2018
Global phosphoproteomic analysis identifies SRMS-regulated secondary signaling intermediates
Goel RK, Meyer M, Paczkowska M, Reimand J, Vizeacoumar F, Vizeacoumar F, Lam TT, Lukong KE. Global phosphoproteomic analysis identifies SRMS-regulated secondary signaling intermediates. Proteome Science 2018, 16: 16. PMID: 30140170, PMCID: PMC6098843, DOI: 10.1186/s12953-018-0143-7.Peer-Reviewed Original ResearchGlobal phosphoproteomic analysisPhosphoproteomic analysisCellular processesSignaling intermediatesTyrosine kinaseNon-receptor tyrosine kinaseCasein kinase 2 alphaDNA repair pathwaysBRK familyPotential kinasesSubstrate proteinsPhosphorylation dynamicsUpregulated phosphositesSrc familyBioinformatics analysisRepair pathwaysBioinfomatic analysisCandidate substratesBiological processesApoptotic pathwayKinaseIndirect regulationDatabase searchingPhosphoproteomeAnalysis of motives
2017
Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition
Musante V, Li L, Kanyo J, Lam TT, Colangelo CM, Cheng SK, Brody AH, Greengard P, Le Novère N, Nairn AC. Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition. ELife 2017, 6: e24998. PMID: 28613156, PMCID: PMC5515580, DOI: 10.7554/elife.24998.Peer-Reviewed Original ResearchConceptsARPP-16ARPP-19Protein phosphatase 2A inhibitionProtein phosphatase PP2A.Inhibition of PP2ASwitch-like responseKinase inhibitsPhosphatase PP2A.Regulatory interactionsPKA phosphorylationAntagonistic interplayReciprocal regulationBasal phosphorylationPhosphorylationMAST3PP2APKAENSAKinaseStriatal signalingPP2A.Multiple sitesInhibitionMitosisSignaling