2012
Structural Basis for Paxillin Binding and Focal Adhesion Targeting of β-Parvin*
Stiegler AL, Draheim KM, Li X, Chayen NE, Calderwood DA, Boggon TJ. Structural Basis for Paxillin Binding and Focal Adhesion Targeting of β-Parvin*. Journal Of Biological Chemistry 2012, 287: 32566-32577. PMID: 22869380, PMCID: PMC3463362, DOI: 10.1074/jbc.m112.367342.Peer-Reviewed Original ResearchConceptsΒ-parvinFocal adhesionsPaxillin bindingΑ-parvinFocal adhesion targetingN-terminal α-helixPaxillin LD1 motifCalponin homology domainFirst molecular detailsHigh sequence similarityCytoplasmic adaptor proteinIntegrin-linked kinasePaxillin LD1Co-crystal structureLD4 motifSignificant conformational flexibilityHomology domainAdaptor proteinCellular functionsSequence similarityRepeat motifsProper localizationMolecular detailsPaxillinStructural basis
2002
A Fragment of Paxillin Binds the α4Integrin Cytoplasmic Domain (Tail) and Selectively Inhibits α4-Mediated Cell Migration*
Liu S, Kiosses WB, Rose DM, Slepak M, Salgia R, Griffin JD, Turner CE, Schwartz MA, Ginsberg MH. A Fragment of Paxillin Binds the α4Integrin Cytoplasmic Domain (Tail) and Selectively Inhibits α4-Mediated Cell Migration*. Journal Of Biological Chemistry 2002, 277: 20887-20894. PMID: 11919182, DOI: 10.1074/jbc.m110928200.Peer-Reviewed Original ResearchConceptsCytoplasmic domainPaxillin interactionCell migrationIntegrin-mediated cell adhesionIntegrin alpha subunitsEnhanced cell migrationPaxillin bindingFunctional responseFocal adhesionsCellular functionsPaxillinCardiac developmentAlanine substitutionsMutational analysisAdaptor moleculeAcid regionAlpha subunitBiological processesCell spreadingCellular responsesCell adhesionIntegrin subunitsSubunitsTernary complexFragments
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