2018
Abl2 is recruited to ventral actin waves through cytoskeletal interactions to promote lamellipodium extension
Zhang K, Lyu W, Yu J, Koleske AJ. Abl2 is recruited to ventral actin waves through cytoskeletal interactions to promote lamellipodium extension. Molecular Biology Of The Cell 2018, 29: 2863-2873. PMID: 30256707, PMCID: PMC6249870, DOI: 10.1091/mbc.e18-01-0044.Peer-Reviewed Original ResearchConceptsCytoskeletal interactionsLamellipodium extensionTotal internal reflection fluorescence microscopyActin-rich structuresActin wavesActin-rich protrusionsN-terminal halfC-terminal halfNonreceptor tyrosine kinaseReflection fluorescence microscopyFoci colocalizeComplementation analysisLamellipodia protrusionKnockout cellsLamellipodium tipActin filament stabilizerCell shapeBind actinTyrosine kinaseCortactinABL2Fluorescence microscopyIntegrin β3High spatiotemporal resolutionPaxillin
2007
Integrin Cytoskeletal Interactions
Lad Y, Harburger DS, Calderwood DA. Integrin Cytoskeletal Interactions. Methods In Enzymology 2007, 426: 69-84. PMID: 17697880, DOI: 10.1016/s0076-6879(07)26004-5.Peer-Reviewed Original ResearchConceptsIntegrin cytoplasmic tailsCytoplasmic tailProtein-protein interaction studiesIntegrin-binding proteinsIntegrin adhesion receptorsCell-substratum adhesionCytoskeletal interactionsPlasma membraneCytoskeletal proteinsBiochemical signalsAdhesion receptorsIntracellular ligandsTail interactionsCellular activitiesIntegrin-cytoskeletal interactionsMechanical forcesRecombinant modelProteinInteraction studiesTailAdhesionInteractionRegulationDynamic interactionMembrane
2005
Lipid segregation and IgE receptor signaling: A decade of progress
Holowka D, Gosse J, Hammond A, Han X, Sengupta P, Smith N, Wagenknecht-Wiesner A, Wu M, Young R, Baird B. Lipid segregation and IgE receptor signaling: A decade of progress. Biochimica Et Biophysica Acta 2005, 1746: 252-259. PMID: 16054713, DOI: 10.1016/j.bbamcr.2005.06.007.Peer-Reviewed Original ResearchConceptsLipid raftsReceptor phosphorylationSrc family kinase LynTransmembrane tyrosine phosphataseLipid segregationPlasma membrane resultsIgE receptor signalingCell surface receptorsActive LynKinase LynTyrosine phosphataseCytoskeletal interactionsSignal transductionRaft environmentMembrane skeletonDisordered regionsReceptor signalingSurface receptorsSegregation of liquidIgE receptorMembrane structureLynPhosphorylationMembrane resultsComplex role
1994
An SH3 binding region in the epithelial Na+ channel (alpha rENaC) mediates its localization at the apical membrane.
Rotin D, Bar‐Sagi D, O'Brodovich H, Merilainen J, Lehto V, Canessa C, Rossier B, Downey G. An SH3 binding region in the epithelial Na+ channel (alpha rENaC) mediates its localization at the apical membrane. The EMBO Journal 1994, 13: 4440-4450. PMID: 7925286, PMCID: PMC395375, DOI: 10.1002/j.1460-2075.1994.tb06766.x.Peer-Reviewed Original ResearchConceptsC-terminal regionAlpha-spectrinSH3 domainCytoskeletal interactionsFusion proteinTerminal proline-rich regionAlpha-rENaCApical membranePolarized epithelial cellsProline-rich sequenceN-terminal proteinProline-rich regionEpithelial cellsApical membrane localizationCytoskeletal protein ankyrinProper channel functionPrimary rat alveolar epithelial cellsEpithelial cell lysatesMembrane localizationRat alveolar epithelial cellsProtein ankyrinApical localizationPlasma membraneRecombinant fusion proteinMolecular mechanisms
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