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Journal article

E3 ligases determine ubiquitination site and conjugate type by enforcing specificity on E2 enzymes.

Abstract:

Ubiquitin-conjugating enzymes (E2s) have a dominant role in determining which of the seven lysine residues of ubiquitin is used for polyubiquitination. Here we show that tethering of a substrate to an E2 enzyme in the absence of an E3 ubiquitin ligase is sufficient to promote its ubiquitination, whereas the type of the ubiquitin conjugates and the identity of the target lysine on the substrate are promiscuous. In contrast, when an E3 enzyme is introduced, a clear decision between mono- and po...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m111.234559

Authors


Ternette, N More by this author
Edelmann, MJ More by this author
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Journal:
The Journal of biological chemistry
Volume:
286
Issue:
51
Pages:
44104-44115
Publication date:
2011-12-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:6e509d3e-1724-42cb-9b43-20bb59026138
Source identifiers:
239712
Local pid:
pubs:239712

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