Capping protein binding to actin in yeast: Biochemical mechanism and physiological relevance

Kyoungtae Kim, Atsuko Yamashita, Martin A. Wear, Yuichiro Maéda, John A. Cooper

Research output: Contribution to journalArticlepeer-review

80 Citations (Scopus)


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 α and β 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 α COOH-terminal region was more important than that of β. The significance of CP's 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.

Original languageEnglish
Pages (from-to)567-580
Number of pages14
JournalJournal of Cell Biology
Issue number4
Publication statusPublished - Feb 16 2004
Externally publishedYes


  • Assembly
  • Cell motility
  • Cytoskeleton
  • Polymerization
  • Saccharomyces cerevisiae

ASJC Scopus subject areas

  • Cell Biology


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