Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1

被引：351
作者：
Skowyra, D
Koepp, DM
Kamura, T
Conrad, MN
Conaway, RC
Conaway, JW
Elledge, SJ
Harper, JW [1 ]
机构：
[1] Baylor Coll Med, Verna & Marrs McLean Dept Biochem, Houston, TX 77030 USA
[2] Baylor Coll Med, Dept Biochem, Houston, TX 77030 USA
[3] Baylor Coll Med, Dept Mol & Human Genet, Houston, TX 77030 USA
[4] Baylor Coll Med, Howard Hughes Med Inst, Houston, TX 77030 USA
[5] Oklahoma Med Res Fdn, Program Mol & Cell Biol, Oklahoma City, OK 73104 USA
[6] Univ Oklahoma, Hlth Sci Ctr, Dept Biochem & Mol Biol, Oklahoma City, OK 73190 USA
来源：
SCIENCE | 1999年 / 284卷 / 5414期
关键词：
D O I：
10.1126/science.284.5414.662
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Control of cyclin Levels is critical for proper cell cycle regulation. In yeast, the stability of the Ci,,cyclin Cln1 is controlled by phosphorylation-dependent ubiquitination. Here it is shown that this reaction can be reconstituted in vitro with an SCF E3 ubiquitin ligase complex. Phosphorylated Cln1 was ubiquitinated by SCF (Skp1Cdc53-F-box protein) complexes containing the F-box protein Grr1, Rbx1, and the E2 Cdc34. Rbx1 promotes association of Cdc34 with Cdc53 and stimulates Cdc34 auto-ubiquitination in the context of Cdc53 or SCF complexes. Rbx1, which is also a component of the von Hippe-Lindau tumor suppressor complex, may define a previously unrecognized class of E3-associated proteins.
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收藏
页码：662 / 665
页数：4
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