PIPkins, their substrates and their products: new functions for old enzymes

被引：98

作者：

Hinchliffe, KA ^{[1
]}

Ciruela, A ^{[1
]}

Irvine, RF ^{[1
]}

机构：

[1] Univ Cambridge, Dept Pharmacol, Cambridge CB2 1QJ, England

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 1998年 / 1436卷 / 1-2期

基金：

英国生物技术与生命科学研究理事会;

关键词：

inositol; lipid kinase; signal transduction;

D O I：

10.1016/S0005-2760(98)00140-4

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 phosphatidylinositolphosphate kinases (PIPkins) are a unique family of enzymes that catalyse the production of phosphorylated inositol lipids. Recent advances have revealed that, due to their ability to utilise a number of different lipid substrates (at least in vitro), this family is potentially able to generate several distinct, physiologically important inositol lipids. Despite their importance, however, our understanding of the regulation of the PIPkins and of their physiological role in cellular signalling and regulation is still poor. Here we describe in turn the diverse physiological functions of the known substrates and major products of the PIPkins. We then examine what is known about the members of the PIPkin family themselves, and their characteristics and regulation. (C) 1998 Elsevier Science B.V. All rights reserved.

引用

页码：87 / 104

页数：18

共 133 条

[21] Complementation of growth factor receptor-dependent mitogenic signaling by a truncated type I phosphatidylinositol 4-phosphate 5-kinase [J].

Davis, JN ;

Rock, CO ;

Cheng, MG ;

Watson, JB ;

Ashmun, RA ;

Kirk, H ;

Kay, RJ ;

Roussel, MF .

MOLECULAR AND CELLULAR BIOLOGY, 1997, 17 (12) :7398-7406

[22] Phosphoinositides as regulators in membrane traffic [J].

DeCamilli, P ;

Emr, SD ;

McPherson, PS ;

Novick, P .

SCIENCE, 1996, 271 (5255) :1533-1539

[23] CA2+ AND PH DETERMINE THE INTERACTION OF CHROMAFFIN CELL SCINDERIN WITH PHOSPHATIDYLSERINE AND PHOSPHATIDYLINOSITOL 4,5,-BIPHOSPHATE AND ITS CELLULAR-DISTRIBUTION DURING NICOTINIC-RECEPTOR STIMULATION AND PROTEIN-KINASE-C ACTIVATION [J].

DELCASTILLO, AR ;

VITALE, ML ;

TRIFARO, JM .

JOURNAL OF CELL BIOLOGY, 1992, 119 (04) :797-810

[24] MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae [J].

Desrivières, S ;

Cooke, FT ;

Parker, PJ ;

Hall, MN .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (25) :15787-15793

[25] High concentrations of phosphatidylinositol-4,5-bisphosphate may promote actin filament growth by three potential mechanisms: Inhibiting capping by neutrophil lysates, severing actin filaments and removing capping protein-beta(2) from barbed ends [J].

DiNubile, MJ ;

Huang, S .

BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 1997, 1358 (03) :261-278

[26] THE CLONING AND SEQUENCE OF THE C-ISOFORM OF PTDINS4P 5-KINASE [J].

DIVECHA, N ;

TRUONG, O ;

HSUAN, JJ ;

HINCHLIFFE, KA ;

IRVINE, RF .

BIOCHEMICAL JOURNAL, 1995, 309 :715-719

[27] PHOSPHOLIPID SIGNALING [J].

DIVECHA, N ;

IRVINE, RF .

CELL, 1995, 80 (02) :269-278

[28] Osmotic stress activates phosphatidylinositol-3,5-bisphosphate synthesis [J].

Dove, SK ;

Cooke, FT ;

Douglas, MR ;

Sayers, LG ;

Parker, PJ ;

Michell, RH .

NATURE, 1997, 390 (6656) :187-192

[29] EVIDENCE THAT THE INOSITOL PHOSPHOLIPIDS ARE NECESSARY FOR EXOCYTOSIS - LOSS OF INOSITOL PHOSPHOLIPIDS AND INHIBITION OF SECRETION IN PERMEABILIZED CELLS CAUSED BY A BACTERIAL PHOSPHOLIPASE-C AND REMOVAL OF ATP [J].

EBERHARD, DA ;

COOPER, CL ;

LOW, MG ;

HOLZ, RW .

BIOCHEMICAL JOURNAL, 1990, 268 (01) :15-25

[30] Direct regulation of the Akt proto-oncogene product by phosphatidylinositol-3,4-bisphosphate [J].

Franke, TF ;

Kaplan, DR ;

Cantley, LC ;

Toker, A .

SCIENCE, 1997, 275 (5300) :665-668

← 1 2 3 4 5 6 7 8 9 10 →