C. Patrick Lusk, PhD
Associate 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
Titles
Associate 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
Associate Professor TenurePrimary
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
Overview
Medical Subject Headings (MeSH)
ORCID
0000-0003-4703-0533- View Lab Website
LusKing Lab Website
Research at a Glance
Yale Co-Authors
Publications Timeline
Research Interests
Chenxiang Lin, PhD
Chunxiang Wu
Megan C. King, PhD
Philip Mannino
Qiancheng Xiong
Yong Xiong, PhD
Nuclear Pore
Nuclear Envelope
Nuclear Pore Complex Proteins
Publications
2024
A-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 ResearchAltmetricThe 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 ConceptsThe capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores
Shen Q, Kumari S, Xu C, Jang S, Shi J, Burdick R, Levintov L, Xiong Q, Wu C, Devarkar S, Tian T, Tripler T, Hu Y, Yuan S, Temple J, Feng Q, Lusk C, Aiken C, Engelman A, Perilla J, Pathak V, Lin C, Xiong Y. The capsid lattice engages a bipartite NUP153 motif to mediate nuclear entry of HIV-1 cores. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2202815120. PMID: 36943880, PMCID: PMC10068764, DOI: 10.1073/pnas.2202815120.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsHIV-1 capsidC-terminal tail regionTriple arginine motifNuclear pore complexPhenylalanine-glycine motifsBipartite motifNuclear importPore complexNuclear poresNuclear entryNup153Capsid latticeInteraction moduleProtein latticeCA assemblyCA hexamersIntact capsidsNucleoporinsHIV-1 coreMotifCapsidTail regionIntact formInfection studiesMechanistic evidenceModeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels
Shen Q, Feng Q, Wu C, Xiong Q, Tian T, Yuan S, Shi J, Bedwell G, Yang R, Aiken C, Engelman A, Lusk C, Lin C, Xiong Y. Modeling HIV-1 nuclear entry with nucleoporin-gated DNA-origami channels. Nature Structural & Molecular Biology 2023, 30: 425-435. PMID: 36807645, PMCID: PMC10121901, DOI: 10.1038/s41594-023-00925-9.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsNuclear pore complexHIV-1 nuclear entryNuclear entryNuclear importNPC central channelPore complexHost nucleusCapsid dockingVirus genomeAffinity gradientNup153Central channelMechanistic insightsMolecular interactionsCapsidNucleoporinsNup358Nup62GenomeNucleusVirusDockingVirus-1 infectionImportComplexes
2022
Functionalized DNA-Origami-Protein Nanopores Generate Large Transmembrane Channels with Programmable Size-Selectivity
Shen Q, Xiong Q, Zhou K, Feng Q, Liu L, Tian T, Wu C, Xiong Y, Melia T, Lusk C, Lin C. Functionalized DNA-Origami-Protein Nanopores Generate Large Transmembrane Channels with Programmable Size-Selectivity. Journal Of The American Chemical Society 2022, 145: 1292-1300. PMID: 36577119, PMCID: PMC9852090, DOI: 10.1021/jacs.2c11226.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsExchange of macromoleculesCholesterol-rich membranesHybrid nanoporesSynthetic biologyBiophysical toolsSynthetic cellsTransmembrane channelsTransmembrane nanoporesDNA ringsProtein nanoporeCell membraneBacterial toxinsDNA origami techniqueLipid membranesAnalytical chemistryMacromolecule sizeDNA origamiMembraneProgrammable sizeNanoporesSized poresNucleoporinsAverage inner diameterCellsPneumolysinKap-β2/Transportin mediates β-catenin nuclear transport in Wnt signaling
Hwang WY, Kostiuk V, González DP, Lusk CP, Khokha M. Kap-β2/Transportin mediates β-catenin nuclear transport in Wnt signaling. ELife 2022, 11: e70495. PMID: 36300792, PMCID: PMC9665845, DOI: 10.7554/elife.70495.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsNuclear transport receptorsΒ-catenin nuclear transportNuclear transportΒ-cateninExcessive WntΒ-catenin nuclear importHeterologous model systemsΒ-catenin accumulatesPrimary embryonic axisNuclear transport machineryRan-dependent mannerNuclear localization signalTCF/LEF reporterPY-NLSNuclear importLocalization signalTransport machineryTransport receptorsResponsive genesEmbryonic developmentEmbryonic axisWnt signalingKey effectorsDirect bindingHuman diseasesQuality control mechanisms that protect nuclear envelope identity and function
Mannino PJ, Lusk CP. Quality control mechanisms that protect nuclear envelope identity and function. Journal Of Cell Biology 2022, 221: e202205123. PMID: 36036741, PMCID: PMC9442147, DOI: 10.1083/jcb.202205123.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsNuclear pore complexQuality control mechanismsNuclear envelopeCellular degradative machineryNE integrityGenome stabilityPore complexMembrane remodelingDegradative machineryOuter membraneDistinct biochemistryBiochemical identityEndoplasmic reticulumAutophagy mechanismControl mechanismsSelective barrierPore membraneMembraneRecent workEukaryotesProteomeDeleterious effectsSpecializationMechanismMachinery
2021
Atg39 selectively captures inner nuclear membrane into lumenal vesicles for delivery to the autophagosome
Chandra S, Mannino PJ, Thaller DJ, Ader NR, King MC, Melia TJ, Lusk CP. Atg39 selectively captures inner nuclear membrane into lumenal vesicles for delivery to the autophagosome. Journal Of Cell Biology 2021, 220: e202103030. PMID: 34714326, PMCID: PMC8575018, DOI: 10.1083/jcb.202103030.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsMeSH KeywordsAutophagosomesAutophagyAutophagy-Related ProteinsCytoplasmic VesiclesGreen Fluorescent ProteinsNuclear EnvelopeProtein DomainsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipTime FactorsVacuolesVesicular Transport ProteinsConceptsInner nuclear membraneNuclear envelope lumenOuter nuclear membraneNuclear membraneSplit-GFP reporterNuclear envelope localizationINM proteinsAutophagy apparatusEnvelope localizationLumenal vesiclesLumenal domainCargo adaptorsAtg39Sequence elementsCorrelative lightVesiclesAutophagosomesMembraneNucleophagyAdaptorReporterProteinOverexpressionMotif
News & Links
Media
- Superresolution image of nuclear pore complexes
News
- February 19, 2023Source: Nature Structural & Molecular Biology
Modeling HIV-1 nuclear entry with DNA-origami nuclear pore mimics
- September 05, 2022Source: ASBMB Today
The importance of team mentorship
- February 07, 2021Source: BioRxiv
A DNA-origami NanoTrap for studying the diffusion barriers
- December 13, 2020Source: BioRxiv
The LusKing lab discovers role for phosphatidic acid in nuclear envelope surveillance
Get In Touch
Contacts
Cell Biology
PO Box 208002, 333 Cedar Street
New Haven, CT 06520-8002
United States
Administrative Support
Locations
Boyer Center for Molecular Medicine
Lab
295 Congress Avenue, Ste BCMM 247
New Haven, CT 06510
Boyer Center for Molecular Medicine
Academic Office
295 Congress Avenue, Ste BCMM 254B
New Haven, CT 06510