Site-specific phosphorylation of synapsin I by mitogen-activated protein kinase and Cdk5 and its effects on physiological functions.

@article{Matsubara1996SitespecificPO,
  title={Site-specific phosphorylation of synapsin I by mitogen-activated protein kinase and Cdk5 and its effects on physiological functions.},
  author={Mamoru Matsubara and Masashi Kusubata and Koichi Ishiguro and Tohru Uchida and Koiti Titani and Hisaaki Taniguchi},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 35},
  pages={21108-13}
}
Posttranslational modifications of synapsin I, a major phosphoprotein in synaptic terminals, were studied by mass spectrometry. In addition to a well known phosphorylation site by calmodulin-dependent protein kinase II (CaM kinase II), a hitherto unrecognized site (Ser553) was found phosphorylated in vivo. The phosphorylation site is immediately followed by a proline, suggesting that the protein is an in vivo substrate of so-called proline-directed protein kinase(s). To identify the kinase… CONTINUE READING