Synapsin IIb interacts with the C-terminal SH2 and SH3 domains of PLCgamma1 and inhibits its enzymatic activity.
To elucidate the function of PLCgamma1, 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 PLCgamma1 and synapsin IIb, which binds the carboxyl terminal SH2 and SH3 domains of the enzyme and inhibits it.
Han
Seung Jin
SJ
School of Biological Sciences, Seoul National University, Seoul, Republic of Korea.
Hong
Seung Hwan
SH
Kim
Chul Geun
CG
Lee
Jung Bin
JB
Choi
Dong Kug
DK
Kim
Kyong-Rae
KR
Kim
Chan Gil
CG
D000818:Animals; D001665:Binding Sites / Q000276:immunology / Q000502:physiology; D004791:Enzyme Inhibitors / Q000276:immunology / Q000378:metabolism / Q000494:pharmacology; D007120:Immunochemistry; D051966:Phospholipase C gamma; D011485:Protein Binding / Q000276:immunology / Q000502:physiology; D011817:Rabbits; D051381:Rats; D016704:Synapsins / Q000276:immunology / Q000378:metabolism* / Q000494:pharmacology; D010738:Type C Phospholipases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D018909:src Homology Domains / Q000276:immunology*
D004791:Enzyme Inhibitors; D016704:Synapsins; D010738:Type C Phospholipases; D051966:Phospholipase C gamma