Research article summary (published 8 Jun 2003):

Phosphorylation-dependent structural alterations in the small hsp30 chaperone are associated with cellular recovery.

Full Abstract

Small heat shock proteins (hsps) act as molecular chaperones by preventing the thermal aggregation and unfolding of cellular protein; however, the manner by which cells regulate chaperone activity remains unclear. In the present study, we examined the role of phosphorylation on the chaperone function of the Xenopus small hsp30. Both heat stress and sodium arsenite treatment in A6 cells resulted in a rapid activation of p38alpha and MAPKAPK-2. Surprisingly, the association of MAPKAPK-2 with hsp30 and its subsequent phosphorylation were more prevalent during recovery after heat stress. Treatment of A6 cells with SB203580, an inhibitor of the p38 MAP kinase pathway, resulted in a loss of hsp30 phosphorylation. Phosphorylation resulted in the formation of smaller multimeric hsp30 complexes and resulted in a significant loss of secondary structure. Consequently the phosphorylation-induced structural changes severely compromised the ability of hsp30 to prevent the heat-induced aggregation of citrate synthase and luciferase in vitro. We confirmed that the loss of chaperone activity was coincident with an attenuated binding of phosphorylated hsp30 with target proteins. Our data suggest that phosphorylation may be necessary to regulate the post-heat stress molecular chaperone activity of hsp30.

Author information

Author/s: Fernando, Pasan (P); Megeney, Lynn A (LA); Heikkila, John J (JJ);

Affiliation: Ottawa Health Research Institute, Ottawa General Hospital, Center for Molecular Medicine, Ottawa, Ontario, Canada K1H 8L6.

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

Journal: Experimental cell research (Exp Cell Res), published in United States. (Language: eng)

Reference: 2003-Jun; vol 286 (issue 2) : pp 175-85

Dates: Created 2003/05/16; Completed 2003/07/11; Revised 2007/11/15;

PMID: 12749847, status: MEDLINE (last retrieval date: 2/18/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Animals Arsenites - pharmacology Cells, Cultured Enzyme Inhibitors - pharmacology Eukaryotic Cells - metabolism HSP30 Heat-Shock Proteins Heat-Shock Proteins - metabolism Heat-Shock Response - physiology Intracellular Signaling Peptides and Proteins Macromolecular Substances Membrane Proteins - metabolism Mitogen-Activated Protein Kinase 14

Mitogen-Activated Protein Kinase 14 Mitogen-Activated Protein Kinases - metabolism Molecular Chaperones - physiology Phosphorylation Protein Binding - drug effects; physiology Protein Folding Protein Structure, Secondary - drug effects; physiology Protein-Serine-Threonine Kinases - metabolism Serine - metabolism Sodium Compounds - pharmacology Xenopus Proteins Xenopus laevis

Associated Chemicals: Arsenites (0) ; Enzyme Inhibitors (0) ; HSP30 Heat-Shock Proteins (0) ; Heat-Shock Proteins (0) ; Intracellular Signaling Peptides and Proteins (0) ; Macromolecular Substances (0) ; Membrane Proteins (0) ; Molecular Chaperones (0) ; Sodium Compounds (0) ; Xenopus Proteins (0) ; hsp30 protein, Xenopus (0) ; sodium arsenite (13768-07-5) ; Serine (56-45-1) ; MAP-kinase-activated kinase 2 (EC 2.7.1.-) ; Mitogen-Activated Protein Kinase 14 (EC 2.7.1.37) ; Mitogen-Activated Protein Kinases (EC 2.7.1.37) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1)

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