The Di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding.
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.
Peden
A A
AA
Department of Molecular and Cellular Physiology, Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305-5345, USA.
Park
G Y
GY
Scheller
R H
RH
D020816:Amino Acid Motifs; D000818:Animals; D001923:Brain Chemistry; D002460:Cell Line; D022163:Clathrin-Coated Vesicles / Q000737:chemistry / Q000378:metabolism*; D006023:Glycoproteins; D008562:Membrane Glycoproteins / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008862:Microsomes, Liver / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D050683:R-SNARE Proteins; D051381:Rats; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D050600:SNARE Proteins; D018808:Transcription Factor AP-1 / Q000378:metabolism*; D033921:Vesicular Transport Proteins
D006023:Glycoproteins; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D050683:R-SNARE Proteins; D011993:Recombinant Fusion Proteins; D050600:SNARE Proteins; C513045:Tgoln2 protein, rat; D018808:Transcription Factor AP-1; D033921:Vesicular Transport Proteins