C. Patrick Lusk, PhD
Professor of Cell BiologyCards
Appointments
Additional Titles
Co-Director, Molecular Cell Biology, Genetics and Development Track, Cell Biology
Co-Director, Cellular, Molecular, and Quantitative Biology Training Program, Cell Biology
Contact Info
Cell Biology
PO Box 208002, 333 Cedar Street
New Haven, CT 06520-8002
United States
Appointments
Additional Titles
Co-Director, Molecular Cell Biology, Genetics and Development Track, Cell Biology
Co-Director, Cellular, Molecular, and Quantitative Biology Training Program, Cell Biology
Contact Info
Cell Biology
PO Box 208002, 333 Cedar Street
New Haven, CT 06520-8002
United States
Appointments
Additional Titles
Co-Director, Molecular Cell Biology, Genetics and Development Track, Cell Biology
Co-Director, Cellular, Molecular, and Quantitative Biology Training Program, Cell Biology
Contact Info
Cell Biology
PO Box 208002, 333 Cedar Street
New Haven, CT 06520-8002
United States
About
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Titles
Professor of Cell Biology
Co-Director, Molecular Cell Biology, Genetics and Development Track, Cell Biology; Co-Director, Cellular, Molecular, and Quantitative Biology Training Program, Cell Biology
Biography
Dr. Lusk runs the joint LusKing laboratory with Megan King in the Department of Cell Biology. He is also the co-director of the MCGD graduate training track. He has a long standing interest in fundamental cellular mechanisms of compartmentalization with an emphasis on those that govern the biogenesis of the nuclear envelope and nuclear pore complexes (NPCs). He has been studying the nuclear envelope and nuclear transport since his graduate work at the University of Alberta in Canada and has been trained during his postdoctoral fellowship by Nobel Laureate Günter Blobel at The Rockefeller University. During this time, he (with collaborators/colleagues) has provided substantial insight into how nuclear transport is regulated and how the NPC is assembled. Moreover, he has helped to develop yeast as a model to study integral membrane proteins that reside at the inner nuclear membrane. While it is generally understood that these proteins are essential factors in gene regulation and genome organization, which is reflected by the discovery of the “nuclear envelopathies”, they remain challenging to study. Dr. Lusk is leveraging his expertise in yeast cell biology and genetics with super-resolution and proteomic approaches to illuminate function at the nuclear periphery.
Appointments
Cell Biology
ProfessorPrimary
Other Departments & Organizations
- Biochemistry, Quantitative Biology, Biophysics and Structural Biology (BQBS)
- Cell Biology
- Cell Biology Research
- Discovery to Cure Internship
- Genomics, Genetics, and Epigenetics
- LusKing Lab
- Molecular Cell Biology, Genetics and Development
- Yale Cancer Center
- Yale Combined Program in the Biological and Biomedical Sciences (BBS)
- Yale Ventures
Education & Training
- Postdoctoral Fellow
- The Rockefeller University (2009)
- PhD
- University of Alberta (2005)
- BS
- University of Alberta (1998)
Research
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Overview
Medical Research Interests
ORCID
0000-0003-4703-0533- View Lab Website
LusKing Lab Website
Research at a Glance
Yale Co-Authors
Publications Timeline
Research Interests
Megan C. King, PhD
Chenxiang Lin, PhD
Chunxiang Wu
Thomas Melia, PhD
Yong Xiong, PhD
Ivan Surovtsev
Nuclear Pore
Nuclear Envelope
Nuclear Pore Complex Proteins
Publications
2025
Nuclear mechanics as a determinant of nuclear pore complex plasticity
Lusk C, Morgan K, King M. Nuclear mechanics as a determinant of nuclear pore complex plasticity. Nature Cell Biology 2025, 1-10. PMID: 40973737, DOI: 10.1038/s41556-025-01768-w.Peer-Reviewed Original ResearchCitationsAltmetricConceptsNuclear pore complexNuclear surfaceSurface of mammalian cellsCell fate decisionsFate decisionsMammalian cellsPore complexNuclear poresTissue-specificNuclear mechanicsComposite plasticsIndividual cellsCell typesMembrane tensionNucleoporinsCellsTransport channelsMolecular compositionTransport conduitsSense, plug, and seal: proteins as both rapid responders and constitutive barriers supporting organelle compartmentalization.
King M, Lusk C, Ader N. Sense, plug, and seal: proteins as both rapid responders and constitutive barriers supporting organelle compartmentalization. Molecular Biology Of The Cell 2025, 36: pe6. PMID: 40601416, PMCID: PMC12367315, DOI: 10.1091/mbc.e23-08-0307.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsOrganelle compartmentalizationNuclear envelopePostmitotic nuclear envelopeInterphase nuclear envelopeProteinaceous barrierObservation of proteinsPlasma membraneRepair proteinsCell biologyOrganelle damageProteinOrganellesCompartmentalizationBiophysical natureBiological membranesConstitutive barriersMembraneLateral diffusionContribution of proteinMembrane rupturePhospholipid bilayer membranesVisualizing nuclear pore complex plasticity with pan-expansion microscopy
Morgan K, Carley E, Coyne A, Rothstein J, Lusk C, King M. Visualizing nuclear pore complex plasticity with pan-expansion microscopy. Journal Of Cell Biology 2025, 224: e202409120. PMID: 40504117, PMCID: PMC12162248, DOI: 10.1083/jcb.202409120.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsA quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope
Mannino P, Perun A, Surovtsev I, Ader N, Shao L, Rodriguez E, Melia T, King M, Lusk C. A quantitative ultrastructural timeline of nuclear autophagy reveals a role for dynamin-like protein 1 at the nuclear envelope. Nature Cell Biology 2025, 27: 464-476. PMID: 39920277, PMCID: PMC11908896, DOI: 10.1038/s41556-025-01612-1.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsInner nuclear membraneDynamin-like protein 1Membrane fissionNuclear envelopeMembrane fission stepNon-canonical rolesDouble-membrane vesiclesProtein 1Nuclear envelope remodelingLattice light-sheet microscopyFission stepDnm1Nuclear autophagyIntact nucleiPerinuclear spaceNuclear membraneAutophagic mechanismsNucleophagyCorrelative lightLight-sheet microscopyFissionElectron tomographyVesiclesVacuolesAtg11Nup107 contributes to the maternal-to-zygotic transition by preventing the premature nuclear export of pri-miR427
Kostiuk V, Kabir R, Levangie K, Empke S, Morgan K, Owens N, Lusk C, Khokha M. Nup107 contributes to the maternal-to-zygotic transition by preventing the premature nuclear export of pri-miR427. Development 2025, 152: dev202865. PMID: 39791357, PMCID: PMC11829755, DOI: 10.1242/dev.202865.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsMaternal transcriptsMaternal-to-zygotic transitionMaternal RNA clearanceZinc-finger transcription factorDegradation of maternal transcriptsEctodermal cell fatesMaternal-zygotic transitionNuclear pore complexNucleoporin functionZygotic transcriptionNuclear exportTranscript stabilityCell fateNuclear retentionTranscription factorsPore complexNup107TranscriptionEarly embryosRecognition sitesRNA clearanceGastrulationGerm layersTime course
2024
Channel width modulates the permeability of DNA origami–based nuclear pore mimics
Feng Q, Saladin M, Wu C, Cao E, Zheng W, Zhang A, Bhardwaj P, Li X, Shen Q, Kapinos L, Kozai T, Mariappan M, Lusk C, Xiong Y, Lim R, Lin C. Channel width modulates the permeability of DNA origami–based nuclear pore mimics. Science Advances 2024, 10: eadq8773. PMID: 39536094, PMCID: PMC11559598, DOI: 10.1126/sciadv.adq8773.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsA-tisket, a-tasket, what a beautiful nuclear basket
Lusk C, King M. A-tisket, a-tasket, what a beautiful nuclear basket. Cell 2024, 187: 5225-5227. PMID: 39303690, DOI: 10.1016/j.cell.2024.08.030.Peer-Reviewed Original ResearchCitationsAltmetricThe multidimensional roles of intermediate filaments - bridging genetic diversity with form, functions, and targets
Lusk C, Eriksson J. The multidimensional roles of intermediate filaments - bridging genetic diversity with form, functions, and targets. Current Opinion In Cell Biology 2024, 88: 102354. PMID: 38604107, DOI: 10.1016/j.ceb.2024.102354.Peer-Reviewed Original ResearchConcepts
2023
An ESCRT grommet cooperates with a diffusion barrier to maintain nuclear integrity
Ader N, Chen L, Surovtsev I, Chadwick W, Rodriguez E, King M, Lusk C. An ESCRT grommet cooperates with a diffusion barrier to maintain nuclear integrity. Nature Cell Biology 2023, 25: 1465-1477. PMID: 37783794, PMCID: PMC11365527, DOI: 10.1038/s41556-023-01235-4.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsSpindle pole body proteinNuclear envelope barrierESCRT-III proteinsNuclear pore complexSpindle pole bodyNucleocytoplasmic compartmentalizationESCRT functionPore complexPole bodyDistinct complementNuclear compartmentNuclear integrityTransport proteinsMolecular mechanismsRemodelling mechanismProteinBody proteinChanging the guard—nuclear pore complex quality control
Veldsink A, Gallardo P, Lusk C, Veenhoff L. Changing the guard—nuclear pore complex quality control. FEBS Letters 2023, 597: 2739-2749. PMID: 37715940, DOI: 10.1002/1873-3468.14739.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and Concepts
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Cell Biology
PO Box 208002, 333 Cedar Street
New Haven, CT 06520-8002
United States
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