Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes.

Molecular cell ·Vol. 3 ·No. 6 ·1999-06-00 ·Pages 751-60

Min J, Okada S, Kanzaki M, Elmendorf JS, Coker KJ, Ceresa BP, Syu LJ, Noda Y, Saltiel AR, Pessin JE

Abstract

Insulin-stimulated glucose transport and GLUT4 translocation require regulated interactions between the v-SNARE, VAMP2, and the t-SNARE, syntaxin 4. We have isolated a novel syntaxin 4-binding protein, Synip, which specifically interacts with syntaxin 4. Insulin induces a dissociation of the Synip:syntaxin 4 complex due to an apparent decrease in the binding affinity of Synip for syntaxin 4. In contrast, the carboxyterminal domain of Synip does not dissociate from syntaxin 4 in response to insulin stimulation but inhibits glucose transport and GLUT4 translocation. These data implicate Synip as an insulin-regulated syntaxin 4-binding protein directly involved in the control of glucose transport and GLUT4 vesicle translocation.

MeSH Terms

Adipocytes/drug effects,metabolism Amino Acid Sequence Animals Binding, Competitive Biological Transport/drug effects Carrier Proteins/metabolism Cell Line Cloning, Molecular Cricetinae Genes, Dominant Glucose/metabolism Glucose Transporter Type 4 Humans Insulin/pharmacology Membrane Proteins/metabolism Mice Molecular Sequence Data Monosaccharide Transport Proteins/metabolism Muscle Proteins Mutation Organelles/metabolism Protein Binding/drug effects Qa-SNARE Proteins Qb-SNARE Proteins Qc-SNARE Proteins R-SNARE Proteins RNA, Messenger/analysis,genetics,metabolism Vesicular Transport Proteins Yeasts/genetics

Chemicals

Carrier Proteins Glucose Transporter Type 4 Insulin Membrane Proteins Monosaccharide Transport Proteins Muscle Proteins Qa-SNARE Proteins Qb-SNARE Proteins Qc-SNARE Proteins R-SNARE Proteins RNA, Messenger SLC2A4 protein, human SNAP23 protein, human STXBP4 protein, human Slc2a4 protein, mouse Snap23 protein, mouse Stxbp4 protein, mouse Vesicular Transport Proteins Glucose

Authors & Affiliations

10 authors, click to expand affiliations / ORCID

Min J

Department of Cell Biology, Parke-Davis Pharmaceutical Research Division, Warner-Lambert Company, Ann Arbor, Michigan 48105, USA.

Okada S

Kanzaki M

Elmendorf J S

Coker K J

Ceresa B P

Syu L J

Noda Y

Saltiel A R

Pessin J E

Article Info

Journal

Molecular cell

Abbr.

Mol Cell

ISSN

1097-2765

DOI

10.1016/s1097-2765(01)80007-1

Published

1999-06-00

Pages

751-60

Language

English

Region

United States

NLM ID

9802571

Subset

Databases

GENBANK

AF152924

Corrections

ErratumIn

External Links

PubMed source DOI: 10.1016/s1097-2765(01)80007-1 View journal details

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Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes.

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