2023
The 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 ResearchConceptsHIV-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 evidence
2019
An ESCRT-LEM protein surveillance system is poised to directly monitor the nuclear envelope and nuclear transport system
Thaller DJ, Allegretti M, Borah S, Ronchi P, Beck M, Lusk CP. An ESCRT-LEM protein surveillance system is poised to directly monitor the nuclear envelope and nuclear transport system. ELife 2019, 8: e45284. PMID: 30942170, PMCID: PMC6461442, DOI: 10.7554/elife.45284.Peer-Reviewed Original ResearchConceptsNuclear pore complexNPC assemblyNuclear membraneNuclear envelope barrierNuclear envelope herniationsNuclear envelope integrityNuclear transport systemXPO1/CRM1Membrane deliveryPore complexEnvelope integrityNuclear transportYeast modelNuclear poresChm7Nuclear envelopeFenestrated sheetHeh1Membrane disruptionMechanical membrane disruptionSelective barrierDisease mechanismsMembrane sealingTransport systemMembrane