Phosphorylation and activation of nuclear Ca2+/calmodulin-dependent protein kinase phosphatase (CaMKP-N/PPM1E) by Ca2+/calmodulin-dependent protein kinase I (CaMKI)

Article ID	Journal	Published Year	Pages	File Type
10760721	Biochemical and Biophysical Research Communications	2012	7 Pages	PDF

Abstract

âº CaMKP-N/PPM1E underwent proteolytic processing and translocated to cytosol. âº The proteolysis was effectively inhibited by the proteasome inhibitors. âº Ser-480 of zebrafish CaMKP-N was phosphorylated by cytosolic CaMKI. âº Phosphorylation-mimic mutants of CaMKP-N showed enhanced activity. âº These results suggest that CaMKP-N is regulated by CaMKI.

Keywords

CaMK NLS MUP 4-methylumbelliferyl phosphate Translocation CAM nuclear localization signal Protein phosphorylation Proteolytic processing Ca2+/calmodulin-dependent protein kinase Calmodulin CaM kinase