Reactome | SMURF1 ubiquitinates RHOA

SMURF1 ubiquitinates RHOA

Stable Identifier

R-HSA-2160935

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cell junction, cytosol, plasma membrane

ReviewStatus

5/5

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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
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