Interaction of phospholipase C γ 1 via its COOH-terminal SRC homology 2 domain with synaptojanin

被引：13

作者：

Ahn, SJ

Han, SJ

Mo, HJ

Chung, JK

Hong, SH

Park, TK

Kim, CG

机构：

[1] Konkuk Univ, Dept Biol Mol, Chungju City, South Korea

[2] Seoul Natl Univ, Dept Biol Mol, Seoul, South Korea

[3] Bu Kyung Univ, Dept Fish Pathol, Pusan, South Korea

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 244卷 / 01期

关键词：

D O I：

10.1006/bbrc.1998.8220

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The role of the phospholipase C gamma 1 (PLC gamma 1) in signal transduction was investigated by characterizing its interactions with proteins that may represent components of a novel signalling pathway. A 145-kDa protein that binds SH2 domain of PLC gamma 1 was purified from rat brain. The sequence of peptide derived from the purified binding protein now identify it as synaptojanin, a nerve terminal protein that has been implicated in the endocytosis of fused synaptic vesicles and shown to be a member of the inositol polyphosphate 5-phosphatase family. We demonstrate here stable association of PLC gamma 1 with synaptojanin, a protein that not only binds carboxyl terminal SH2 domain of PLC gamma 1, but also inhibits PLC gamma 1 activity. (C) 1998 Academic Press.

引用

页码：62 / 67

页数：6

共 35 条

[1] INOSITOL TRISPHOSPHATE AND CALCIUM SIGNALING [J].