Phosphorylation of alphaB-crystallin alters chaperone function through loss of dimeric substructure.

Journal article

Phosphorylation is the most common posttranslational modification of the alpha-crystallins in the human lens. These phosphorylated forms are not only important because of their abundance in aging lenses and the implications for cataract but also because they have been identified in patients with degenerative brain disease. By using mimics corresponding to the reported in vivo phosphorylation sites in the human lens, we have examined the effects of phosphorylation upon the chaperone-like prope...

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Authors: Aquilina, J; Benesch, J; Ding, L; Yaron, O; Horwitz, J

• Publication status: Published
• Journal: Journal of biological chemistry
• Volume: 279
• Issue: 27
• Pages: 28675-28680
• Publication date: 2004-07-01
• DOI: 10.1074/jbc.m403348200
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Protein Conformation; Binding Sites; Scattering, Radiation; Phosphorylation; Molecular Chaperones; Models, Biological; Dimerization; Models, Molecular; Lens, Crystalline; Serine; Humans; Polymerase Chain Reaction; alpha-Crystallin B Chain; Mass Spectrometry; Triticum; Time Factors; Light; Mutation; Brain; Ultraviolet Rays; Circular Dichroism