2007
Phosphorylation at Ser244 by CK1 determines nuclear localization and substrate targeting of PKD2
von Blume J, Knippschild U, Dequiedt F, Giamas G, Beck A, Auer A, Van Lint J, Adler G, Seufferlein T. Phosphorylation at Ser244 by CK1 determines nuclear localization and substrate targeting of PKD2. The EMBO Journal 2007, 26: 4619-4633. PMID: 17962809, PMCID: PMC2080801, DOI: 10.1038/sj.emboj.7601891.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCasein Kinase 1 epsilonCasein Kinase IdeltaCell LineCell Line, TumorCell NucleusChlorocebus aethiopsCOS CellsDNA-Binding ProteinsGastrinsHeLa CellsHistone DeacetylasesHumansNuclear Receptor Subfamily 4, Group A, Member 1PhosphorylationProtein Kinase CProtein Kinase D2Protein KinasesReceptor, Cholecystokinin BReceptors, Cytoplasmic and NuclearReceptors, SteroidSerineTranscription FactorsConceptsProtein kinase D2Nuclear accumulationEfficient phosphorylationCritical post-translational modificationSerine/threonine kinaseZinc finger domainPost-translational modificationsSignal transduction pathwaysG protein-coupled receptorsHuman gastric cancer cellsExport machinerySubstrate targetingHDAC7 phosphorylationActivation loopNuclear substratesThreonine kinaseActive kinaseNuclear exportGastric cancer cellsSubcellular compartmentsTransduction pathwaysNuclear localizationPKD familyPKC etaPhosphorylation
2005
Role of the Regulatory Domain of Protein Kinase D2 in Phorbol Ester Binding, Catalytic Activity, and Nucleocytoplasmic Shuttling
Auer A, von Blume J, Sturany S, von Wichert G, Van Lint J, Vandenheede J, Adler G, Seufferlein T. Role of the Regulatory Domain of Protein Kinase D2 in Phorbol Ester Binding, Catalytic Activity, and Nucleocytoplasmic Shuttling. Molecular Biology Of The Cell 2005, 16: 4375-4385. PMID: 15975900, PMCID: PMC1196345, DOI: 10.1091/mbc.e05-03-0251.Peer-Reviewed Original Research