2010
Deciphering Protein Kinase Specificity Through Large-Scale Analysis of Yeast Phosphorylation Site Motifs
Mok J, Kim PM, Lam HY, Piccirillo S, Zhou X, Jeschke GR, Sheridan DL, Parker SA, Desai V, Jwa M, Cameroni E, Niu H, Good M, Remenyi A, Nianhan J, Sheu YJ, Sassi HE, Sopko R, Chan CS, De Virgilio C, Hollingsworth NM, Lim WA, Stern DF, Stillman B, Andrews BJ, Gerstein MB, Snyder M, Turk BE. Deciphering Protein Kinase Specificity Through Large-Scale Analysis of Yeast Phosphorylation Site Motifs. Science Signaling 2010, 3: ra12. PMID: 20159853, PMCID: PMC2846625, DOI: 10.1126/scisignal.2000482.Peer-Reviewed Original ResearchConceptsPhosphorylation site motifsSite motifShort linear sequence motifsKinase substrate recognitionKinase-substrate relationshipsProtein kinase specificityKinase catalytic domainLinear sequence motifsPrediction of thousandsCMGC groupKinase specificityPhosphorylation targetsKinase substrateYeast proteomeSequence motifsSubstrate recognitionKinase familyProtein substratesCatalytic domainProtein kinaseLarge-scale analysisPrimary sequenceCandidate substratesComputational scanningKinase
2003
FHA Domain-Mediated DNA Checkpoint Regulation of Rad53
Schwartz MF, Lee SJ, Duong JK, Eminaga S, Stern DF. FHA Domain-Mediated DNA Checkpoint Regulation of Rad53. Cell Cycle 2003, 2: 381-394. PMID: 12851493, DOI: 10.4161/cc.2.4.457.Peer-Reviewed Original ResearchConceptsDNA damage checkpoint pathwayDamage checkpoint pathwayFHA domainReplication blocksCheckpoint pathwayChromatin assembly factor Asf1Phosphorylation-dependent associationDNA damageDNA replication checkpointActivation of Rad53Phosphopeptide binding domainsReplication checkpointReplicational stressDNA checkpointCheckpoint defectRad53Checkpoint regulationCatalytic domainProtein kinaseFHA1Binding domainsAsf1FHA2Persistent activationPathway
2002
Chk2 Activation and Phosphorylation-Dependent Oligomerization
Xu X, Tsvetkov LM, Stern DF. Chk2 Activation and Phosphorylation-Dependent Oligomerization. Molecular And Cellular Biology 2002, 22: 4419-4432. PMID: 12024051, PMCID: PMC133858, DOI: 10.1128/mcb.22.12.4419-4432.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAtaxia Telangiectasia Mutated ProteinsBinding SitesCell Cycle ProteinsCell-Free SystemCells, CulturedCheckpoint Kinase 2DNA DamageDNA-Binding ProteinsEnzyme ActivationFibroblastsGenes, Tumor SuppressorHumansMutationPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiaryRabbitsRadiation, IonizingRecombinant ProteinsSignal TransductionTumor Suppressor ProteinsConceptsSQ/TQ cluster domainsChk2 activationDNA damageDNA damage checkpoint pathwaySerine/threonine kinaseAutophosphorylation of Chk2Phosphorylation-dependent oligomerizationDamage checkpoint pathwayKinase catalytic domainForkhead-associated (FHA) domainWortmannin-sensitive kinaseChk2 kinase activityLimited DNA damageAmino acid substitutionsCell-free systemEukaryotic proteinsFHA domainActive Chk2Threonine kinaseCheckpoint functionCatalytic domainOligomeric complexesCheckpoint pathwayKinase activityChk2