PURIFICATION OF A 20-KDA PHOSPHOPROTEIN FROM EPITHELIAL-CELLS AND IDENTIFICATION AS A MYOSIN LIGHT CHAIN - PHOSPHORYLATION INDUCED BY ENTEROPATHOGENIC ESCHERICHIA-COLI AND PHORBOL ESTER

被引：27

作者：

MANJARREZHERNANDEZ, HA

AMESS, B

SELLERS, L

BALDWIN, TJ

KNUTTON, S

WILLIAMS, PH

AITKEN, A

机构：

[1] NATL INST MED RES,PROTEIN STRUCT LAB,RIDGEWAY,MILL HILL,LONDON NW7 1AA,ENGLAND

[2] UNIV LEICESTER,DEPT GENET,LEICESTER LE1 7RH,ENGLAND

[3] UNIV BIRMINGHAM,INST CHILD HLTH,BIRMINGHAM B16 8ET,ENGLAND

来源：

FEBS LETTERS | 1991年 / 292卷 / 1-2期

基金：

英国惠康基金;

关键词：

MYOSIN LIGHT CHAIN; PROTEIN PHOSPHORYLATION; PROTEIN KINASE-C; ENTEROPATHOGENIC ESCHERICHIA-COLI; CACO-2; CELL; HEP-2;

D O I：

10.1016/0014-5793(91)80848-W

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：

Previous studies on the mechanism of enteropathogenic Escherichia coli (EPEC) infection have revealed an increase in the phosphorylation state of a number of proteins in human laryngeal HEp-2 cells. The most prominent was an acidic phosphoprotein(s) of M(r) 20-21 kDa. The present study reports: (a) a simple method for purification of phosphorylated 20 kDa protein; (b) identification of the 20 kDa phosphoprotein as myosin light chain; and (c) that the phorbol ester, TPA, also increased the phosphorylation of the 20 kDa myosin light chain. In contrast to the effects of EPEC, TPA stimulation resulted in the dissociation of myosin from the cytoskeleton to the cytosol.

引用

页码：121 / 127

页数：7

共 24 条

[1] REGULATION AND KINETICS OF THE ACTIN-MYOSIN-ATP INTERACTION [J].