期刊
JOURNAL OF CELL BIOLOGY
卷 164, 期 4, 页码 567-580出版社
ROCKEFELLER UNIV PRESS
DOI: 10.1083/jcb.200308061
关键词
cytoskeleton; cell motility; polymerization; assembly; Saccharomyces cerevisiae
类别
资金
- NIGMS NIH HHS [R01 GM047337, GM47337, R01 GM038542-15, R01 GM038542] Funding Source: Medline
The mechanism by which capping protein (CP) binds barbed ends of actin filaments is not understood, and the physiological significance of CP binding to actin is not defined. The CP crystal structure suggests that the COOH-terminal regions of the CP alpha and beta subunits bind to the barbed end. Using purified recombinant mutant yeast CP, we tested this model. CP lacking both COOH-terminal regions did not bind actin. The alpha COOH-terminal region was more important than that of beta. The significance of CPs actin-binding activity in vivo was tested by determining how well CP actin-binding mutants rescued null mutant phenotypes. Rescue correlated well with capping activity, as did localization of CP to actin patches, indicating that capping is a physiological function for CP. Actin filaments of patches appear to be nucleated first, then capped with CP. The binding constants of yeast CP for actin suggest that actin capping in yeast is more dynamic than in vertebrates.
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