Degradation of RhoA by Smurf1 ubiquitin ligase.

@article{Wang2006DegradationOR,
  title={Degradation of RhoA by Smurf1 ubiquitin ligase.},
  author={Hong-rui Wang and Abiodun A. Ogunjimi and Yue Zhang and Barish Ozdamar and Rohit Bose and Jeffrey L. Wrana},
  journal={Methods in enzymology},
  year={2006},
  volume={406},
  pages={437-47}
}
The Rho family of small GTPases plays a key role in the dynamic regulation of the actin cytoskeleton that underlies various important cellular functions such as shape changes, migration, and polarity. We found that Smurf1, a HECT domain E3 ubiquitin ligase, could specifically target RhoA but not Cdc42 or Rac1 for degradation. Smurf1 interacts with the dominant inactive form of RhoA, RhoA N19, which binds constitutively to guanine nucleotide exchange factors (GEFs) in vivo. Smurf1 also interacts… CONTINUE READING