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TL;DR
Using yeast E3 ligase knockout extracts, the authors first identified Rsp5p, the yeast homolog of mammalian Nedd4 family E3 ligases, as required for p27 ubiquitination.
The Journal of Biological Chemistry · 5 authors, 1 centre
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Using yeast E3 ligase knockout extracts, the authors first identified Rsp5p, the yeast homolog of mammalian Nedd4 family E3 ligases, as required for p27 ubiquitination.
Using yeast E3 ligase knockout extracts, the authors first identified Rsp5p, the yeast homolog of mammalian Nedd4 family E3 ligases, as required for p27 ubiquitination. Overexpression of individual Nedd4 family members in mammalian cells revealed that SMURF1 stabilizes p27, while knockdown of SMURF1 reduces p27 levels. In vitro ubiquitination reactions confirmed SMURF1 modifies p27 with K29-linked chains. AlphaFold modeling predicted sequential binding of UbcH7 and p27 to the SMURF1 HECT domain.