Search Within
Applied Filters:
Keyword:'camkp'
Showing 1-15 of 15 results for "

camkp

" within Papers
Noriyuki Sueyoshi et al.
Biochemical and biophysical research communications, 363(3), 715-721 (2007-09-28)
Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaMKP) and its nuclear isoform CaMKP-N are unique Ser/Thr protein phosphatases that negatively regulate the Ca(2+)/calmodulin-dependent protein kinase (CaMK) cascade by dephosphorylating multifunctional CaMKI, II, and IV. However, the lack of specific inhibitors of these phosphatases...
Masayuki Takeuchi et al.
Journal of biochemistry, 136(2), 183-188 (2004-10-22)
Calmodulin-dependent protein kinase phosphatase (CaMKP) and CaMKP-N dephosphorylate and regulate multifunctional Ca(2+)/calmodulin-dependent protein kinases. The enzymatic properties of CaMKP-N and CaMKP resemble each other, whereas their localizations are different. CaMKP-N is localized in the nucleus, whereas CaMKP is localized in...
M Takeuchi et al.
Journal of biochemistry, 130(6), 833-840 (2001-12-01)
Calmodulin-dependent protein kinase phosphatase (CaMKP) dephosphorylates and concomitantly deactivates multifunctional Ca(2+)/calmodulin-dependent protein kinases (CaMKs), such as CaMKI, CaMKII, and CaMKIV. In the present study, a nuclear CaMKP-related protein, CaMKP-N, was identified. This protein consisted of 757 amino acid residues with...
Yukiyo Tada et al.
Archives of biochemistry and biophysics, 452(2), 174-185 (2006-07-18)
Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaMKP) is a member of the serine/threonine protein phosphatases and shares 29% sequence identity with protein phosphatase 2Calpha (PP2Calpha) in its catalytic domain. To investigate the functional domains of CaMKP, mutational analysis was carried out using...
Hiromi Baba et al.
Archives of biochemistry and biophysics, 526(1), 9-15 (2012-06-30)
Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaMKP/PPM1F) is a Ser/Thr protein phosphatase that dephosphorylates and regulates multifunctional Ca(2+)/calmodulin-dependent protein kinases. Although CaMKP is known to be activated by phosphorylation with CaMKII and stimulated by the addition of polycations such as poly-l-lysine, detailed...
Noriyuki Sueyoshi et al.
Archives of biochemistry and biophysics, 488(1), 48-59 (2009-06-17)
Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaMKP) dephosphorylates and regulates multifunctional Ca(2+)/calmodulin-dependent protein kinases (CaMKs). However, the biological functions of this enzyme have not been clarified in vivo. To investigate the biological significance of CaMKP during zebrafish embryogenesis, we cloned and characterized...
Miresta Prévilon et al.
PloS one, 9(6), e90822-e90822 (2014-03-13)
Ca2+/calmodulin-dependent protein kinase phosphatase (CaMKP) has been proposed as a potent regulator of multifunctional Ca2+/calmodulin-dependent protein kinases (i.e., CaMKII). The CaMKII-dependent activation of myocyte enhancer factor 2 (MEF2) disrupts interactions between MEF2-histone deacetylases (HDACs), thereby de-repressing downstream gene transcription. Whether...
Takashi Onouchi et al.
Biochemical and biophysical research communications, 422(4), 703-709 (2012-05-26)
Nuclear Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaMKP-N/PPM1E) is an enzyme that dephosphorylates and downregulates multifunctional Ca(2+)/calmodulin-dependent protein kinases (CaMKs) as well as AMP-dependent protein kinase. In our previous study, we found that zebrafish CaMKP-N (zCaMKP-N) underwent proteolytic processing and translocated to...
Noriyuki Sueyoshi et al.
Archives of biochemistry and biophysics, 517(1), 43-52 (2011-11-22)
Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaMKP) and its nuclear homolog CaMKP-N are Ser/Thr protein phosphatases that belong to the PPM family. These phosphatases are highly specific for multifunctional CaM kinases and negatively regulate their activities. CaMKP-N is only expressed in the...
Atsuhiko Ishida et al.
Archives of biochemistry and biophysics, 435(1), 134-146 (2005-02-01)
Ca(2+)/calmodulin-dependent protein kinase phosphatase (CaMKP) is a unique protein phosphatase that specifically dephosphorylates and regulates multifunctional Ca(2+)/calmodulin-dependent protein kinases (CaMKs). To clarify the physiological significance of CaMKP, we identified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and fructose bisphosphate aldolase as major binding partners...
A Ishida et al.
British journal of pharmacology, 154(4), 729-740 (2008-05-06)
Multifunctional Ca2+/calmodulin-dependent protein kinases (CaMKs) play pivotal roles in intracellular Ca2+ signaling pathways. There is growing evidence that CaMKs are involved in the pathogenic mechanisms underlying various human diseases. In this review, we begin by briefly summarizing our knowledge of...
Takaki Nimura et al.
Archives of biochemistry and biophysics, 457(2), 205-216 (2006-12-16)
Nuclear Ca2+/calmodulin-dependent protein kinase phosphatase (CaMKP-N) is an enzyme that dephosphorylates and concomitantly downregulates multifunctional Ca2+/calmodulin-dependent protein kinases (CaMKs) in vitro. However, the functional roles of this enzyme in vivo are not well understood. To investigate the biological significance of...
Isamu Kameshita et al.
Analytical biochemistry, 400(1), 118-122 (2010-01-05)
We developed a method for the detection of phosphatase activity using fluorogenic substrates after polyacrylamide gel electrophoresis. When phosphatases such as Ca2+/calmodulin-dependent protein kinase phosphatase (CaMKP), protein phosphatase 2C (PP2C), protein phosphatase 5 (PP5), and alkaline phosphatase were resolved by...
Takaki Nimura et al.
Journal of biochemistry, 147(6), 857-865 (2010-03-02)
Ca(2+)/calmodulin-dependent protein kinase (CaMK) IV is a multifunctional Ser/Thr protein kinase that is predominantly expressed in the nuclei of neurons. CaMKIV consists of a catalytic domain and a regulatory (Ca(2+)/calmodulin binding and autoinhibitory) domain, which are located in the N-terminal...
Juan Tang et al.
Oncotarget, 6(33), 34831-34845 (2015-10-27)
Oscillations in intracellular Ca2+ concentrations ([Ca2+]i) mediate various cellular function. Although it is known that [Ca2+]i oscillations are susceptible to dysregulation in tumors, the tumor-specific regulators of [Ca2+]i oscillations are poorly characterized. We discovered that CD147 promotes hepatocellular carcinoma (HCC)...
Page 1 of 1
Page 1 of 1