Following Ariadne's thread: a new perspective on RBR ubiquitin ligases

BMC Biology

Review

Dawn M Wenzel¹  Rachel E Klevit² 

[1] Department of Biochemistry, University of Utah School of Medicine, 15 N. Medical Drive East, 84112-5650, Salt Lake City, UT, USA;Department of Biochemistry, University of Washington, 98195, Seattle, Washington, USA;

关键词: Parkin;    Thioester;    Ring Domain;    Active Site Cysteine;    Thioester Bond;   

DOI  :  10.1186/1741-7007-10-24

 received in 2011-12-05, accepted in 2012-03-15,  发布年份 2012

来源: Springer

【 摘 要 】

Ubiquitin signaling pathways rely on E3 ligases for effecting the final transfer of ubiquitin from E2 ubiquitin conjugating enzymes to a protein target. Here we re-evaluate the hybrid RING/HECT mechanism used by the E3 family RING-between-RINGs (RBRs) to transfer ubiquitin to substrates. We place RBRs into the context of current knowledge of HECT and RING E3s. Although not as abundant as the other types of E3s (there are only slightly more than a dozen RBR E3s in the human genome), RBRs are conserved in all eukaryotes and play important roles in biology. Re-evaluation of RBR ligases as RING/HECT E3s provokes new questions and challenges the field.

【 授权许可】

CC BY   
© Wenzel and Klevit; licensee BioMed Central Ltd. 2012