SYVN1 ubiquitinates Hh C-terminal fragments

Stable Identifier
R-HSA-5362412
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

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).

Literature References
PubMed ID Title Journal Year
21357747 Processing and turnover of the Hedgehog protein in the endoplasmic reticulum

Chen, X, Tukachinsky, H, Huang, CH, Jao, C, Chu, YR, Tang, HY, Mueller, B, Schulman, S, Rapoport, TA, Salic, A

J. Cell Biol. 2011
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
ubiquitin-protein transferase activity of C-terminal Hh fragments:ERLEC/OS9:SEL1:SYVN1dimer:DERL2:VCP hexamer [endoplasmic reticulum membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed