STIMULATION BY PHOSPHOLIPIDS OF A PROTEIN-TYROSINE-PHOSPHATASE CONTAINING 2 SRC HOMOLOGY-2 DOMAINS

被引：115

作者：

ZHAO, ZH ^{[1
]}

SHEN, SH ^{[1
]}

FISCHER, EH ^{[1
]}

机构：

[1] NATL RES COUNCIL CANADA, INST BIOTECHNOL RES, MOLEC BIOL SECT, MONTREAL H3A 2B2, PQ, CANADA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1993年 / 90卷 / 09期

关键词：

D O I：

10.1073/pnas.90.9.4251

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

PTP1C, a protein-tyrosine-phosphatase (protein-tyrosine-phosphate phosphohydrolase, EC 3.1.3.48) containing two src homology 2 domains, is poorly active when assayed with various protein substrates in vitro. Its activity is stimulated >1000-fold by anionic phospholipids when myelin basic protein or mitogen-activated protein kinase is used as substrate but reduced in the presence of several other substrates. Data are presented to indicate a direct interaction of the enzyme with phospholipids. Enzyme stimulation directed only toward certain specific substrates is interpreted by assuming that these compounds also bind to the phospholipid vesicles where they will be subjected to rapid enzymatic attack. A possible regulation of PTP1C by its translocation to the cell membrane is hypothesized.

引用

页码：4251 / 4255

页数：5

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