Heat shock increases turnover of 90 kDa heat shock protein phosphate groups in HeLa cells.
The 90 kDa heat shock protein (hsp90) 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 hsp90 in recovery from stress. In this report, we describe a dramatic increase in the rate of both phosphate uptake and dephosphorylation of hsp90 in HeLa cells submitted to acute stresses. This increased turnover of hsp90 phosphate groups might reflect a greater protein binding activity of hsp90 in stressed cells.
Département de Biologie, Ecole Normale Supérieure, Paris, France.
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Legagneux
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Morange
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Bensaude
D002352:Carrier Proteins / Q000378:metabolism*; D006367:HeLa Cells / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D008970:Molecular Weight; D028044:Phosphate-Binding Proteins; D010710:Phosphates / Q000378:metabolism*; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation
D002352:Carrier Proteins; D006360:Heat-Shock Proteins; D028044:Phosphate-Binding Proteins; D010710:Phosphates; D010750:Phosphoproteins