Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 277, Issue 11, Pages 9010-9015Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M110815200
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- NIA NIH HHS [R01 AG13620] Funding Source: Medline
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Synaptophysin is a synaptic vesicle (SV) protein of unknown function. Here we show that a repeated sequence in the cytoplasmic tail of synaptophysin mediates the formation of a protein complex containing the GTPase dynamin. The formation of this complex requires a high Ca2+ concentration, suggesting that it occurs preferentially at the sites of SV exocytosis. Coimmunoprecipitation of a dynamin-synaptophysin complex from brain extracts is promoted by dissociation of vesicle-associated membrane protein 2 from synaptophysin. This finding suggests that dynamin only associates with synaptophysin in vivo after vesicle-associated membrane protein 2 (VAMP2) enters the SNARE complex. GTP binding releases dynamin from synaptophysin, possibly serving to regulate dynamin selfassembly during endocytosis. Our results suggest that synaptophysin plays a role in SV recycling by recruiting dynamin to the vesicle membrane.
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