- 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...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1074/jbc.m111.234559
-
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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
- Language:
- English
- Keywords:
- Copyright date:
- 2011
Journal article
E3 ligases determine ubiquitination site and conjugate type by enforcing specificity on E2 enzymes.
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