Mimicking phosphorylation of αB-crystallin affects its chaperone activity
نویسندگان
چکیده
Heath ECROYD*, Sarah MEEHAN*, Joseph HORWITZ†, J. Andrew AQUILINA‡, Justin L. P. BENESCH§, Carol V. ROBINSON§, Cait E. MACPHEE‖ and John A. CARVER*1 *School of Chemistry and Physics, University of Adelaide, Adelaide, SA 5005, Australia, †Jules Stein Institute, University of California, Los Angeles, School of Medicine, Los Angeles, CA 90095-7008, U.S.A., ‡School of Biological Sciences, University of Wollongong, Wollongong, NSW 2522, Australia, §Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, U.K., and ‖The Biological and Soft Systems Group, Cavendish Laboratory, University of Cambridge, Cambridge CB3 0HE, U.K.
منابع مشابه
Mimicking phosphorylation of alphaB-crystallin affects its chaperone activity.
AlphaB-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 alphaB-crystallin. In the present study, we produced recombinant proteins designed to mimic phosphorylation of alphaB-cry...
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α-Crystallin is the principal lens protein which, in addition to its structural role, also acts as a molecular chaperone, to prevent aggregation and precipitation of other lens proteins. One of its two subunits, αBcrystallin, is also expressed in many non-lenticular tissues, and a natural missense mutation, R120G, has been associated with cataract and desminrelated myopathy, a disorder of skele...
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Stress conditions can destabilize proteins, promoting them to unfold and adopt intermediately folded states. Partially folded protein intermediates are unstable and prone to aggregation down off-folding pathways leading to the formation of either amorphous or amyloid fibril aggregates. The sHsp (small heat-shock protein) αB-crystallin acts as a molecular chaperone to prevent both amorphous and ...
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