Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies

@article{Zhang2008SumoylationRL,
  title={Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies},
  author={Yu-qian Zhang and Kevin D. Sarge},
  journal={The Journal of Cell Biology},
  year={2008},
  volume={182},
  pages={35 - 39}
}
Lamin A mutations cause many diseases, including cardiomyopathies and Progeria Syndrome. The covalent attachment of small ubiquitin-like modifier (SUMO) polypeptides regulates the function of many proteins. Until now, no examples of human disease-causing mutations that occur within a sumoylation consensus sequence and alter sumoylation were known. We show that lamin A is sumoylated at lysine 201 and that two lamin A mutants associated with familial dilated cardiomyopathy, E203G and E203K… CONTINUE READING