YOD1 binds VCP

Stable Identifier
R-HSA-6781953
Type
Reaction [binding]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

YOD1 (OTU1) is a highly conserved deubiquitinating enzyme of the ovarian tumor (otubain) family. It forms a complex with Valosin containing protein (VCP, p97) that may participate in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins (Ernst et al. 2009, Kim et al. 2014). It may act by triming the ubiquitin chain on the associated substrate to facilitate their threading through the VCP/p97 pore. Ubiquitin moieties on substrates may present a steric impediment to the threading process when the substrate is transferred to the VCP pore and threaded through VCP's axial channel.

Literature References
PubMed ID Title Journal Year
19818707 The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER

Ernst, R, Mueller, B, Ploegh, HL, Schlieker, C

Mol. Cell 2009
24610782 Structural basis for ovarian tumor domain-containing protein 1 (OTU1) binding to p97/valosin-containing protein (VCP)

Kim, SJ, Cho, J, Song, EJ, Kim, SJ, Kim, HM, Lee, KE, Suh, SW, Kim, EE

J. Biol. Chem. 2014
Participants
Participant Of
Orthologous Events
Authored
Reviewed
Created