Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/109141
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Type: Journal article
Title: Phosphomimics destabilize Hsp27 oligomeric assemblies and enhance chaperone activity
Author: Jovcevski, B.
Kelly, M.
Rote, A.
Berg, T.
Gastall, H.
Benesch, J.
Aquilina, J.
Ecroyd, H.
Citation: Chemistry and Biology, 2015; 22(2):186-195
Publisher: Cell Press
Issue Date: 2015
ISSN: 1074-5521
1879-1301
Statement of
Responsibility: 
Blagojce Jovcevski, Megan A. Kelly, Anthea P. Rote, Tracey Berg, Heidi Y. Gastall, Justin L.P. Benesch, J. Andrew Aquilina and Heath Ecroyd
Abstract: Serine phosphorylation of the mammalian small heat-shock protein Hsp27 at residues 15, 78, and 82 is thought to regulate its structure and chaperone function; however, the site-specific impact has not been established. We used mass spectrometry to assess the combinatorial effect of mutations that mimic phosphorylation upon the oligomeric state of Hsp27. Comprehensive dimerization yielded a relatively uncrowded spectrum, composed solely of even-sized oligomers. Modification at one or two serines decreased the average oligomeric size, while the triple mutant was predominantly a dimer. These changes were reflected in a greater propensity for oligomers to dissociate upon increased modification. The ability of Hsp27 to prevent amorphous or fibrillar aggregation of target proteins was enhanced and correlated with the amount of dissociated species present. We propose that, in vivo, phosphorylation promotes oligomer dissociation, thereby enhancing chaperone activity. Our data support a model in which dimers are the chaperone-active component of Hsp27.
Keywords: Molecular Chaperones
Rights: © 2015 Elsevier Ltd All rights reserved
RMID: 0030075961
DOI: 10.1016/j.chembiol.2015.01.001
Grant ID: http://purl.org/au-research/grants/arc/FT110100586
Appears in Collections:Biochemistry publications

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