2006
Stimulation of Gαq-coupled M1 muscarinic receptor causes reversible spectrin redistribution mediated by PLC, PKC and ROCK
Street M, Marsh SJ, Stabach PR, Morrow JS, Brown DA, Buckley NJ. Stimulation of Gαq-coupled M1 muscarinic receptor causes reversible spectrin redistribution mediated by PLC, PKC and ROCK. Journal Of Cell Science 2006, 119: 1528-1536. PMID: 16551696, DOI: 10.1242/jcs.02872.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntineoplastic Combined Chemotherapy ProtocolsCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCricetinaeCyclophosphamideDoxorubicinGTP-Binding Protein alpha Subunits, Gq-G11Intracellular Signaling Peptides and ProteinsProtein Kinase CProtein Serine-Threonine KinasesReceptor, Muscarinic M1Receptors, MuscarinicRho-Associated KinasesSignal TransductionSpectrinType C PhospholipasesVincristineConceptsG protein-coupled receptorsAlphaII-spectrinSpecialized plasma membrane domainsPlasma membrane domainsIntact actin cytoskeletonStimulation of GPCRsProtein kinase CExtracellular stimuliActin cytoskeletonProtein complexesM1 muscarinic receptorsMembrane domainsMembrane blebbingPlasma membraneCytoskeletal proteinsKinase ROCKMolecular mechanismsConstitutive activationKinase CCellular localizationGlobal rearrangementsPhospholipase CSpectrinCHO cellsReversible redistribution
2005
Neutrophils Lacking Platelet-Endothelial Cell Adhesion Molecule-1 Exhibit Loss of Directionality and Motility in CXCR2-Mediated Chemotaxis
Wu Y, Stabach P, Michaud M, Madri JA. Neutrophils Lacking Platelet-Endothelial Cell Adhesion Molecule-1 Exhibit Loss of Directionality and Motility in CXCR2-Mediated Chemotaxis. The Journal Of Immunology 2005, 175: 3484-3491. PMID: 16148090, DOI: 10.4049/jimmunol.175.6.3484.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell ShapeChemokine CXCL1ChemokinesChemokines, CXCChemotaxis, LeukocyteCytokinesInterleukin-8Intracellular Signaling Peptides and ProteinsMiceMice, KnockoutNeutrophilsPlatelet Endothelial Cell Adhesion Molecule-1Protein Phosphatase 1Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesReceptors, Interleukin-8BConceptsCell motilitySrc homology 2 domainF-actinSHP-1 phosphatase activityWild-type neutrophilsF-actin polymerizationPhosphatase 1Time-lapse videomicroscopyPECAM-1Cytokine-induced mobilizationPhosphatase activityExhibit lossMurine neutrophilsMotilityChemotaxisZigmond chamberCellsPECAMLeading frontCytoskeletonMoesinIL-8FMLP gradientProteinActin
1998
Utilization of an 86bp exon generates a novel adducin isoform (β4) lacking the MARCKS homology domain1The first two authors contributed equally to this work.1
Sinard J, Stewart G, Stabach P, Argent A, Gilligan D, Morrow J. Utilization of an 86bp exon generates a novel adducin isoform (β4) lacking the MARCKS homology domain1The first two authors contributed equally to this work.1. Biochimica Et Biophysica Acta 1998, 1396: 57-66. PMID: 9524222, DOI: 10.1016/s0167-4781(97)00167-x.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceBase SequenceCalmodulin-Binding ProteinsCloning, MolecularExonsHumansIntracellular Signaling Peptides and ProteinsIsomerismMembrane ProteinsMolecular Sequence DataMyristoylated Alanine-Rich C Kinase SubstrateOrgan SpecificityPolymerase Chain ReactionProtein Structure, TertiaryProteinsSequence Homology, Amino AcidSequence Homology, Nucleic AcidTranscription, GeneticConceptsNovel amino acidAmino acidsBeta-adducinNew isoformHuman bone marrow cDNA libraryBone marrow cDNA libraryDifferent reading framesCalcium/calmodulinLysine-rich sequenceNT-2 cellsProtein kinase CGenomic clonesGenomic mapNew amino acidsAlternate exonsActin crossCDNA libraryReading frameSplice consensus sequenceNew exonsNovel isoformConsensus sequenceStop codonKinase CExons