Purification of erythrocyte dematin (protein 4.9) reveals an endogenous protein kinase that modulates actin-bundling activity.
作者： A Husain-Chishti , W Faquin , C C Wu , D Branton
DOI: 10.1016/S0021-9258(18)81891-9
关键词: Biology 、 Actin 、 In vitro 、 Cell 、 Protein kinase A 、 Gene isoform 、 Phosphorylation 、 Biochemistry 、 Kinase 、 Protein subunit
摘要: A partially purified preparation of human erythrocyte protein 4.9, consisting 48-, 52-, and 55-kilodalton polypeptides, is capable bundling rabbit muscle actin in vitro (Siegel, D. L., Branton, (1985) J. Cell Biol. 100, 775–785). Purification schemes, peptide mapping, antibody cross-reactivity, chemical cross-linking techniques show that the 48- 52-kDa polypeptides are sequence-related phosphorylated components, whereas 55-kDa polypeptide not. Purified 4.9 (dematin), effectively bundles vitro; under similar conditions, isolated does not bundle actin. In fact, when added back to dematin, fractions containing can completely abolish dematin's actin-bundling activity. The basis for this inhibitory activity an endogenous kinase phosporylates both isoforms thus abolishing (Husain-Chishti, A., Levin, (1988) Nature 334, 718–721). Although often co-purifies with polypeptide, it be separated from has characteristics a catalytic subunit cyclic AMP-dependent kinase.
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