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Reconstitution of G1 Cyclin Ubiquitination with Complexes Containing SCFGrr1 and Rbx1

Science  23 Apr 1999:
Vol. 284, Issue 5414, pp. 662-665
DOI: 10.1126/science.284.5414.662

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Abstract

Control of cyclin levels is critical for proper cell cycle regulation. In yeast, the stability of the G1 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 (Skp1-Cdc53–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 Hippel–Lindau tumor suppressor complex, may define a previously unrecognized class of E3-associated proteins.

  • * To whom correspondence should be addressed. E-mail: jharper{at}bcm.tmc.edu.

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