Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase.

@article{Peng2004UbiquitylationON,
  title={Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase.},
  author={H Peng and Yoshihiro Morishima and Gary J. Jenkins and Anwar Y. Dunbar and Miranda Lau and C. G. Patterson and William A B Pratt and Yoichi Osawa},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 51},
  pages={52970-7}
}
It is established that neuronal nitric-oxide synthase (nNOS) is ubiquitylated and proteasomally degraded. The proteasomal degradation of nNOS is enhanced by suicide inactivation of nNOS or by the inhibition of hsp90, which is a chaperone found in a native complex with nNOS. In the current study, we have examined whether CHIP, a chaperone-dependent E3 ubiquitin-protein isopeptide ligase that is known to ubiquitylate other hsp90-chaperoned proteins, could act as an ubiquitin ligase for nNOS. We… CONTINUE READING