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http://purl.uniprot.org/citations/16314523http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16314523http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16314523http://www.w3.org/2000/01/rdf-schema#comment"NDR protein kinases are involved in the regulation of cell cycle progression and morphology. NDR1/NDR2 protein kinase is activated by phosphorylation on the activation loop phosphorylation site Ser281/Ser282 and the hydrophobic motif phosphorylation site Thr444/Thr442. Autophosphorylation of NDR is responsible for phosphorylation on Ser281/Ser282, whereas Thr444/Thr442 is targeted by an upstream kinase. Here we show that MST3, a mammalian Ste20-like protein kinase, is able to phosphorylate NDR protein kinase at Thr444/Thr442. In vitro, MST3 selectively phosphorylated Thr442 of NDR2, resulting in a 10-fold stimulation of NDR activity. MOB1A (Mps one binder 1A) protein further increased the activity, leading to a fully active kinase. In vivo, Thr442 phosphorylation after okadaic acid stimulation was potently inhibited by MST3KR, a kinase-dead mutant of MST3. Knockdown of MST3 using short hairpin constructs abolished Thr442 hydrophobic motif phosphorylation of NDR in HEK293F cells. We conclude that activation of NDR is a multistep process involving phosphorylation of the hydrophobic motif site Thr444/2 by MST3, autophosphorylation of Ser281/2, and binding of MOB1A."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.org/dc/terms/identifier"doi:10.1128/mcb.25.24.11019-11029.2005"xsd:string
http://purl.uniprot.org/citations/16314523http://purl.org/dc/terms/identifier"doi:10.1128/mcb.25.24.11019-11029.2005"xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/author"Hemmings B.A."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/author"Hemmings B.A."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/author"Hergovich A."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/author"Hergovich A."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/author"Bichsel S.J."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/author"Bichsel S.J."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/author"Stegert M.R."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/author"Stegert M.R."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/author"Tamaskovic R."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/author"Tamaskovic R."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/pages"11019-11029"xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/pages"11019-11029"xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/title"Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/title"Regulation of NDR protein kinase by hydrophobic motif phosphorylation mediated by the mammalian Ste20-like kinase MST3."xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/volume"25"xsd:string
http://purl.uniprot.org/citations/16314523http://purl.uniprot.org/core/volume"25"xsd:string