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Synapsin IIb interacts with the C‐terminal SH2 and SH3 domains of PLCγ1 and inhibits its enzymatic activity
Author(s) -
Han Seung Jin,
Hong Seung Hwan,
Kim Chul Geun,
Lee Jung Bin,
Choi Dong Kug,
Kim KyongRae,
Kim Chan Gil
Publication year - 2004
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2004.09.007
Subject(s) - synapsin i , enzyme , chemistry , synapsin , biochemistry , microbiology and biotechnology , biology , vesicle , membrane , synaptic vesicle
To elucidate the function of PLCγ1, we have investigated the proteins that bind to its SH (Src homology) domain. Immunoscreening was performed with purified antisera specific for SH223 (two SH2 and one SH3)‐binding proteins. Several immunoreactive clones were identified as putative binding proteins and one of them was identified as synapsin IIb. We demonstrate a stable association between PLCγ1 and synapsin IIb, which binds the carboxyl terminal SH2 and SH3 domains of the enzyme and inhibits it.