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Heat shock increases turnover of 90 kDa heat shock protein phosphate groups in HeLa cells
Author(s) -
Legagneux Vincent,
Morange Michel,
Bensaude Olivier
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)81320-8
Subject(s) - dephosphorylation , phosphoprotein , heat shock protein , phosphate , receptor , phosphorylation , hela , chemistry , hspa14 , biochemistry , microbiology and biotechnology , phosphatase , hsp70 , biology , cell , gene
The 90 kDa heat shock protein (hsp9O) is a major phosphoprotein which associates various other cellular polypeptides such as actin, calmodulin, steroid hormone receptors and certain protein‐kinases. Little is known about the function of hsp9O in recovery from stress. In this report, we describe a dramatic increase in the rate of both phosphate uptake and dephosphorylation of hsp9O in HeLa cells submitted to acute stresses. This increased turnover of hsp9O phosphate groups might reflect a greater protein binding activity of hsp9O in stressed cells.