Featured Publications
TRIM5 is an innate immune sensor for the retrovirus capsid lattice
Pertel T, Hausmann S, Morger D, Züger S, Guerra J, Lascano J, Reinhard C, Santoni FA, Uchil PD, Chatel L, Bisiaux A, Albert ML, Strambio-De-Castillia C, Mothes W, Pizzato M, Grütter MG, Luban J. TRIM5 is an innate immune sensor for the retrovirus capsid lattice. Nature 2011, 472: 361-365. PMID: 21512573, PMCID: PMC3081621, DOI: 10.1038/nature09976.Peer-Reviewed Original ResearchMeSH KeywordsAntiviral Restriction FactorsCapsidCarrier ProteinsCell LineEnzyme ActivationHEK293 CellsHIV-1HumansImmunity, InnateLipopolysaccharidesMAP Kinase Kinase KinasesNF-kappa BProtein BindingReceptors, Pattern RecognitionRetroviridaeSignal TransductionTranscription Factor AP-1Transcription FactorsTripartite Motif ProteinsUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesTRIM15 is a focal adhesion protein that regulates focal adhesion disassembly
Uchil PD, Pawliczek T, Reynolds TD, Ding S, Hinz A, Munro JB, Huang F, Floyd RW, Yang H, Hamilton WL, Bewersdorf J, Xiong Y, Calderwood DA, Mothes W. TRIM15 is a focal adhesion protein that regulates focal adhesion disassembly. Journal Of Cell Science 2014, 127: 3928-3942. PMID: 25015296, PMCID: PMC4163643, DOI: 10.1242/jcs.143537.Peer-Reviewed Original ResearchConceptsFocal adhesion proteinsFocal adhesionsCell migrationAdhesion proteinsMulti-adaptor proteinTripartite motif (TRIM) protein familyFocal adhesion dynamicsFocal adhesion turnoverFocal adhesion componentsCoiled-coil domainImpaired cell migrationII-independent mannerLD2 motifAdhesion turnoverActin cytoskeletonProtein familyAdhesion dynamicsCellular functionsDynamic turnoverMacromolecular complexesRegulatory componentsFocal contactsAdhesion componentsExtracellular matrixTRIM15
2011
TRIM22 Inhibits HIV-1 Transcription Independently of Its E3 Ubiquitin Ligase Activity, Tat, and NF-κB-Responsive Long Terminal Repeat Elements
Kajaste-Rudnitski A, Marelli SS, Pultrone C, Pertel T, Uchil PD, Mechti N, Mothes W, Poli G, Luban J, Vicenzi E. TRIM22 Inhibits HIV-1 Transcription Independently of Its E3 Ubiquitin Ligase Activity, Tat, and NF-κB-Responsive Long Terminal Repeat Elements. Journal Of Virology 2011, 85: 5183-5196. PMID: 21345949, PMCID: PMC3126207, DOI: 10.1128/jvi.02302-10.Peer-Reviewed Original ResearchMeSH KeywordsCell LineHIV-1HumansMinor Histocompatibility AntigensMonocytesRepressor ProteinsT-LymphocytesTranscription, GeneticTripartite Motif ProteinsVirus ReplicationConceptsHIV-1 replicationHIV-1 transcriptionHuman immunodeficiency virus type 1 (HIV-1) replicationU937 promonocytic cell lineHIV-1 restriction factorsTumor necrosis factor alphaInhibits HIV-1 transcriptionType 1 replicationRestriction factorsHIV-1 productionNecrosis factor alphaLower peak levelsPermissive cellsHIV-1 LTRHost restriction factorsPromonocytic cell lineU937 cellsReplication-competent virusNF-κB binding siteFactor alphaT cellsHIV-1Overexpression of TRIM22NF-κBLTR transactivation