High impact information on Ppm1f

• These findings suggest that CaM kinase phosphatase N is involved in the regulation of not only CaM kinase IV but also CaM kinases II and I [1].
• Subcellular distributions of rat CaM kinase phosphatase N and other members of the CaM kinase regulatory system [2].
• Thus, the activity of CaMKPase appears to be regulated through phosphorylation by its target enzyme, CaMKII [3].
• Immunohistochemical study of the distribution of Ca(2+)/calmodulin-dependent protein kinase phosphatase in the rat central nervous system [4].
• Distribution of Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaM-K Pase) which dephosphorylate multifunctional Ca(2+)/calmodulin-dependent protein kinases (CaM-kinases) in the rat brain and spinal cord were examined immunohistochemically by using an antibody against this enzyme [4].

Biological context of Ppm1f

• In the present study, cDNA for CaM-kinase phosphatase was cloned from a rat brain cDNA library [5].
• Western blot analysis showed the ubiquitous tissue distribution of CaM-kinase phosphatase [5].
• Substrate specificity of Ca(2+)/calmodulin-dependent protein kinase phosphatase: kinetic studies using synthetic phosphopeptides as model substrates [6].

Anatomical context of Ppm1f

• In contrast, CaM kinase phosphatase N has been reported to occur almost exclusively in the brain and to be localized in the nucleus in the transfected COS-7 cells, as examined immunocytochemically with antibodies against the carboxyl-terminal segment of the enzyme, indicating its involvement in the deactivation of CaM kinase IV [1].

Associations of Ppm1f with chemical compounds

• CaMKPase was not significantly phosphorylated by CaMKII under the standard phosphorylation conditions but was phosphorylated in the presence of poly-L-lysine, which is a potent activator of CaMKPase [3].

References