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 advances
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
2017
Novel ecto-tagged integrins reveal their trafficking in live cells
Huet-Calderwood C, Rivera-Molina F, Iwamoto DV, Kromann EB, Toomre D, Calderwood DA. Novel ecto-tagged integrins reveal their trafficking in live cells. Nature Communications 2017, 8: 570. PMID: 28924207, PMCID: PMC5603536, DOI: 10.1038/s41467-017-00646-w.Peer-Reviewed Original ResearchConceptsIntegrin functionΒ1 integrinLive cellsCell surface adhesion receptorsHeterodimeric cell-surface adhesion receptorsIntegrin endocytosisMulticellular organismsNovel powerful toolFocal adhesionsKnockout fibroblastsIntegrin activationAdhesion receptorsExtracellular loopIntegrinsTraffickingMajor mysteriesCellsTagsAdhesionHaloTagEndocytosisPowerful toolExocytosisOrganismsVesicles
2015
Regulation of integrin-mediated adhesions
Iwamoto DV, Calderwood DA. Regulation of integrin-mediated adhesions. Current Opinion In Cell Biology 2015, 36: 41-47. PMID: 26189062, PMCID: PMC4639423, DOI: 10.1016/j.ceb.2015.06.009.Peer-Reviewed Original ResearchConceptsIntegrin-mediated adhesionHeterodimeric transmembrane adhesion receptorsShort cytoplasmic tailTransmembrane adhesion receptorsSpecific intracellular proteinsClustering of integrinsMetazoan developmentActin cytoskeletonExtracellular ligandsCytoplasmic tailIntracellular traffickingExtracellular environmentIntracellular proteinsAdhesion receptorsAdhesive structuresIntegrin receptorsCell membraneRelay signalsIntegrinsEssential roleMechanical forcesCell attachmentAdhesionRecent advancesCytoskeletonPAK6 targets to cell–cell adhesions through its N-terminus in a Cdc42-dependent manner to drive epithelial colony escape
Morse EM, Sun X, Olberding JR, Ha BH, Boggon TJ, Calderwood DA. PAK6 targets to cell–cell adhesions through its N-terminus in a Cdc42-dependent manner to drive epithelial colony escape. Journal Of Cell Science 2015, 129: 380-393. PMID: 26598554, PMCID: PMC4732285, DOI: 10.1242/jcs.177493.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigens, CDCadherinsCdc42 GTP-Binding ProteinCell AdhesionCell Line, TumorEpithelial CellsHEK293 CellsHumansIntercellular JunctionsMolecular Sequence DataP21-Activated KinasesProtein BindingProtein Interaction Domains and MotifsProtein Sorting SignalsProtein TransportConceptsCell-cell adhesionN-terminusCdc42/Rac interactive binding (CRIB) domainSerine/threonine kinaseP21-activated kinase (PAK) familyCdc42-dependent mannerPolybasic regionThreonine kinaseCdc42 knockdownKinase familyBinding domainsKinase activityImportant regulatorCell adhesionPAK6Broader rolePAKAdhesionTargetingCdc42PAK1KinaseKnockdownRegulatorMutations
2014
TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly
Uchil PD, Pawliczek T, Reynolds TD, Ding S, Hinz A, Munro JB, Huang F, Floyd RW, Yang H, Hamilton WL, Bewersdorf J, Xiong Y, Calderwood DA, Mothes W. TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly. Journal Of Cell Science 2014, 127: 3928-3942. PMID: 25015296, PMCID: PMC4163643, DOI: 10.1242/jcs.143537.Peer-Reviewed Original ResearchConceptsFocal adhesion proteinsFocal adhesionsCell migrationAdhesion proteinsMulti-adaptor proteinTripartite motif (TRIM) protein familyFocal adhesion dynamicsFocal adhesion turnoverFocal adhesion componentsCoiled-coil domainImpaired cell migrationII-independent mannerLD2 motifAdhesion turnoverActin cytoskeletonProtein familyAdhesion dynamicsCellular functionsDynamic turnoverMacromolecular complexesRegulatory componentsFocal contactsAdhesion componentsExtracellular matrixTRIM15
2012
FAK promotes recruitment of talin to nascent adhesions to control cell motility
Lawson C, Lim ST, Uryu S, Chen XL, Calderwood DA, Schlaepfer DD. FAK promotes recruitment of talin to nascent adhesions to control cell motility. Journal Of Cell Biology 2012, 196: 223-232. PMID: 22270917, PMCID: PMC3265949, DOI: 10.1083/jcb.201108078.Peer-Reviewed Original ResearchConceptsFocal adhesion kinaseNascent adhesionsCell motilityCell migrationRecruitment of talinCytoskeletal protein talinTension-independent mannerCytoskeletal-associated proteinDirect binding siteTalin associationProtein talinFAK recruitmentAdhesion dynamicsAdhesion kinaseFAK localizationTalinAdhesion sitesTalin cleavageIntegrin receptorsΒ1 integrinPoint mutationsNew adhesionsBinding sites
2009
The Role of FilGAP-Filamin A Interactions in Mechanoprotection
Shifrin Y, Arora PD, Ohta Y, Calderwood DA, McCulloch CA. The Role of FilGAP-Filamin A Interactions in Mechanoprotection. Molecular Biology Of The Cell 2009, 20: 1269-1279. PMID: 19144823, PMCID: PMC2649276, DOI: 10.1091/mbc.e08-08-0872.Peer-Reviewed Original Research