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| F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex |
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| Author(s): Skowyra D, Craig KL, Tyers M, Elledge SJ, Harper JW |
| Source: CELL Volume: 91 Issue: 2 Pages: 209-219 Published: OCT 17 1997 |
| Times Cited: 664 References: 42 |
| Abstract: We have reconstituted the ubiquitination pathway for the Cdk inhibitor Sic1 using recombinant proteins. Skp1, Cdc53, and the F-box protein Cdc4 form a complex, SCFCdc4, which functions as a Sic1 ubiquitin-ligase (E3) in combination with the ubiquitin conjugating enzyme (E2) Cdc34 and E1. Cdc4 assembled with Skp1 functions as the receptor that selectively binds phosphorylated Sic1. Grr1, an F-box protein involved in Cln destruction, forms complexes with Skp1 and Cdc53 and binds phosphorylated Cln1 and Cln2, but not Sic1. Because the constituents of the SCF complex are members of protein families, SCFCdc4 in likely to serve as the prototype for a large class of E3s formed by combinatorial interactions of related family members. SCF complexes couple protein kinase signaling pathways to the control of protein abundance. |
| Document Type: Article |
| Language: English |
Addresses:
1. BAYLOR COLL MED, VERNA & MARRS MCLEAN DEPT BIOCHEM, HOUSTON, TX 77030 USA
2. BAYLOR COLL MED, DEPT MOL & HUMAN GENET, HOUSTON, TX 77030 USA
3. BAYLOR COLL MED, HOWARD HUGHES MED INST, HOUSTON, TX 77030 USA
4. MT SINAI HOSP, SAMUEL LUNENFELD RES INST, PROGRAM MOL BIOL & CANC, TORONTO, ON M5G 1X5 CANADA |
| Publisher: CELL PRESS, 1050 MASSACHUSETTES AVE, CIRCULATION DEPT, CAMBRIDGE, MA 02138 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: YC350 |
| ISSN: 0092-8674 |
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