Heat shock increases turnover of 90 kDa heat shock protein phosphate groups in HeLa cells
- 21 October 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 291 (2) , 359-362
- https://doi.org/10.1016/0014-5793(91)81320-8
Abstract
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.Keywords
This publication has 22 references indexed in Scilit:
- The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent mannerCell, 1990
- Renaturation of denatured λ repressor requires heat shock proteinsCell, 1990
- Interaction of Hsp 70 with Newly Synthesized Proteins: Implications for Protein Folding and AssemblyScience, 1990
- Protein Denaturation During Heat Shock and Related StressPublished by Springer Nature ,1990
- Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cellsCell, 1989
- Protein Denaturation during Heat Shock and Related StressJournal of Biological Chemistry, 1989
- THE HEAT-SHOCK PROTEINSAnnual Review of Genetics, 1988
- Two mammalian heat shock proteins, HSP90 and HSP100, are actin-binding proteins.Proceedings of the National Academy of Sciences, 1986
- THE HEAT-SHOCK RESPONSEAnnual Review of Biochemistry, 1986
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970