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Trends Cell Biol. 2000 Oct;10(10):429-39.

The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases.

Author information

  • 1Dept of Pathology, The Stanford University School of Medicine, Stanford, CA 94305-5324, USA. pjackson@cmgm.stanford.edu

Abstract

Recently, many new examples of E3 ubiquitin ligases or E3 enzymes have been found to regulate a host of cellular processes. These E3 enzymes direct the formation of multiubiquitin chains on specific protein substrates, and - typically - the subsequent destruction of those proteins. We discuss how the modular architecture of E3 enzymes connects one of two distinct classes of catalytic domains to a wide range of substrate-binding domains. In one catalytic class, a HECT domain transfers ubiquitin directly to substrate bound to a non-catalytic domain. Members of the other catalytic class, found in the SCF, VBC and APC complexes, use a RING finger domain to facilitate ubiquitylation. The separable substrate-recognition domains of E3 enzymes provides a flexible means of linking a conserved ubiquitylation function to potentially thousands of ubiquitylated substrates in eukaryotic cells.

PMID:
10998601
[PubMed - indexed for MEDLINE]
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