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http://purl.uniprot.org/citations/15003508http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15003508http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15003508http://www.w3.org/2000/01/rdf-schema#comment"The protein kinase C-potentiated inhibitor protein of 17kDa, called CPI-17, specifically inhibits myosin light chain phosphatase (MLCP). Phosphorylation of Thr-38 in vivo highly potentiates the ability of CPI-17 to inhibit MLCP. Thr-38 has been shown to be phosphorylated in vitro by a number of protein kinases including protein kinase C (PKC), Rho-associated coiled-coil kinase (ROCK), and protein kinase N (PKN). In this study we have focused on the association of protein kinases with CPI-17. Using affinity chromatography and Western blot analysis, we found interaction with all PKC isotypes and casein kinase I isoforms, CKIalpha and CKI. By contrast, ROCK and PKN did not associate with CPI-17, suggesting that PKC may be the relevant kinase that phosphorylates Thr-38 in vivo. CPI-17 interacted with the cysteine-rich domain of PKC and was phosphorylated by all PKC isotypes. We previously found that CPI-17 co-purified with casein kinase I in brain suggesting they are part of a complex and we now show that CPI-17 associates with the kinase domain of CKI isoforms."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2004.02.014"xsd:string
http://purl.uniprot.org/citations/15003508http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2004.02.014"xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/author"Aitken A."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/author"Aitken A."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/author"Dubois T."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/author"Dubois T."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/author"Zemlickova E."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/author"Zemlickova E."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/author"Johannes F.J."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/author"Johannes F.J."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/pages"39-47"xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/pages"39-47"xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/title"Association of CPI-17 with protein kinase C and casein kinase I."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/title"Association of CPI-17 with protein kinase C and casein kinase I."xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/volume"316"xsd:string
http://purl.uniprot.org/citations/15003508http://purl.uniprot.org/core/volume"316"xsd:string
http://purl.uniprot.org/citations/15003508http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15003508
http://purl.uniprot.org/citations/15003508http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15003508