2020
Signalling through cerebral cavernous malformation protein networks
Su VL, Calderwood DA. Signalling through cerebral cavernous malformation protein networks. Open Biology 2020, 10: 200263. PMID: 33234067, PMCID: PMC7729028, DOI: 10.1098/rsob.200263.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiomarkersCarrier ProteinsDisease ManagementDisease SusceptibilityGenetic Predisposition to DiseaseHemangioma, Cavernous, Central Nervous SystemHumansIntracellular SpaceMutationProtein BindingProtein Interaction Domains and MotifsProtein Interaction MappingProtein Interaction MapsProtein TransportSignal TransductionConceptsCCM proteinsCerebral cavernous malformationsCell junctionalMEKK3-MEK5Protein complexesAdaptor proteinProtein functionSubcellular localizationCytoskeletal reorganizationComplex proteinsProtein networkRhoA-ROCKMolecular basisProtein activityGene expressionFunction mutationsCell adhesionCell contractilityProteinPathwayLeaky blood vesselsCurrent knowledgeDisease pathologyCdc42Recent advancesSerine phosphorylation of the small phosphoprotein ICAP1 inhibits its nuclear accumulation
Su VL, Simon B, Draheim KM, Calderwood DA. Serine phosphorylation of the small phosphoprotein ICAP1 inhibits its nuclear accumulation. Journal Of Biological Chemistry 2020, 295: 3269-3284. PMID: 32005669, PMCID: PMC7062153, DOI: 10.1074/jbc.ra119.009794.Peer-Reviewed Original ResearchConceptsIntegrin cytoplasmic domain-associated protein-1N-terminal regionNuclear accumulationP21-activated kinase 4Ser-10Nuclear roleSerine phosphorylationNuclear localizationPhosphorylation-mimicking substitutionsNuclear localization signalCell-cell junctionsSer-25Localization signalKRIT1 functionThreonine residuesAdaptor proteinKRIT1 lossSubcellular localizationNeurovascular dysplasiaBlood vessel integrityVascular developmentKinase 4Cultured cellsPhosphorylationProtein 1
2019
The subcellular localization of type I p21-activated kinases is controlled by the disordered variable region and polybasic sequences
Sun X, Su VL, Calderwood DA. The subcellular localization of type I p21-activated kinases is controlled by the disordered variable region and polybasic sequences. Journal Of Biological Chemistry 2019, 294: 14319-14332. PMID: 31391252, PMCID: PMC6768646, DOI: 10.1074/jbc.ra119.007692.Peer-Reviewed Original ResearchConceptsCell-cell contactCell-cell junctionsPolybasic sequenceP21-activated kinaseSmall GTPases RacVariable regionsCell-cell boundariesPAK regulationDomain organizationCdc42 bindingAdhesion dynamicsCRIB domainGTPases RacSubcellular localizationTruncation mutantsKinase domainKinase effectorsCellular signalsExtensive similaritySequence regionsPAK1Cell adhesionCdc42PAKKinase
2013
ASB2α, an E3 Ubiquitin Ligase Specificity Subunit, Regulates Cell Spreading and Triggers Proteasomal Degradation of Filamins by Targeting the Filamin Calponin Homology 1 Domain*
Razinia Z, Baldassarre M, Cantelli G, Calderwood DA. ASB2α, an E3 Ubiquitin Ligase Specificity Subunit, Regulates Cell Spreading and Triggers Proteasomal Degradation of Filamins by Targeting the Filamin Calponin Homology 1 Domain*. Journal Of Biological Chemistry 2013, 288: 32093-32105. PMID: 24052262, PMCID: PMC3814802, DOI: 10.1074/jbc.m113.496604.Peer-Reviewed Original ResearchConceptsHematopoietic cell differentiationSpecificity subunitProteasomal degradationF-actin-rich structuresE3 ubiquitin ligase complexCell differentiationNormal subcellular localizationHomology 1 domainLoss of filaminUbiquitin acceptor sitesActin-binding domainCross-linking proteinsActin-binding siteLigase complexActin cytoskeletonTransmembrane proteinSubcellular localizationΑ-actinin1Transient expressionASB2αDegradation of filaminMinimal fragmentLysine residuesFilaminCell adhesion
2011
The E3 ubiquitin ligase specificity subunit ASB2α targets filamins for proteasomal degradation by interacting with the filamin actin-binding domain
Razinia Z, Baldassarre M, Bouaouina M, Lamsoul I, Lutz PG, Calderwood DA. The E3 ubiquitin ligase specificity subunit ASB2α targets filamins for proteasomal degradation by interacting with the filamin actin-binding domain. Journal Of Cell Science 2011, 124: 2631-2641. PMID: 21750192, PMCID: PMC3138704, DOI: 10.1242/jcs.084343.Peer-Reviewed Original ResearchConceptsFilamin degradationProteasomal degradationCell differentiationDomain of filaminActin-rich structuresUbiquitin-proteasome pathwayExtracellular matrix connectionsActin cytoskeletonTransmembrane proteinSubcellular localizationMolecular basisSignaling cascadesASB2αActin filamentsFilaminAcute degradationBiochemical assaysMyeloid leukemia cellsImportant familyActinEarly eventsProteinLeukemia cellsImportant mechanismDifferentiation
2001
PEA-15 Mediates Cytoplasmic Sequestration of ERK MAP Kinase
Formstecher E, Ramos J, Fauquet M, Calderwood D, Hsieh J, Canton B, Nguyen X, Barnier J, Camonis J, Ginsberg M, Chneiweiss H. PEA-15 Mediates Cytoplasmic Sequestration of ERK MAP Kinase. Developmental Cell 2001, 1: 239-250. PMID: 11702783, DOI: 10.1016/s1534-5807(01)00035-1.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsActive Transport, Cell NucleusAmino Acid SequenceAnimalsApoptosis Regulatory ProteinsBlotting, NorthernCell DivisionCell NucleusCell SurvivalCHO CellsCricetinaeCytoplasmDNA, ComplementaryDose-Response Relationship, DrugGreen Fluorescent ProteinsImmunohistochemistryLuminescent ProteinsMAP Kinase Signaling SystemMiceMicroscopy, FluorescenceMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesModels, BiologicalMolecular Sequence DataMutationPhosphoproteinsPrecipitin TestsProtein BindingSequence Homology, Amino AcidTime FactorsTranscription, GeneticTransfectionTwo-Hybrid System TechniquesConceptsERK MAP kinasePEA-15MAP kinaseERK nuclear localizationNuclear export sequenceERK-dependent transcriptionMAP kinase pathwayMultiple cell typesERK 1/2 MAP kinase pathwayExport sequenceSubcellular localizationNuclear localizationCytoplasmic sequestrationKinase pathwayIntegrin functionCell typesCell growthKinaseBiological outcomesCell proliferationGenetic deletionTranscriptionERKLocalizationProliferation