期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 276, 期 32, 页码 29748-29753出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M103093200
关键词
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资金
- NIGMS NIH HHS [R37GM41628] Funding Source: Medline
The heterodimeric. Elongin BC complex has been shown to interact in vitro and in mammalian cells with a conserved BC-box motif found in a growing number of proteins including RNA polymerase Il elongation factor Elongin A, SOCS-box proteins, and the von Hippel-Lindau (VHL) tumor suppressor protein. Recently, the VHL-EIongin BC complex was found to interact with a module composed of Cullin family member Cul2 and RING-H2 finger protein Rbx1 to reconstitute a novel E3 ubiquitin ligase that activates ubiquitylation by the E2 ubiquitin-conjugating enzymes Ubc5 and Cdc34. In the context of: the VEL ubiquitin ligase, Elongin BC functions as an adaptor that links the VHL protein to the CuI2/Rbx1 module, raising the possibility that the Elongin BC complex could function as an integral component of a larger family of E3 ubiquitin ligases by linking alternative BC-box proteins to Cullin/Rbx1 modules. In this report, we describe identification and purification from rat liver of a novel leucine-rich repeat-containing BO-box protein, MUF1, which we demonstrate is capable of assembling, with a Cullin/Rbx1 module containing the Cullin family member Cul5 to reconstitute ubiquitin ligase activity. In addition, we show that the additional BC-box, proteins Elongin A, SOCS1, and WSB1 are also capable of assembling with the Cul5/Rbx1. module to reconstitute potential ubiquitin ligases. Taken together, our findings identify MUF1 as a new member of the BO-box family of proteins, and they predict the existence of a larger family of Elongin BC-based E3 ubiquitin ligases.
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