E3 ligases determine ubiquitination site and conjugate type by enforcing specificity on E2 enzymes.
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, whe...
Hoofdauteurs: | , , , , , , , , |
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Formaat: | Journal article |
Taal: | English |
Gepubliceerd in: |
2011
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