2024
Structural insights into PPP2R5A degradation by HIV-1 Vif
Hu Y, Delviks-Frankenberry K, Wu C, Arizaga F, Pathak V, Xiong Y. Structural insights into PPP2R5A degradation by HIV-1 Vif. Nature Structural & Molecular Biology 2024, 31: 1492-1501. PMID: 38789685, DOI: 10.1038/s41594-024-01314-6.Peer-Reviewed Original ResearchHost-virus protein interactionsCullin RING E3 ubiquitin ligasesInduced G2/M cell cycle arrestSets of proteinsG2/M cell cycle arrestSubstrate-binding siteCryogenic-electron microscopy structuresProtein phosphatase 2ADegradation-independent mechanismCell cycle arrestUbiquitin ligaseProtein interactionsPhosphatase 2AAntiviral proteinCycle arrestDegradation-dependentA-resolutionHIV-1 VifPPP2R5AStructural insightsDiverse interactionsProteinCellular studiesPhosphatase activityPotential target
2023
Biochemical functions and structure of Caenorhabditis elegans ZK177.8 protein: Aicardi–Goutières syndrome SAMHD1 dNTPase ortholog
Maehigashi T, Lim C, Wade L, Bowen N, Knecht K, Alvarez N, Kelly W, Schinazi R, Kim D, Xiong Y, Kim B. Biochemical functions and structure of Caenorhabditis elegans ZK177.8 protein: Aicardi–Goutières syndrome SAMHD1 dNTPase ortholog. Journal Of Biological Chemistry 2023, 299: 105148. PMID: 37567474, PMCID: PMC10485159, DOI: 10.1016/j.jbc.2023.105148.Peer-Reviewed Original ResearchSterile alpha motif (SAM) domainMotif domainHistidine-aspartate domain-containing protein 1Allosteric regulatory mechanismsDomain-containing protein 1Cellular dNTP levelsStriking conservationCaenorhabditis elegansBiochemical functionsDevelopmental roleGene knockdownRegulatory mechanismsDevelopmental defectsHuman monocytic cell lineDNTP levelsMonocytic cell lineMouse SAMHD1Aicardi-Goutières syndromeProtein 1OrthologsHIV-1 restriction factorsProteinCell linesRestriction factorsDNA building blocksStructural basis for recruitment of host CypA and E3 ubiquitin ligase by maedi-visna virus Vif
Hu Y, Gudnadóttir R, Knecht K, Arizaga F, Jónsson S, Xiong Y. Structural basis for recruitment of host CypA and E3 ubiquitin ligase by maedi-visna virus Vif. Science Advances 2023, 9: eadd3422. PMID: 36638173, PMCID: PMC9839330, DOI: 10.1126/sciadv.add3422.Peer-Reviewed Original ResearchConceptsMVV VifCryo-electron microscopy structureE3 ubiquitin ligase complexLentiviral VifUbiquitin ligase complexHost cofactorsUbiquitin-proteasome pathwayDistinct interaction modesUnique structural elementsLentiviral Vif proteinsEvolutionary relationshipsMicroscopy structureLigase complexCellular proteinsE3 ubiquitinAntiviral APOBEC3Structural basisFunctional analysisMolecular mechanismsMaedi-visna virusRecruitment mechanismsVif proteinCofactorProteinCypA
2012
Structural insights into the function of FANCM‐mediated complexes
Saro D, Sachpatzidis A, Zheng X, Singh T, Meetei A, Xiong Y, Sung P. Structural insights into the function of FANCM‐mediated complexes. The FASEB Journal 2012, 26: 536.8-536.8. DOI: 10.1096/fasebj.26.1_supplement.536.8.Peer-Reviewed Original ResearchCore complex proteinsComplex proteinsDNA bindingDNA damage-induced monoubiquitinationFA-BRCA pathwayBranch migration activityProtein-protein interactionsDNA damage responseHigh-resolution crystal structuresResolution crystal structureChromatin localizationNovel histoneDamage responseSensitivity of cellsFANCMStructural insightsBiochemical characterizationFoci formationProteinStructural workX-ray crystallographyChromosome aberrationsMigration activityFunctional integrityComplexes