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
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
1997
Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †
Stabach P, Cianci C, Glantz S, Zhang Z, Morrow J. Site-Directed Mutagenesis of αII Spectrin at Codon 1175 Modulates Its μ-Calpain Susceptibility †. Biochemistry 1997, 36: 57-65. PMID: 8993318, DOI: 10.1021/bi962034i.Peer-Reviewed Original ResearchConceptsSite-directed mutagenesisAlpha II spectrinCalpain cleavage sitesCleavage siteII-spectrinHelix CRecombinant GST-fusion proteinsBona fide proteinGST fusion proteinTriple-helical motifsStrict substrate specificityFamily of Ca2Protein kinase CDynamic molecular modelingStructural repeatsProminent substrateDifferent amino acidsSubstrate specificityIntracellular proteolysisPenultimate residueCysteine proteasesKinase CMost proteasesSteroid receptor activationSpectrin