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PMID: 7905823 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Stress- and mitogen-induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance.

The EMBO journal ·Vol. 13 ·No. 1 ·1994-01-01 ·Pages 54-60

Knauf U, Jakob U, Engel K, Buchner J, Gaestel M

Abstract

Small heat shock proteins (sHsps) show a very rapid stress- and mitogen-dependent phosphorylation by MAPKAP kinase 2. Based on this observation, phosphorylation of sHsps was thought to play a key role in mediating thermoresistance immediately after heat shock, before the increased synthesis of heat shock proteins becomes relevant. We have analysed the phosphorylation dependence of the chaperone and thermoresistance-mediating properties of the small heat shock protein Hsp25. Surprisingly, overexpression of Hsp25 mutants, which are not phosphorylated in the transfected cells, confers the same thermoresistant phenotype as overexpression of wild type Hsp25, which is either mono- or bis-phosphorylated at serine residues 15 and 86 within the cells. Furthermore, in vitro phosphorylated Hsp25 shows the same oligomerization properties and the same chaperone activity as the nonphosphorylated protein. No differences between phosphorylated and nonphosphorylated Hsp25 are detected in preventing thermal aggregation of unfolding proteins and assisting refolding of denatured proteins. The results suggest that chaperone properties of the small heat shock proteins contribute to the increased cellular thermoresistance in a phosphorylation-independent manner.

MeSH Terms
3T3 Cells Animals Blotting, Western Chaperonins Heat-Shock Proteins/biosynthesis,metabolism Hot Temperature Intracellular Signaling Peptides and Proteins Mice Mitogens/metabolism Molecular Chaperones Mutagenesis, Site-Directed Neoplasm Proteins/biosynthesis,genetics,metabolism Phosphorylation Protein Serine-Threonine Kinases/metabolism Proteins/metabolism Transfection
Chemicals
Heat-Shock Proteins Hsbp1 protein, mouse Intracellular Signaling Peptides and Proteins Mitogens Molecular Chaperones Neoplasm Proteins Proteins MAP-kinase-activated kinase 2 Protein Serine-Threonine Kinases Chaperonins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Knauf U
Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany.
Jakob U
Engel K
Buchner J
Gaestel M
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1994-01-01
Pages
54-60
Language
English
Region
England
NLM ID
8208664
PMCID
PMC394778
Subset
IM
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