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Following Ariadne's thread: a new perspective on RBR ubiquitin ligases. BMC Biol 2012 Mar 15;10:24

Date

03/17/2012

Pubmed ID

22420831

Pubmed Central ID

PMC3305615

DOI

10.1186/1741-7007-10-24

Scopus ID

2-s2.0-84858135252 (requires institutional sign-in at Scopus site)   72 Citations

Abstract

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.

Author List

Wenzel DM, Klevit RE

Author

Dawn M. Wenzel PhD Assistant Professor in the Biochemistry department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Animals
Drosophila
Humans
RING Finger Domains
Saccharomyces cerevisiae
Ubiquitin-Protein Ligases
Ubiquitination