2016
Kv3.3 Channels Bind Hax-1 and Arp2/3 to Assemble a Stable Local Actin Network that Regulates Channel Gating
Zhang Y, Zhang XF, Fleming MR, Amiri A, El-Hassar L, Surguchev AA, Hyland C, Jenkins DP, Desai R, Brown MR, Gazula VR, Waters MF, Large CH, Horvath TL, Navaratnam D, Vaccarino FM, Forscher P, Kaczmarek LK. Kv3.3 Channels Bind Hax-1 and Arp2/3 to Assemble a Stable Local Actin Network that Regulates Channel Gating. Cell 2016, 165: 434-448. PMID: 26997484, PMCID: PMC4826296, DOI: 10.1016/j.cell.2016.02.009.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin-Related Protein 2Actin-Related Protein 2-3 ComplexActin-Related Protein 3Adaptor Proteins, Signal TransducingAmino Acid SequenceCell MembraneMolecular Sequence DataMutationNeuronsPluripotent Stem CellsRac GTP-Binding ProteinsShaw Potassium ChannelsSignal TransductionSpinocerebellar AtaxiasConceptsCytoplasmic C-terminusProline-rich domainPlasma membraneHAX-1Actin nucleationC-terminusCortical actin filament networkLocal actin networkStem cell-derived neuronsActin filament networkCell-derived neuronsAnti-apoptotic proteinsActin cytoskeletonKv3.3 potassium channelActin assemblyActin structuresActin networkArp2/3Channel gatingFilament networkGrowth conesCerebellar neurodegenerationKv3.3TerminusPotassium channels
2013
Protein kinase C activation decreases peripheral actin network density and increases central nonmuscle myosin II contractility in neuronal growth cones
Yang Q, Zhang XF, Van Goor D, Dunn AP, Hyland C, Medeiros N, Forscher P. Protein kinase C activation decreases peripheral actin network density and increases central nonmuscle myosin II contractility in neuronal growth cones. Molecular Biology Of The Cell 2013, 24: 3097-3114. PMID: 23966465, PMCID: PMC3784383, DOI: 10.1091/mbc.e13-05-0289.Peer-Reviewed Original ResearchConceptsProtein kinase CMyosin II contractilityActin network densityNeuronal growth conesPKC activationCentral cytoplasmic domainRetrograde actin network flowTwo-tiered mechanismEffect of PKCActin network flowActin network structureActin filament networkGrowth conesProtein kinase C activationKinase C activationCytoplasmic domainActin polymerizationKinase CFilament networkCytoskeletal mechanismsRegulatory light chain phosphorylationPKC actionPKC activityC activationGuidance responses
2001
Transmission of growth cone traction force through apCAM–cytoskeletal linkages is regulated by Src family tyrosine kinase activity
Suter D, Forscher P. Transmission of growth cone traction force through apCAM–cytoskeletal linkages is regulated by Src family tyrosine kinase activity. Journal Of Cell Biology 2001, 155: 427-438. PMID: 11673478, PMCID: PMC2150837, DOI: 10.1083/jcb.200107063.Peer-Reviewed Original Research
2000
Substrate–cytoskeletal coupling as a mechanism for the regulation of growth cone motility and guidance
Suter D, Forscher P. Substrate–cytoskeletal coupling as a mechanism for the regulation of growth cone motility and guidance. Developmental Neurobiology 2000, 44: 97-113. PMID: 10934315, DOI: 10.1002/1097-4695(200008)44:2<97::aid-neu2>3.0.co;2-u.Peer-Reviewed Original ResearchConceptsGrowth cone motilityCone motilityGuidance cuesGrowth conesDifferent guidance cuesDynamic cytoskeletonCell adhesion moleculeSignal transducerAxon guidanceMolecular componentsCytoskeletonMotile structuresMotility deviceAppropriate target cellsDifferent functionsRespective receptorsAdhesion moleculesProteinAxonal growthMotilityGrowth cone movementTarget cellsNeuronal processesRecent evidenceCone movementLocalization of unconventional myosins V and VI in neuronal growth cones
Suter D, Espindola F, Lin C, Forscher P, Mooseker M. Localization of unconventional myosins V and VI in neuronal growth cones. Developmental Neurobiology 2000, 42: 370-382. PMID: 10645976, DOI: 10.1002/(sici)1097-4695(20000215)42:3<370::aid-neu8>3.0.co;2-v.Peer-Reviewed Original Research
1992
Novel form of growth cone motility involving site-directed actin filament assembly
Forscher P, Lin C, Thompson C. Novel form of growth cone motility involving site-directed actin filament assembly. Nature 1992, 357: 515-518. PMID: 1608453, DOI: 10.1038/357515a0.Peer-Reviewed Original ResearchConceptsActin filament assemblyFilament assemblyNeuronal growth conesCortical F-actin networkMembrane-cytoskeletal interfaceF-actin assemblyF-actin networkGrowth conesGrowth cone migrationGrowth cone motilityExtracellular signalsBacterial parasiteMembrane proteinsCell movementCytoskeletal structuresIntracellular movementDevelopmental processesBead movementCell locomotionCone migrationMorphogenic changesMotile cellsAxonal guidanceCone motilityCellular mechanisms