Journal
TRENDS IN CELL BIOLOGY
Volume 10, Issue 10, Pages 429-439Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/S0962-8924(00)01834-1
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Funding
- NIGMS NIH HHS [GM54811, GM60439] Funding Source: Medline
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Recently, many nay 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.
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