Mammalian phospholipase D structure and regulation

被引：268

作者：

Frohman, MA ^{[1
]}

Sung, TC

Morris, AJ

机构：

[1] SUNY Stony Brook, Dept Pharmacol Sci, Stony Brook, NY 11794 USA

[2] SUNY Stony Brook, Inst Cell & Dev Biol, Stony Brook, NY 11794 USA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 1999年 / 1439卷 / 02期

关键词：

HKD motif; catalytic domain; phospholipase D structure;

D O I：

10.1016/S1388-1981(99)00093-1

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 recent identification of cDNA clones for phospholipase D1 and 2 has opened the door to new studies on its structure and regulation. PLD activity is encoded by at least two different genes that contain catalytic domains that relate their mechanism of action to phosphodiesterases. In vivo roles for PLD suggest that it may be important for multiple specialized steps in receptor dependent and constitutive processes of secretion, endocytosis, and membrane biogenesis. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：175 / 186

页数：12

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