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

被引：78

作者：

Wenzel, Dawn M. ^{[2
]}

Klevit, Rachel E. ^{[1
]}

机构：

[1] Univ Washington, Dept Biochem, Seattle, WA 98195 USA

[2] Univ Utah, Sch Med, Dept Biochem, Salt Lake City, UT 84112 USA

来源：

BMC BIOLOGY | 2012年 / 10卷

关键词：

PROTEIN LIGASE; CONJUGATING ENZYME; ALPHA-SYNUCLEIN; PARKIN; RING; E3; DOMAIN; COMPLEX; BINDING; POLYUBIQUITINATION;

D O I：

10.1186/1741-7007-10-24

中图分类号：

Q [生物科学];

学科分类号：

090105 [作物生产系统与生态工程];

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.

引用

页数：8

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