New insights into ubiquitin E3 ligase mechanism

Christopher E. Berndsen; Cynthia Wolberger

doi:10.1038/nsmb.2780

New insights into ubiquitin E3 ligase mechanism

Christopher E. Berndsen, Cynthia Wolberger

School of Medicine

Research output: Contribution to journal › Review article › peer-review

312 Scopus citations

Abstract

E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct classes of E3 ligases have been identified that stimulate transfer of ubiquitin and ubiquitin-like proteins through either a direct or an indirect mechanism. Only recently have the catalytic mechanisms of E3 ligases begun to be elucidated.

Original language	English (US)
Pages (from-to)	301-307
Number of pages	7
Journal	Nature Structural and Molecular Biology
Volume	21
Issue number	4
DOIs	https://doi.org/10.1038/nsmb.2780
State	Published - Apr 2014

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1038/nsmb.2780

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title = "New insights into ubiquitin E3 ligase mechanism",

abstract = "E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct classes of E3 ligases have been identified that stimulate transfer of ubiquitin and ubiquitin-like proteins through either a direct or an indirect mechanism. Only recently have the catalytic mechanisms of E3 ligases begun to be elucidated.",

author = "Berndsen, {Christopher E.} and Cynthia Wolberger",

note = "Funding Information: We thank R. Hay, A. Plechanovov{\'a} and B. Schulman for providing coordinates of modeled complexes. C.W. acknowledges grant support from the US National Institutes of Health (GM095822) and National Science Foundation (MCB0920082).",

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N2 - E3 ligases carry out the final step in the ubiquitination cascade, catalyzing transfer of ubiquitin from an E2 enzyme to form a covalent bond with a substrate lysine. Three distinct classes of E3 ligases have been identified that stimulate transfer of ubiquitin and ubiquitin-like proteins through either a direct or an indirect mechanism. Only recently have the catalytic mechanisms of E3 ligases begun to be elucidated.

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New insights into ubiquitin E3 ligase mechanism

Abstract

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