Regulating the yeast kinetochore by ubiquitin-dependent degradation and Skp1p-mediated phosphorylation

Kenneth B. Kaplan, Anthony A. Hyman, Peter K. Sorger

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128 Scopus citations

Abstract

In S. cerevisiae, the four-protein Cbf3 complex binds to the essential CDEIII region of centromeric DNA to initiate kinetochore assembly. We report the reconstitution of Cbf3p from recombinant proteins and an analysis of its p58(Ctf13) and p23(Skp1) subunits. p23(Skp1) has both G1- and G2-specific functions in yeast and binds to p58(Ctf13) and to the essential Cdc4p component of the ubiquitin conjugating complex Scul(Cdc4). We show that the function of p23(skp1) in Cbf3p is to activate p58(Ctf13) by phosphorylation. p58(Ctf13) is an unstable protein that is targeted to the proteosome, probably by Scul(Cdc4)mediated ubiquitination. Thus, p58 appears to be activated by phosphorylation in a p23(Skp1)-dependent step and degraded by the proteosome in a ubiquitin-dependent step. We propose that coupled activation and destruction link the assembly of Cbf3p to the duplication of centromeres in S phase.

Original languageEnglish (US)
Pages (from-to)491-500
Number of pages10
JournalCell
Volume91
Issue number4
StatePublished - Nov 14 1997
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

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    Kaplan, K. B., Hyman, A. A., & Sorger, P. K. (1997). Regulating the yeast kinetochore by ubiquitin-dependent degradation and Skp1p-mediated phosphorylation. Cell, 91(4), 491-500.