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Ubiquitination and degradation of the substrate recognition subunits of SCF ubiquitin-protein ligases.

Abstract：

:The S. cerevisiae SCFCdc4p ubiquitin-protein ligase complex promotes cell cycle transitions through degradation of cell cycle regulators. To investigate SCFCdc4p regulation in vivo, we examined the stability of individual SCFCdc4p components. Whereas Cdc53p and Skp1p were stable, Cdc4p, the F box-containing component responsible for substrate recognition, was short lived and subject to SCF-mediated ubiquitination. Grr1p, another F box component of SCF complexes, was also ubiquitinated. A stable truncated Cdc4pF-beta-gal hybrid protein capable of binding Skp1p and entering into an SCF complex interfered with proteolysis of SCF targets and inhibited cell proliferation. The finding that the F box-containing SCF components are unstable suggests a mechanism of regulating SCF function through ubiquitination and proteolysis of F box components.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Zhou P,Howley PM

doi

10.1016/s1097-2765(00)80156-2

subject

Has Abstract

pub_date

1998-11-01 00:00:00

pages

571-80

issue

5

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(00)80156-2

journal_volume

2

pub_type

杂志文章

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