In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2.
作者： Mechthild M. Schroeter , Brent Beall , Hans W. Heid , Joseph M. Chalovich
DOI: 10.1042/BSR20080079
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摘要: An analysis of the primary structure actin-binding protein fesselin revealed it to be avian homologue mammalian synaptopodin 2 [Schroeter, Beall, Heid, and Chalovich (2008) Biochem. Biophys. Res. Commun. 371, 582-586]. We isolated two isoforms from rabbit stomach that corresponded known types human 2. The purification scheme used was developed for fesselin. These forms shared several key functions with Both bound Ca(2+)-calmodulin, alpha-actinin smooth-muscle myosin. In addition, both proteins stimulated polymerization actin in a Ca(2+)-calmodulin-dependent manner. Synaptopodin has never before been shown polymerize absence alpha-actinin, manner, or bind Ca(2+)-calmodulin properties are consistent proposed function organizing cytoskeleton.
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