Mark Mooseker, PhD
Ross Granville Harrison Professor of Molecular, Cellular, and Developmental Biology and Professor of Cell BiologyCards
Appointments
Additional Titles
and Pathlogy
Contact Info
Yale University
MCD-Biology, Yale University
New Haven, CT 06520
United States
Appointments
Additional Titles
and Pathlogy
Contact Info
Yale University
MCD-Biology, Yale University
New Haven, CT 06520
United States
Appointments
Additional Titles
and Pathlogy
Contact Info
Yale University
MCD-Biology, Yale University
New Haven, CT 06520
United States
About
Titles
Ross Granville Harrison Professor of Molecular, Cellular, and Developmental Biology and Professor of Cell Biology
and PathlogyAppointments
Cell Biology
ProfessorSecondary
Other Departments & Organizations
- Cell Biology
- Cytoskeletal Dynamics
- Developmental Cell Biology and Genetics
- Interdepartmental Neuroscience Program
- Membrane Traffic
- Neuroscience Track
- Yale Combined Program in the Biological and Biomedical Sciences (BBS)
- Yale Ventures
Education & Training
- PhD
- University of Pennsylvania (1976)
Research
Overview
Our laboratory pursues questions regarding the molecular and functional organization of the cell’s cytoskeleton. The major thrust of current effort is focused on the molecular and functional characterization of actin-filament based molecular motors—i.e., myosins. To date, 24 structurally distinct, evolutionarily-ancient classes of this molecular motor (in addition to the familiar two-headed, filament forming myosins of muscle and nonmuscle cells) have been identified. In vertebrate cells, multiple myosins of multiple classes are expressed, and for most of these myosins little is known regarding their function, since most have only just been discovered. At present we are conducting studies on a number of the novel myosins identified by our laboratory.
Ongoing projects include the following: a) cell biological and molecular genetic assessment of novel myosin functions in selected cell lines; b) biochemical and biophysical assessment of mechano-chemical (motor) properties; c) characterization of myosin-dependent organelle transport and membrane traffic; d) phenotypic analysis of myosin mutants in mouse and Drosophila. Among the myosins recently characterized by our laboratory include five classes of motor myosins (I,V, VI, VII, and IX) that are target genes for well-characterized mutations in mouse and man.
A key hypothesis to be tested is that, while some of the myosins expressed in the cell are probably involved in motile phenomena such as organelle movement or endocytosis, others utilize their mechanochemical properties not to locomote but rather to mechanochemically modulate the biological activities of those proteins with which that motor interacts (e.g., a membrane pump or channel). Still other myosins are likely to be key players in a variety of signal transduction cascades based on the identification of a variety of protein domains (e.g., SH-3, pleckstrin homology, GAP domains) that have been identified within the tail (non-motor) domains of certain myosins.
Research at a Glance
Yale Co-Authors
Publications Timeline
Jon Morrow, PhD, MD
Paul Forscher, PhD
Jorge Galán, PhD, DVM
Nadia Ameen, MBBS
Anthony Koleske, PhD
Enrique M. De La Cruz, PhD
Publications
2013
Role of Myosin1a in regulated exocytosis of CFTR in villus enterocytes
Hoekstra N, Kravtsov D, Mooseker M, Ameen N. Role of Myosin1a in regulated exocytosis of CFTR in villus enterocytes. The FASEB Journal 2013, 27: 913.11-913.11. DOI: 10.1096/fasebj.27.1_supplement.913.11.Peer-Reviewed Original ResearchConceptsSurface biotinylationRegulated exocytosisCFTR trafficSurface CFTRSubapical endosomesBrush border membraneMembrane traffickingCFTR deliveryKD cellsKnockdown cellsCFTR channelsCFTR distributionVillus enterocytesMolecular mechanismsEnterocyte brush border membraneCFTRBiotinylationConfocal microscopyEndosomesIntestinal brush border membraneMouse intestineExocytosisCGMP agonistMyo1aBorder membrane
2012
Mo1821 Normalization of CFTR Brush Border Membrane Trafficking Defects in the Intestines of Myosin 1A/6 Double Mutant Mice
Hoekstra N, Mooseker M, Ameen N. Mo1821 Normalization of CFTR Brush Border Membrane Trafficking Defects in the Intestines of Myosin 1A/6 Double Mutant Mice. Gastroenterology 2012, 142: s-692-s-693. DOI: 10.1016/s0016-5085(12)62674-2.Peer-Reviewed Original Research
2008
Myo2p, a class V myosin in budding yeast, associates with a large ribonucleic acid–protein complex that contains mRNAs and subunits of the RNA-processing body
Chang W, Zaarour RF, Reck-Peterson S, Rinn J, Singer RH, Snyder M, Novick P, Mooseker MS. Myo2p, a class V myosin in budding yeast, associates with a large ribonucleic acid–protein complex that contains mRNAs and subunits of the RNA-processing body. RNA 2008, 14: 491-502. PMID: 18218704, PMCID: PMC2248268, DOI: 10.1261/rna.665008.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsMeSH KeywordsActinsAdenosine TriphosphatasesBase SequenceDNA PrimersMacromolecular SubstancesMyosin Heavy ChainsMyosin Type VOligonucleotide Array Sequence AnalysisOrganellesPolyribosomesRibonucleoproteinsRNA Processing, Post-TranscriptionalRNA, FungalRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSecretory VesiclesVacuolesConceptsRNA processing bodiesClass V myosinsP-bodiesRelease of mRNAProcessing bodiesOrganelle traffickingSpindle orientationMotor mutantsMyo2-66Ribosomal subunitMyo2pProtein subunitsPartial colocalizationMicroarray analysisSubunitsSedimentation analysisYeastMRNAComplexesMyosinMutantsPolysomesTraffickingRNAColocalization
2007
Roles for Drosophila melanogaster Myosin IB in Maintenance of Enterocyte Brush-Border Structure and Resistance to the Bacterial Pathogen Pseudomonas entomophila
Hegan PS, Mermall V, Tilney LG, Mooseker MS. Roles for Drosophila melanogaster Myosin IB in Maintenance of Enterocyte Brush-Border Structure and Resistance to the Bacterial Pathogen Pseudomonas entomophila. Molecular Biology Of The Cell 2007, 18: 4625-4636. PMID: 17855510, PMCID: PMC2043548, DOI: 10.1091/mbc.e07-02-0191.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsMutant larvaePseudomonas entomophilaTail domainMyosin IBMidgut epithelial cellsActin filament coreDrosophila genomeApical brush borderMidgut enterocytesBrush borderCytoskeletal defectsLarval gutResponse pathwaysApical localizationMV membraneBrush border structureDeletion mutationsFood uptakeGram-negative bacterial infectionsInnate immune responseMyo1bGut physiologyEntomophilaEpithelial cellsMidgutAssessment of myosin II, Va, VI and VIIa loss of function on endocytosis and endocytic vesicle motility in bone marrow‐derived dendritic cells
Holt JP, Bottomly K, Mooseker MS. Assessment of myosin II, Va, VI and VIIa loss of function on endocytosis and endocytic vesicle motility in bone marrow‐derived dendritic cells. Cytoskeleton 2007, 64: 756-766. PMID: 17615572, DOI: 10.1002/cm.20220.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsDendritic cellsBone marrow-derived dendritic cellsMarrow-derived dendritic cellsShaker-1Immune surveillanceDendritic cell endocytosisCytometric analysisMouse linesBlebbistatin-treated cellsMyosin mutationsDextran uptakeVesicle movementEndosomal acidificationMyosin IIPhagocytosisWaltzerCell rateCellsFluorescent dextranMyosin II functionFluid-phase uptakeUptakeMyosin Va.Vesicle motilityMyosin familyMyosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis
Krendel M, Osterweil EK, Mooseker MS. Myosin 1E interacts with synaptojanin‐1 and dynamin and is involved in endocytosis. FEBS Letters 2007, 581: 644-650. PMID: 17257598, PMCID: PMC1861834, DOI: 10.1016/j.febslet.2007.01.021.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsMeSH Keywords3T3 CellsAnimalsChlorocebus aethiopsClathrin-Coated VesiclesCOS CellsDynaminsEndocytosisHeLa CellsHumansImmunoprecipitationMiceMyosin Type INerve Tissue ProteinsPhosphoric Monoester HydrolasesProtein BindingProtein TransportRatsSrc Homology DomainsSynapsesTissue ExtractsTransferrinTwo-Hybrid System TechniquesConceptsSH3 domainMyosin 1eSynaptojanin 1Myosin IIntact SH3 domainDominant-negative mannerReceptor-mediated endocytosisHigher eukaryotesArp2/3 complexInhibits endocytosisPlasma membraneActin polymerizationImportant regulatorEndocytosisHuman class IProminent functionDynaminTail regionDomainEukaryotesClathrinYeastRegulatorProteinBindsThe Structural And Functional Diversity Of The Myosin Family Of Actin-Based Molecular Motors
Mooseker M, Foth B. The Structural And Functional Diversity Of The Myosin Family Of Actin-Based Molecular Motors. Proteins And Cell Regulation 2007, 7: 1-34. DOI: 10.1007/978-1-4020-6519-4_1.Peer-Reviewed Original ResearchCitations
2006
Modulation of Cell Adhesion and Motility in the Immune System by Myo1f
Kim SV, Mehal WZ, Dong X, Heinrich V, Pypaert M, Mellman I, Dembo M, Mooseker MS, Wu D, Flavell RA. Modulation of Cell Adhesion and Motility in the Immune System by Myo1f. Science 2006, 314: 136-139. PMID: 17023661, DOI: 10.1126/science.1131920.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsMeSH KeywordsActinsAnimalsCD18 AntigensCell AdhesionCell DegranulationCell MovementChemotaxis, LeukocyteColony Count, MicrobialCytoplasmic GranulesExocytosisImmunity, InnateLigandsListeria monocytogenesListeriosisMiceMice, KnockoutMyosin Type INeutrophil ActivationNeutrophilsN-Formylmethionine Leucyl-PhenylalanineThe Tail Domain of Myosin Va Modulates Actin Binding to One Head*
Olivares A, Chang W, Mooseker M, Hackney D, De La Cruz E. The Tail Domain of Myosin Va Modulates Actin Binding to One Head*. Journal Of Biological Chemistry 2006, 281: 31326-31336. DOI: 10.1016/s0021-9258(19)84045-0.Peer-Reviewed Original ResearchCitations
2005
Cell Polarity Protein Spa2P Associates With Proteins Involved In Actin Function In Saccharomyces Cerevisiae
Shih J, Reck-Peterson S, Newitt R, Mooseker M, Aebersold R, Herskowitz I. Cell Polarity Protein Spa2P Associates With Proteins Involved In Actin Function In Saccharomyces Cerevisiae. Molecular Biology Of The Cell 2005, 16: 4595-4608. PMID: 16030260, PMCID: PMC1237067, DOI: 10.1091/mbc.e05-02-0108.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsCell polarityPolarity proteinsActin functionCell wall morphogenesisCell polarity proteinsYeast cell polarityPresumptive bud siteCell separation defectATP-sensitive mannerTandem mass spectrometry analysisNonessential proteinsWall morphogenesisMolecular functionsBud sitePolarized localizationSpa2pMass spectrometry analysisSite of growthSaccharomyces cerevisiaeMyo2pCoimmunoprecipitation strategyCell cycleF-actinIndirect interactionsProtein
Links & Media
Get In Touch
Contacts
Yale University
MCD-Biology, Yale University
New Haven, CT 06520
United States