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PMID: 19851334 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Review

Building ubiquitin chains: E2 enzymes at work.

Nature reviews. Molecular cell biology ·Vol. 10 ·No. 11 ·2009-11-00 ·Pages 755-64

Ye Y, Rape M

Abstract

The modification of proteins with ubiquitin chains can change their localization, activity and/or stability. Although ubiquitylation requires the concerted action of ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s), it is the E2s that have recently emerged as key mediators of chain assembly. These enzymes are able to govern the switch from ubiquitin chain initiation to elongation, regulate the processivity of chain formation and establish the topology of assembled chains, thereby determining the consequences of ubiquitylation for the modified proteins.

MeSH Terms
Animals Humans Ubiquitin/metabolism Ubiquitin-Conjugating Enzymes/physiology
Chemicals
Ubiquitin Ubiquitin-Conjugating Enzymes
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ye Yihong
Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, NIH, Bethesda, Maryland 20892, USA. [email protected]
Rape Michael
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Article Info
Journal
Nature reviews. Molecular cell biology
Abbr.
Nat Rev Mol Cell Biol
ISSN
1471-0080
Published
2009-11-00
Pages
755-64
Language
English
Region
England
NLM ID
100962782
PMCID
PMC3107738
Subset
IM
Grants
NIGMS NIH HHS · R01 GM083064 · United States
Intramural NIH HHS · ZIA DK036137-03 · United States
NIGMS NIH HHS · 5 R01 GM083064-02 · United States
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