A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p

R. M Renny Feldman, Craig C. Correll, Kenneth B. Kaplan, Raymond J. Deshaies

Research output: Contribution to journalArticle

673 Citations (Scopus)

Abstract

In S. cerevisiae, the G1/S transition requires Cdc4p, Cdc34p, Cdc53p, Skp1p, and the Cln/Cdc28p cyclin-dependent kinase (Cdk). These proteins are thought to promote the proteolytic inactivation of the S-phase Cdk inhibitor Sic1p. We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCF(Cdc4p). When mixed together, SCF(Cdc4p) subunits, E1 enzyme, the E2 enzyme Cdc34p, and ubiquitin are sufficient to reconstitute ubiquitination of Cdk-phosphorylated Sic1p. Phosphorylated Sic1p substrate is specifically targeted for ubiquitination by binding to a Cdc4p/Skp1p subcomplex. Taken together, these data illuminate the molecular basis for the G1/S transition in budding yeast and suggest a general mechanism for phosphorylation-targeted ubiquitination in eukaryotes.

Original languageEnglish (US)
Pages (from-to)221-230
Number of pages10
JournalCell
Volume91
Issue number2
DOIs
StatePublished - Oct 17 1997
Externally publishedYes

Fingerprint

Cullin Proteins
Cyclin-Dependent Kinases
Ubiquitination
Ubiquitin
Phosphorylation
Saccharomycetales
Enzymes
Ligases
Eukaryota
S Phase
Yeast
Saccharomyces cerevisiae
Substrates
Proteins

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. / Feldman, R. M Renny; Correll, Craig C.; Kaplan, Kenneth B.; Deshaies, Raymond J.

In: Cell, Vol. 91, No. 2, 17.10.1997, p. 221-230.

Research output: Contribution to journalArticle

Feldman, R. M Renny ; Correll, Craig C. ; Kaplan, Kenneth B. ; Deshaies, Raymond J. / A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. In: Cell. 1997 ; Vol. 91, No. 2. pp. 221-230.
@article{f9003711cbba4dbbadbfc8f2f375e61a,
title = "A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p",
abstract = "In S. cerevisiae, the G1/S transition requires Cdc4p, Cdc34p, Cdc53p, Skp1p, and the Cln/Cdc28p cyclin-dependent kinase (Cdk). These proteins are thought to promote the proteolytic inactivation of the S-phase Cdk inhibitor Sic1p. We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCF(Cdc4p). When mixed together, SCF(Cdc4p) subunits, E1 enzyme, the E2 enzyme Cdc34p, and ubiquitin are sufficient to reconstitute ubiquitination of Cdk-phosphorylated Sic1p. Phosphorylated Sic1p substrate is specifically targeted for ubiquitination by binding to a Cdc4p/Skp1p subcomplex. Taken together, these data illuminate the molecular basis for the G1/S transition in budding yeast and suggest a general mechanism for phosphorylation-targeted ubiquitination in eukaryotes.",
author = "Feldman, {R. M Renny} and Correll, {Craig C.} and Kaplan, {Kenneth B.} and Deshaies, {Raymond J.}",
year = "1997",
month = "10",
day = "17",
doi = "10.1016/S0092-8674(00)80404-3",
language = "English (US)",
volume = "91",
pages = "221--230",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "2",

}

TY - JOUR

T1 - A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p

AU - Feldman, R. M Renny

AU - Correll, Craig C.

AU - Kaplan, Kenneth B.

AU - Deshaies, Raymond J.

PY - 1997/10/17

Y1 - 1997/10/17

N2 - In S. cerevisiae, the G1/S transition requires Cdc4p, Cdc34p, Cdc53p, Skp1p, and the Cln/Cdc28p cyclin-dependent kinase (Cdk). These proteins are thought to promote the proteolytic inactivation of the S-phase Cdk inhibitor Sic1p. We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCF(Cdc4p). When mixed together, SCF(Cdc4p) subunits, E1 enzyme, the E2 enzyme Cdc34p, and ubiquitin are sufficient to reconstitute ubiquitination of Cdk-phosphorylated Sic1p. Phosphorylated Sic1p substrate is specifically targeted for ubiquitination by binding to a Cdc4p/Skp1p subcomplex. Taken together, these data illuminate the molecular basis for the G1/S transition in budding yeast and suggest a general mechanism for phosphorylation-targeted ubiquitination in eukaryotes.

AB - In S. cerevisiae, the G1/S transition requires Cdc4p, Cdc34p, Cdc53p, Skp1p, and the Cln/Cdc28p cyclin-dependent kinase (Cdk). These proteins are thought to promote the proteolytic inactivation of the S-phase Cdk inhibitor Sic1p. We show here that Cdc4p, Cdc53p, and Skp1p assemble into a ubiquitin ligase complex named SCF(Cdc4p). When mixed together, SCF(Cdc4p) subunits, E1 enzyme, the E2 enzyme Cdc34p, and ubiquitin are sufficient to reconstitute ubiquitination of Cdk-phosphorylated Sic1p. Phosphorylated Sic1p substrate is specifically targeted for ubiquitination by binding to a Cdc4p/Skp1p subcomplex. Taken together, these data illuminate the molecular basis for the G1/S transition in budding yeast and suggest a general mechanism for phosphorylation-targeted ubiquitination in eukaryotes.

UR - http://www.scopus.com/inward/record.url?scp=0030695025&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030695025&partnerID=8YFLogxK

U2 - 10.1016/S0092-8674(00)80404-3

DO - 10.1016/S0092-8674(00)80404-3

M3 - Article

C2 - 9346239

AN - SCOPUS:0030695025

VL - 91

SP - 221

EP - 230

JO - Cell

JF - Cell

SN - 0092-8674

IS - 2

ER -