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PMID: 7909608 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin A.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 91 ·No. 9 ·1994-04-26 ·Pages 3931-5

Price ER, Jin M, Lim D, Pati S, Walsh CT, McKeon FD

Abstract

Cyclophilin B is targeted to the secretory pathway via an endoplasmic reticulum signal sequence. We analyzed the localization and trafficking of endogenous and transfected cyclophilin B in mammalian cells. Cyclophilin B accumulates both in the endoplasmic reticulum and in complexes on the plasma membrane. The immunosuppressant cyclosporin A specifically mobilizes cyclophilin B from the endoplasmic reticulum, and promotes the secretion of cyclophilin B into the medium. We suggest that cyclosporin A competes with endogenous plasma membrane proteins for association with cyclophilin B in the secretory pathway. These findings argue in favor of a role for cyclophilin B as a chaperone to proteins destined for the plasma membrane, rather than solely as a proline isomerase functioning within the endoplasmic reticulum.

MeSH Terms
Amino Acid Isomerases/metabolism Amino Acid Sequence Animals Biological Transport Carrier Proteins/metabolism Cell Compartmentation Cell Membrane/metabolism Chaperonins Cricetinae Cyclophilins Cyclosporine/metabolism Endoplasmic Reticulum/metabolism Golgi Apparatus/metabolism HeLa Cells Humans In Vitro Techniques Intracellular Membranes/metabolism Molecular Sequence Data Mutagenesis, Site-Directed Peptides/chemistry Peptidylprolyl Isomerase Protein Binding Proteins/metabolism Structure-Activity Relationship
Chemicals
Carrier Proteins Peptides Proteins cyclophilin B Cyclosporine Chaperonins Amino Acid Isomerases Cyclophilins Peptidylprolyl Isomerase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Price E R
Department of Cell Biology, Harvard Medical School, Boston, MA 02115.
Jin M
Lim D
Pati S
Walsh C T
McKeon F D
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.91.9.3931
Published
1994-04-26
Pages
3931-5
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC43696
Subset
IM
Grants
NIGMS NIH HHS · GM20011 · United States
External Links
PubMed source DOI: 10.1073/pnas.91.9.3931 PMC Full Text View journal details
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