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 language | English (US) |
|---|---|
| Pages (from-to) | 221-230 |
| Number of pages | 10 |
| Journal | Cell |
| Volume | 91 |
| Issue number | 2 |
| DOIs | |
| State | Published - Oct 17 1997 |
| Externally published | Yes |
Fingerprint
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 journal › Article
}
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 -