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• W1993718695 abstract "αB-crystallin is a member of the sHsp (small heat-shock protein) family that prevents misfolded target proteins from aggregating and precipitating. Phosphorylation at three serine residues (Ser19, Ser45 and Ser59) is a major post-translational modification that occurs to αB-crystallin. In the present study, we produced recombi-nant proteins designed to mimic phosphorylation of αB-crystallin by incorporating a negative charge at these sites. We employed these mimics to undertake a mechanistic and structural invest-igation of the effect of phosphorylation on the chaperone activity of αB-crystallin to protect against two types of protein misfolding, i.e. amorphous aggregation and amyloid fibril assembly. We show that mimicking phosphorylation of αB-crystallin results in more efficient chaperone activity against both heat-induced and reduc-tion-induced amorphous aggregation of target proteins. Mimick-ing phosphorylation increased the chaperone activity of αB-crystallin against one amyloid-forming target protein (κ-casein), but decreased it against another (ccβ-Trp peptide). We observed that both target protein identity and solution (buffer) conditions are critical factors in determining the relative chaperone ability of wild-type and phosphorylated αB-crystallins. The present study provides evidence for the regulation of the chaperone activity of αB-crystallin by phosphorylation and indicates that this may play an important role in alleviating the pathogenic effects associated with protein conformational diseases." @default.
• W1993718695 created "2016-06-24" @default.
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• W1993718695 date "2006-12-11" @default.
• W1993718695 modified "2023-09-28" @default.
• W1993718695 title "Mimicking phosphorylation of αB-crystallin affects its chaperone activity" @default.
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• W1993718695 doi "https://doi.org/10.1042/bj20060981" @default.
• W1993718695 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1698675" @default.
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• W1993718695 hasPublicationYear "2006" @default.
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