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PMID: 2868889 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles.

The EMBO journal ·Vol. 4 ·No. 13A ·1985-12-16 ·Pages 3385-91

Ungewickell E

Abstract

It is shown that in immunological, structural and functional terms the uncoating protein, which catalyses ATP-dependent dissociation of clathrin triskelia from clathrin-coated vesicles is intimately related to two major stress proteins of mammalian cells. These proteins of hitherto unknown functions have polypeptide mol. wts. of 73 kd and 72 kd, respectively. They are normal cell constituents which are synthesized in increased abundance under adverse environmental circumstances, such as non-physiological temperatures or treatment with amino acid analogues.

MeSH Terms

Animals Carrier Proteins/immunology,physiology Cattle Cell Nucleus/metabolism Clathrin/immunology,physiology Coated Pits, Cell-Membrane/immunology,physiology Cross Reactions Cytoplasm/metabolism Endosomes/physiology Fluorescent Antibody Technique HSC70 Heat-Shock Proteins HSP70 Heat-Shock Proteins Heat-Shock Proteins/immunology,physiology Hot Temperature Molecular Weight Peptide Fragments/analysis

Chemicals

Carrier Proteins Clathrin HSC70 Heat-Shock Proteins HSP70 Heat-Shock Proteins Heat-Shock Proteins Peptide Fragments

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Ungewickell E

References (26)

26 references, click to expand

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Article Info

Journal

The EMBO journal

Abbr.

EMBO J

ISSN

0261-4189

Published

1985-12-16

Pages

3385-91

Language

English

Region

England

NLM ID

8208664

PMCID

PMC554674

Subset

External Links

PubMed source PMC Full Text View journal details

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The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles.

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