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PMID: 1983272 Published · ppublish English Journal Article Review

Transport and assembly processes in the endoplasmic reticulum.

Seminars in cell biology ·Vol. 1 ·No. 1 ·1990-02-00 ·Pages 65-72

Gething MJ, Sambrook J

Abstract

Until recently, the endoplasmic reticulum (ER) of eukaryotic cells was regarded as an open corridor for the unregulated movement of newly-synthesized exocytotic proteins from their site of membrane translocation to the vesicles that ferry them from the transitional elements of the ER to the Golgi apparatus. Moreover, it was widely assumed that the folding and assembly of newly translocated polypeptides into their tertiary and quaternary structure is a spontaneous process that does not involve the intervention of other cellular proteins. In this article we review evidence that the ER is a highly discriminatory organelle that grants passage only to proteins that have attained an essentially native conformation, and summarize current knowledge about resident ER proteins that appear to facilitate and/or monitor protein folding and assembly in this organelle.

MeSH Terms
Amino Acid Sequence Animals Biological Transport Carrier Proteins/genetics,metabolism Chaperonins Endoplasmic Reticulum/metabolism Endoplasmic Reticulum Chaperone BiP Heat-Shock Proteins/metabolism Humans Molecular Chaperones Molecular Sequence Data Molecular Structure Protein Conformation Proteins/metabolism Sequence Alignment
Chemicals
Carrier Proteins Endoplasmic Reticulum Chaperone BiP Heat-Shock Proteins Molecular Chaperones Proteins Chaperonins
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Gething M J
Department of Biochemistry, University of Texas Southwestern Medical Center, Dallas 75235.
Sambrook J
Article Info
Journal
Seminars in cell biology
Abbr.
Semin Cell Biol
ISSN
1043-4682
Published
1990-02-00
Pages
65-72
Language
English
Region
England
NLM ID
9007587
Subset
IM
External Links
PubMed source
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