SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box

Bai Chang, Sen Partha, Kay Hofmann, Ma Lei, Mark Goebl, J. Wade Harper, Stephen J. Elledge

Research output: Contribution to journalArticle

886 Scopus citations

Abstract

We have identified the yeast and human homologs of the SKP1 gene as a suppressor of cdc4 mutants and as a cyclin F-binding protein. Skp1p indirectly binds cyclin A/Cdk2 through Skp2p, and directly binds Skp2p, cyclin F, and Cdc4p through a novel structural motif called the F-box. SKP1 is required for ubiquitin-mediated proteolysis of Cln2p, Clb5p, and the Cdk inhibitor Sic1p, and provides a link between these molecules and the proteolysis machinery. A large number of proteins contain the F-box motif and are thereby implicated in the ubiquitin pathway. Different skp1 mutants arrest cells in either G1 or G2, suggesting a connection between regulation of proteolysis in different stages of the cycle.

Original languageEnglish (US)
Pages (from-to)263-274
Number of pages12
JournalCell
Volume86
Issue number2
DOIs
StatePublished - Jul 26 1996

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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