2007
COP1D, an alternatively spliced constitutive photomorphogenic-1 (COP1) product, stabilizes UV stress-induced c-Jun through inhibition of full-length COP1
Savio M, Rotondo G, Maglie S, Rossetti G, Bender J, Pardi R. COP1D, an alternatively spliced constitutive photomorphogenic-1 (COP1) product, stabilizes UV stress-induced c-Jun through inhibition of full-length COP1. Oncogene 2007, 27: 2401-2411. PMID: 17968316, DOI: 10.1038/sj.onc.1210892.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBreast NeoplasmsCell LineDown-RegulationEnzyme StabilityHealthHeLa CellsHumansIsoenzymesJNK Mitogen-Activated Protein KinasesKineticsMolecular Sequence DataProteasome Endopeptidase ComplexRNA, MessengerTranscription, GeneticTumor Suppressor Protein p53Ubiquitin-Protein LigasesConceptsFull-length proteinC-JunCullin-RING ligase complexRING finger ubiquitin ligaseProteasome-dependent degradationDominant-negative functionCoiled-coil regionFunction of COP1Post-translational changesP53 protein levelsLigase complexCRL complexesE3 ligasesE3 ligaseUbiquitin ligaseCOP1Ectopic expressionRNA interferenceUV stressElevated c-JunPolyubiquitinationSplice variants
1999
A tyrosine‐based sorting signal in the β2 integrin cytoplasmic domain mediates its recycling to the plasma membrane and is required for ligand‐supported migration
Fabbri M, Fumagalli L, Bossi G, Bianchi E, Bender J, Pardi R. A tyrosine‐based sorting signal in the β2 integrin cytoplasmic domain mediates its recycling to the plasma membrane and is required for ligand‐supported migration. The EMBO Journal 1999, 18: 4915-4925. PMID: 10487744, PMCID: PMC1171563, DOI: 10.1093/emboj/18.18.4915.Peer-Reviewed Original ResearchConceptsIntegrin cytoplasmic domainCytoplasmic domainBeta-subunit cytoplasmic domainAdhesive functionTyrosine-based endocytic signalsSubunit cytoplasmic domainClathrin-dependent endocytosisSite-directed mutagenesisNon-conservative substitutionsChinese hamster ovary cellsEndocytic signalsRegulated internalizationMembrane rufflesUnrelated functionsRecycling compartmentHamster ovary cellsEctopic expressionPlasma membraneReceptor recyclingDegradative pathwayIntegrin dynamicsCell adhesionCell migrationCell surfaceOvary cells
1995
Conserved regions in the cytoplasmic domains of the leukocyte integrin alpha L beta 2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association.
Pardi R, Bossi G, Inverardi L, Rovida E, Bender J. Conserved regions in the cytoplasmic domains of the leukocyte integrin alpha L beta 2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association. The Journal Of Immunology 1995, 155: 1252-63. PMID: 7636193, DOI: 10.4049/jimmunol.155.3.1252.Peer-Reviewed Original ResearchMeSH KeywordsAllosteric RegulationAmino Acid SequenceAnimalsCell CompartmentationCell Line, TransformedChlorocebus aethiopsCytoskeletonEndoplasmic ReticulumLymphocyte Function-Associated Antigen-1Molecular Sequence DataProtein ConformationProtein MultimerizationProtein Structure, TertiaryRecombinant Fusion ProteinsSequence DeletionTetradecanoylphorbol AcetateT-LymphocytesTransfectionConceptsAlpha L beta 2Cytoplasmic domainEndoplasmic reticulum retentionCytoskeletal associationBeta subunitAlpha L subunitAlpha beta complexFunction of integrinsBeta 2GFFKR motifAdherent cellsDeletion mutantsSubstitution mutantsEctopic expressionIntegrin alphaPlasma membraneHeterodimer formationConserved regionsAdhesion receptorsBeta complexCytoplasmic truncationRegulated functionsL subunitsStructural determinantsAlpha L