ALPHA-CRYSTALLIN SMALL HEAT-SHOCK PROTEIN HAS AUTOKINASE ACTIVITY

被引:120
作者
KANTOROW, M
PIATIGORSKY, J
机构
[1] Lab. of Molec. and Devmtl. Biology, National Eye Institute, National Institutes of Health, Bethesda
关键词
LENS; PHOSPHORYLATION;
D O I
10.1073/pnas.91.8.3112
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The alpha-crystallins (alphaA and alphaB) are major water-soluble proteins of the transparent eye lens that are expressed in a variety of tissues and can function as molecular chaperones. AlphaB-crystallin is also a small heat shock protein associated with numerous degenerative diseases and abnormal growth patterns. Previous experiments have shown that alphaA- and alphaB-crystallin are phosphorylated on specific serine residues by a cAMP-dependent pathway. Here we provide evidence that either total bovine alpha-crystallin or its isolated polypeptides can autophosphorylate serine by a cAMP-independent mechanism in the presence of Mg2+ and [gamma-P-32]ATP; the autophosphorylated products isoelectrically focus with the authentic phosphorylated forms of the alpha-crystallin polypeptides. Thus, the alphaA- and alphaB-crystallin/small heat shock protein polypeptides are enzyme-crystallins which may be involved in metabolic pathways important for the development, maintenance, or pathology of the lens and other tissues.
引用
收藏
页码:3112 / 3116
页数:5
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