Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding.

@article{Shani2001AutophosphorylationRT,
  title={Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding.},
  author={Gidi Shani and Sivan Henis-Korenblit and Ghil Jona and Opher Gileadi and Miriam Eisenstein and Tamar Ziv and Arie Admon and Adi Kimchi},
  journal={The EMBO journal},
  year={2001},
  volume={20 5},
  pages={1099-113}
}
DRP-1 is a pro-apoptotic Ca2+/calmodulin (CaM)-regulated serine/threonine kinase, recently isolated as a novel member of the DAP-kinase family of proteins. It contains a short extra-catalytic tail required for homodimerization. Here we identify a novel regulatory mechanism that controls its pro-apoptotic functions. It comprises a single autophosphorylation event mapped to Ser308 within the CaM regulatory domain. A negative charge at this site reduces both the binding to CaM and the formation of… CONTINUE READING