GCP60 preferentially interacts with a caspase-generated golgin-160 fragment.

@article{Sbodio2006GCP60PI,
  title={GCP60 preferentially interacts with a caspase-generated golgin-160 fragment.},
  author={Juan I. Sbodio and Stuart W. Hicks and Dan Simon and Carolyn E. Machamer},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 38},
  pages={27924-31}
}
Golgin-160, a ubiquitous protein in vertebrates, localizes to the cytoplasmic face of the Golgi complex. Golgin-160 has a large coiled-coil C-terminal domain and a non-coiled-coil N-terminal ("head") domain. The head domain contains important motifs, including a nuclear localization signal, a Golgi targeting domain, and three aspartates that are recognized by caspases during apoptosis. Some of the caspase cleavage products accumulate in the nucleus when overexpressed. Expression of a non… CONTINUE READING