Phosphorylation of alphaB-crystallin and HSP27 is induced by similar stressors in HeLa cells

Biochemical and Biophysical Research Communications
P R van den IJsselW W de Jong

Abstract

Three members of the small heat shock protein family, alphaA-, alphaB-crystallin, and HSP27, confer thermoresistance upon their overexpression in mammalian cells. Phosphorylation, in conjunction with the molecular chaperone-like activity of these small HSPs, is believed to be important for this in situ functional property. We here report the influence of heat shock and other kinds of stress on the phosphorylation of alphaA-, alphaB-crystallin, and HSP27 in stably transfected HeLa cells. It is observed that alphaB-crystallin becomes phosphorylated upon exposure to the same inducers as is HSP27, although to a lesser extent. In contrast, phosphorylation of alphaA-crystallin is very low upon heat stress and even absent when other stressors are used. This indicates that phosphorylation is not in all instances essential for the stress protective functioning of the various small HSPs.

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Citations

Aug 10, 2000·Neuropathology and Applied Neurobiology·M W Head, J E Goldman
Jul 8, 1999·Proceedings of the National Academy of Sciences of the United States of America·A A van RijkH Bloemendal
Feb 15, 2015·Journal of Molecular Biology·Martin Haslbeck, Elizabeth Vierling
Nov 30, 1999·Molecular Cell Biology Research Communications : MCBRC·W RustG E Plopper
Nov 6, 2018·The Journal of Biological Chemistry·Martin HaslbeckJohannes Buchner
Aug 6, 2020·International Journal of Molecular Sciences·Mareike RiedlMartin Haslbeck
Oct 18, 2019·Frontiers in Pharmacology·Jack M WebsterLaura J Blair
Oct 30, 2014·Cellular and Molecular Life Sciences : CMLS·Teresa M TreweekJohn A Carver
Aug 20, 2003·European Journal of Cell Biology·Anke E van RijkHans Bloemendal

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