

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Hendershot L M

Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38101.

Ting J

Lee A S

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Article Info

Journal

Molecular and cellular biology

Abbr.

Mol Cell Biol

ISSN

0270-7306

DOI

10.1128/mcb.8.10.4250-4256.1988

Published

1988-10-00

Pages

4250-6

Language

English

Region

United States

NLM ID

8109087

PMCID

PMC365497

Subset

Grants

NCI NIH HHS · CA13148 · United States

NCI NIH HHS · CA16673 · United States

NIAID NIH HHS · R23-AI23526-02 · United States

External Links

PubMed source DOI: 10.1128/mcb.8.10.4250-4256.1988 PMC Full Text View journal details

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Identity of the immunoglobulin heavy-chain-binding protein with the 78,000-dalton glucose-regulated protein and the role of posttranslational modifications in its binding function.

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