Synapsin I is phosphorylated at Ser603 by p21-activated kinases (PAKs) in vitro and in PC12 cells stimulated with bradykinin.

@article{Sakurada2002SynapsinII,
  title={Synapsin I is phosphorylated at Ser603 by p21-activated kinases (PAKs) in vitro and in PC12 cells stimulated with bradykinin.},
  author={Katsuhiko Sakurada and Hirotsugu Kato and Hiromitsu Nagumo and Hideji Hiraoka and Kaoru Furuya and Toshihiko Ikuhara and Yoshihiko Yamakita and Kouji Fukunaga and Eishichi Miyamoto and Fumio Matsumura and Y Matsuo and Yasuhito Naito and Yasuharu Sasaki},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 47},
  pages={45473-9}
}
The function of synapsin I is regulated by phosphorylation of the molecule at multiple sites; among them, the Ser(603) residue (site 3) is considered to be a pivotal site targeted by Ca(2+)/calmodulin-dependent kinase II (CaMKII). Although phosphorylation of the Ser(603) residue responds to several kinds of stimuli, it is unlikely that many or all of the stimuli activate the CaMKII-involved pathway. Among the several stimulants tested in PC12 cells, bradykinin evoked the phosphorylation of Ser… CONTINUE READING

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