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
2012
Membrane Tension, Myosin Force, and Actin Turnover Maintain Actin Treadmill in the Nerve Growth Cone
Craig EM, Van Goor D, Forscher P, Mogilner A. Membrane Tension, Myosin Force, and Actin Turnover Maintain Actin Treadmill in the Nerve Growth Cone. Biophysical Journal 2012, 102: 1503-1513. PMID: 22500750, PMCID: PMC3318135, DOI: 10.1016/j.bpj.2012.03.003.Peer-Reviewed Original Research
1999
A diffusion barrier maintains distribution of membrane proteins in polarized neurons
Winckler B, Forscher P, Mellman I. A diffusion barrier maintains distribution of membrane proteins in polarized neurons. Nature 1999, 397: 698-701. PMID: 10067893, DOI: 10.1038/17806.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsAxonsBiological TransportCell CompartmentationCell MembraneCell PolarityCells, CulturedCytoskeletonDiffusionDimethyl SulfoxideLeukocyte L1 Antigen ComplexMembrane GlycoproteinsMembrane ProteinsMicrospheresNeural Cell Adhesion MoleculesNeuronsRatsReceptors, AMPAThy-1 AntigensConceptsMembrane proteinsDiffusion barrierObvious physical barriersPlasma membrane domainsLateral mobilityOptical tweezersCell-cell contactMembrane domainsPresumptive domainPolarized neuronsPlasma membraneCytoskeletal componentsPolarized distributionF-actinDiffusion of proteinsDistinct domainsBasolateral surfaceMembrane markersProteinSpecialized domainsInitial segmentTight junctionsAsymmetric distributionPhysical barrierTweezers
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