SMURF1 ubiquitinates RHOA

Stable Identifier
R-HSA-2160935
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
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

SMURF1, recruited to tight junctions through association with phosphorylated PARD6A, ubiquitinates RHOA, leading to RHOA degradation and disassembly of tight junctions (Ozdamar et al. 2005). Disassembly of tight junctions is an important step in epithelial to mesenchymal transition. SMURF1, but not SMURF2, decreases RHOA level, and this effect is proteasome dependent (Wang et al. 2003).

Literature References
PubMed ID Title Journal Year
15761148 Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity

Barrios-Rodiles, M, Zhang, Y, Wrana, JL, Wang, HR, Bose, R, Ozdamar, B

Science 2005
14657501 Regulation of cell polarity and protrusion formation by targeting RhoA for degradation

Zhang, Y, Thomsen, GH, Wrana, JL, Wang, HR, Ogunjimi, AA, Ozdamar, B, Alexandrova, E

Science 2003
Participants
Participates
Orthologous Events
Authored
Reviewed
Created
Cite Us!