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PMID: 11598115 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The Di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding.

The Journal of biological chemistry ·Vol. 276 ·No. 52 ·2001-12-28 ·Pages 49183-7

Peden AA, Park GY, Scheller RH

Abstract

Heterotetrameric adaptor complexes and SNAREs play key roles in the specificity of membrane budding and fusion. Here we test the hypothesis that vesicle budding and membrane fusion are coupled by the interaction of these molecules. We investigate the role of the di-leucine motif of vesicle-associated membrane protein 4 (VAMP4) in adaptor binding and localization of VAMP4. Mutation of the di-leucine motif inhibits AP-1 binding in vitro and affects the steady state distribution of VAMP4 in vivo.

MeSH Terms
Amino Acid Motifs Animals Brain Chemistry Cell Line Clathrin-Coated Vesicles/chemistry,metabolism Glycoproteins Membrane Glycoproteins/metabolism Membrane Proteins/chemistry,genetics,metabolism Microsomes, Liver/chemistry,metabolism Protein Binding R-SNARE Proteins Rats Recombinant Fusion Proteins/metabolism SNARE Proteins Transcription Factor AP-1/metabolism Vesicular Transport Proteins
Chemicals
Glycoproteins Membrane Glycoproteins Membrane Proteins R-SNARE Proteins Recombinant Fusion Proteins SNARE Proteins Tgoln2 protein, rat Transcription Factor AP-1 Vesicular Transport Proteins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Peden A A
Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305-5345, USA.
Park G Y
Scheller R H
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
2001-12-28
Epub
2001-00-11
Pages
49183-7
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
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