Phospholipase C delta(1) requires a pleckstrin homology domain for interaction with the plasma membrane

被引：110

作者：

Paterson, HF ^{[1
]}

Savopoulos, JW ^{[1
]}

Perisic, O ^{[1
]}

Cheung, R ^{[1
]}

Ellis, MV ^{[1
]}

Williams, RL ^{[1
]}

Katan, M ^{[1
]}

机构：

[1] MRC CTR,CTR PROT ENGN,CAMBRIDGE CB2 2QH,ENGLAND

来源：

BIOCHEMICAL JOURNAL | 1995年 / 312卷

基金：

英国医学研究理事会;

关键词：

D O I：

10.1042/bj3120661

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 structural requirements of phospholipase C delta(1), for interaction with the plasma membrane were analysed by immunofluorescence after microinjection into living cells, Microinjection of deletion mutants revealed that the region required for membrane attachment and binding of inositol 1,4,5-trisphosphate in vitro corresponded to the pleckstrin homology domain, a structural module described in more than 90 proteins.

引用

页码：661 / 666

页数：6

共 25 条

[1]

ASANO M, 1994, J BIOL CHEM, V269, P12360

[2] EF-HAND MOTIFS IN INOSITOL PHOSPHOLIPID-SPECIFIC PHOSPHOLIPASE-C [J].