2013
ASB2α, an E3 Ubiquitin Ligase Specificity Subunit, Regulates Cell Spreading and Triggers Proteasomal Degradation of Filamins by Targeting the Filamin Calponin Homology 1 Domain*
Razinia Z, Baldassarre M, Cantelli G, Calderwood DA. ASB2α, an E3 Ubiquitin Ligase Specificity Subunit, Regulates Cell Spreading and Triggers Proteasomal Degradation of Filamins by Targeting the Filamin Calponin Homology 1 Domain*. Journal Of Biological Chemistry 2013, 288: 32093-32105. PMID: 24052262, PMCID: PMC3814802, DOI: 10.1074/jbc.m113.496604.Peer-Reviewed Original ResearchConceptsHematopoietic cell differentiationSpecificity subunitProteasomal degradationF-actin-rich structuresE3 ubiquitin ligase complexCell differentiationNormal subcellular localizationHomology 1 domainLoss of filaminUbiquitin acceptor sitesActin-binding domainCross-linking proteinsActin-binding siteLigase complexActin cytoskeletonTransmembrane proteinSubcellular localizationΑ-actinin1Transient expressionASB2αDegradation of filaminMinimal fragmentLysine residuesFilaminCell adhesion
2011
The E3 ubiquitin ligase specificity subunit ASB2α targets filamins for proteasomal degradation by interacting with the filamin actin-binding domain
Razinia Z, Baldassarre M, Bouaouina M, Lamsoul I, Lutz PG, Calderwood DA. The E3 ubiquitin ligase specificity subunit ASB2α targets filamins for proteasomal degradation by interacting with the filamin actin-binding domain. Journal Of Cell Science 2011, 124: 2631-2641. PMID: 21750192, PMCID: PMC3138704, DOI: 10.1242/jcs.084343.Peer-Reviewed Original ResearchConceptsFilamin degradationProteasomal degradationCell differentiationDomain of filaminActin-rich structuresUbiquitin-proteasome pathwayExtracellular matrix connectionsActin cytoskeletonTransmembrane proteinSubcellular localizationMolecular basisSignaling cascadesASB2αActin filamentsFilaminAcute degradationBiochemical assaysMyeloid leukemia cellsImportant familyActinEarly eventsProteinLeukemia cellsImportant mechanismDifferentiationFunctional and Structural Insights into ASB2α, a Novel Regulator of Integrin-dependent Adhesion of Hematopoietic Cells*
Lamsoul I, Burande CF, Razinia Z, Houles TC, Menoret D, Baldassarre M, Erard M, Moog-Lutz C, Calderwood DA, Lutz PG. Functional and Structural Insights into ASB2α, a Novel Regulator of Integrin-dependent Adhesion of Hematopoietic Cells*. Journal Of Biological Chemistry 2011, 286: 30571-30581. PMID: 21737450, PMCID: PMC3162417, DOI: 10.1074/jbc.m111.220921.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsCarrier ProteinsCell AdhesionFibronectinsGene Expression RegulationHeLa CellsHematopoietic Stem CellsHumansIntegrinsMiceMusclesNIH 3T3 CellsProtein BindingProtein Structure, TertiarySubstrate SpecificitySuppressor of Cytokine Signaling ProteinsConceptsN-terminal regionHematopoietic cellsE3 ubiquitin ligase complexE3 ubiquitin ligase functionShort N-terminal regionUbiquitin ligase complexUbiquitin ligase functionAcid-responsive genesIntegrin-dependent adhesionRetinoic acid-responsive geneCell fateLigase complexSpecificity subunitLigase functionResponsive genesLeukemia cellsProteasomal degradationNovel regulatorFilamin A.Myogenic differentiationStructural insightsASB2αΒ-integrinAcute promyelocytic leukemia cellsStructural homology