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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
Author(s) -
Manjarrez-Hernandez Ha,
Bob Amess,
L. G. Sellers,
TJ Baldwin,
Stuart Knutton,
Williams Ph,
A. Aitken
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80848-w
Subject(s) - enteropathogenic escherichia coli , phosphoprotein , myosin light chain kinase , phosphorylation , myosin , immunoglobulin light chain , escherichia coli , biochemistry , cytosol , biology , chemistry , microbiology and biotechnology , antibody , enzyme , immunology , gene
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.