Defined sequence segments of the small heat shock proteins HSP25 and alphaB-crystallin inhibit actin polymerization

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Item Type:	Article
Title:	Defined sequence segments of the small heat shock proteins HSP25 and alphaB-crystallin inhibit actin polymerization
Creators Name:	Wieske, M., Benndorf, R., Behlke, J., Doelling, R., Grelle, G., Bielka, H. and Lutsch, G.
Abstract:	The interaction of small heat shock proteins (sHSPs) with the actin cytoskeleton has been described and some members of this family, e.g. chicken and murine HSP25 (HSP27), inhibit the polymerization of actin in vitro. To analyse the molecular basis of this interaction, we synthesized a set of overlapping peptides covering the complete sequence of murine HSP25 and tested the effect of these peptides on actin polymerization in vitro by fluorescence spectroscopy and electron microscopy. Two peptides comprising the sequences W43 to R57 (peptide 6) and I92 to N106 (peptide 11) of HSP25 were found to be potent inhibitors of actin polymerization. Phosphorylation of N-terminally extended peptide 11 at serine residues known to be phosphorylated in vivo resulted in decline of their inhibitory activity. Interestingly, peptides derived from the homologous peptide 11 sequence of murine αB-crystallin showed the same behaviour. The results suggest that both HSP25 and αB-crystallin have the potential to inhibit actin polymerization and that this activity is regulated by phosphorylation.
Keywords:	Actin Polymerization, Electron Microscopy, Fluorescence Spectroscopy, Phosphorylation, Small Heat Shock Proteins, Animals, Mice
Source:	European Journal of Biochemistry
ISSN:	0014-2956
Publisher:	Blackwell Publishing
Volume:	268
Number:	7
Page Range:	2083-2090
Date:	1 January 2001
Official Publication:	https://doi.org/10.1046/j.1432-1327.2001.02082.x
PubMed:	View item in PubMed

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