SYVN1 ubiquitinates Hh-C as part of the retrotranslocon that targets these Hh fragments for degradation through the ERAD pathway. Both depletion of SYVN1 by siRNA and expression of a catalytically inactive form of the enzyme strongly inhibits Hh-C degradation. Consistent with this, a dominant negative version of SYVN1 abrogates the polyubiquitination of Hh-C as assessed by IP-Western from HEK293 cells (Chen et al, 2011).
Jao, C, Rapoport, TA, Tang, HY, Chu, YR, Schulman, S, Huang, CH, Chen, X, Salic, A, Mueller, B, Tukachinsky, H
ubiquitin-protein transferase activity of C-terminal Hh fragments:ERLEC/OS9:SEL1:SYVN1dimer:DERL2:VCP hexamer [endoplasmic reticulum membrane]
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