2023
ALK inhibitors increase ALK expression and sensitize neuroblastoma cells to ALK.CAR-T cells
Bergaggio E, Tai W, Aroldi A, Mecca C, Landoni E, Nüesch M, Mota I, Metovic J, Molinaro L, Ma L, Alvarado D, Ambrogio C, Voena C, Blasco R, Li T, Klein D, Irvine D, Papotti M, Savoldo B, Dotti G, Chiarle R. ALK inhibitors increase ALK expression and sensitize neuroblastoma cells to ALK.CAR-T cells. Cancer Cell 2023, 41: 2100-2116.e10. PMID: 38039964, PMCID: PMC10793157, DOI: 10.1016/j.ccell.2023.11.004.Peer-Reviewed Original ResearchConceptsALK inhibitorsALK expressionChimeric antigen receptor TBest tumor antigensPromising clinical activityExpression of ALKMost normal tissuesHematologic malignanciesClinical activityMost neuroblastomasAnaplastic lymphoma kinase (ALK) receptorTherapeutic successTumor antigensPotent efficacySolid tumorsTherapeutic efficacyNeuroblastomaTumor growthOncogenic driversNeuroblastoma cellsNormal tissuesALKKinase receptorsMonotherapyInhibitors
2001
High-Affinity Binding of a FYVE Domain to Phosphatidylinositol 3-Phosphate Requires Intact Phospholipid but Not FYVE Domain Oligomerization †
Sankaran V, Klein D, Sachdeva M, Lemmon M. High-Affinity Binding of a FYVE Domain to Phosphatidylinositol 3-Phosphate Requires Intact Phospholipid but Not FYVE Domain Oligomerization †. Biochemistry 2001, 40: 8581-8587. PMID: 11456498, DOI: 10.1021/bi010425d.Peer-Reviewed Original ResearchMeSH KeywordsBinding, CompetitiveBlood ProteinsCarrier ProteinsCation Transport ProteinsGlutathione TransferaseGuanine Nucleotide Exchange FactorsHeLa CellsHumansLiposomesMonosaccharide Transport ProteinsPhosphatidylinositol PhosphatesPhospholipidsPhosphoproteinsProtein BindingProtein Structure, TertiaryProteinsRecombinant Fusion ProteinsSymportersZinc FingersConceptsFYVE domainPH domainDomain oligomerizationSpecific PH domainsVacuolar protein sortingPleckstrin homology domainLipid headgroupsProtein sortingMembrane trafficHomology domainSpecific phosphoinositideLike domainEndosomal maturationHigh-affinity bindingPreferred lipidPhospholipase CPhosphoinositideIntact lipidsIntact phospholipidsOligomerizationDomainMembrane
1998
Specificity and Promiscuity in Phosphoinositide Binding by Pleckstrin Homology Domains*
Kavran J, Klein D, Lee A, Falasca M, Isakoff S, Skolnik E, Lemmon M. Specificity and Promiscuity in Phosphoinositide Binding by Pleckstrin Homology Domains*. Journal Of Biological Chemistry 1998, 273: 30497-30508. PMID: 9804818, DOI: 10.1074/jbc.273.46.30497.Peer-Reviewed Original ResearchConceptsPleckstrin homology domainPH domainGrp1 PH domainD-myo-inositolParticular phosphoinositidesPhosphoinositide bindingHomology domainDependent membrane recruitmentDifferent PH domainsPH domain bindsSmall protein modulesSoluble inositol phosphatesMembrane recruitmentDomain bindsProtein modulesSpecific phosphoinositideMammalian cellsPlasma membraneSingle speciesAbundant speciesMultiple phosphoinositidesCellular membranesPhosphoinositidePI 3Clear specificity