SMURF1 ubiquitinates RHOA

Stable Identifier
R-HSA-2160935
Type
Reaction [binding]
Species
Homo sapiens
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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
14657501 Regulation of cell polarity and protrusion formation by targeting RhoA for degradation

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

Science 2003
15761148 Regulation of the polarity protein Par6 by TGFbeta receptors controls epithelial cell plasticity

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

Science 2005
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