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Identification of a novel SNAP25 interacting protein (SIP30)
Author(s) -
Lee HoKi,
Safieddine Saaid,
Petralia Ronald S.,
Wenthold Robert J.
Publication year - 2002
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.2002.00937.x
Subject(s) - snap25 , syntaxin , immunoprecipitation , stx1a , synaptotagmin 1 , snap23 , synaptic vesicle , microbiology and biotechnology , syntaxin 3 , membrane protein , biology , exocytosis , transport protein , munc 18 , chemistry , biochemistry , vesicle , vesicle associated membrane protein 8 , secretion , membrane , gene
Soluble N ‐ethylmaleimide‐sensitive factor attachment protein receptors (SNAREs), including synaptosome‐associated proteins of 25 kDa (SNAP25), syntaxins, and vesicle‐associated membrane proteins (VAMP), are essential for regulated exocytosis of synaptic vesicles in neurotransmission. We identified a cDNA coding for a novel protein of 266 amino acids that we have named SIP30 ( S NAP25 interacting protein of 30 kDa). SIP30 is expressed abundantly in brain and slightly in testis and kidney. In brain, SIP30 is highly expressed in the inferior and superior colliculi, which contain important relay nuclei of the auditory and visual systems. GST–pull‐down and immunoprecipitation assays showed direct binding of SIP30 to SNAP25. Although SIP30 does not directly interact with syntaxin based on pull‐down assays, syntaxin does co‐immunoprecipitate with SIP30 suggesting that syntaxin is indirectly associated with SIP30, perhaps through SNAP25.