2022
The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release
Gray S, Cao W, Montpetit B, De La Cruz EM. The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release. Nucleic Acids Research 2022, 50: 3998-4011. PMID: 35286399, PMCID: PMC9023272, DOI: 10.1093/nar/gkac164.Peer-Reviewed Original ResearchConceptsNuclear pore complexRNA exportDEAD-box protein Dbp5ATPase cycleDbp5's ATPase activityDEAD (Asp-Glu-Ala-Asp) box protein 5Pore complexDbp5ATP bindingATPase cyclingNucleotide stateCytoplasmic faceGle1Pool of ATPADP-PiGene expressionProtein 5Mechanistic understandingNucleoporinsNup159ATPase activityATP dissociationATPPi releasePi release rate
2013
Molecular Basis of Purinergic Signal Metabolism by Ectonucleotide Pyrophosphatase/Phosphodiesterases 4 and 1 and Implications in Stroke*♦
Albright RA, Ornstein DL, Cao W, Chang WC, Robert D, Tehan M, Hoyer D, Liu L, Stabach P, Yang G, De La Cruz EM, Braddock DT. Molecular Basis of Purinergic Signal Metabolism by Ectonucleotide Pyrophosphatase/Phosphodiesterases 4 and 1 and Implications in Stroke*♦. Journal Of Biological Chemistry 2013, 289: 3294-3306. PMID: 24338010, PMCID: PMC3916532, DOI: 10.1074/jbc.m113.505867.Peer-Reviewed Original ResearchConceptsExtracellular membrane proteinsMembrane proteinsSubstrate specificityMolecular basisHigh-resolution crystal structuresResolution crystal structureComparative structural analysisATP hydrolysisNPP1Brain vascular endotheliumCorresponding regionTerminal phosphateLow nanomolar concentrationsPurinergic signalsPlatelet aggregationProteinATPEnzymeNanomolar concentrationsVascular endotheliumPhosphodiesterases 4Ap3AMetabolismSurface of chondrocytesTissue mineralization
2008
Effects of Solution Crowding on Actin Polymerization Reveal the Energetic Basis for Nucleotide-Dependent Filament Stability
Frederick KB, Sept D, De La Cruz EM. Effects of Solution Crowding on Actin Polymerization Reveal the Energetic Basis for Nucleotide-Dependent Filament Stability. Journal Of Molecular Biology 2008, 378: 540-550. PMID: 18374941, PMCID: PMC2424216, DOI: 10.1016/j.jmb.2008.02.022.Peer-Reviewed Original ResearchConceptsADP-actin filamentsFilament stabilityCell structure maintenanceFundamental cellular processesADP-actinADP-F-actinSolution crowdingCellular processesAllosteric regulatorsMolecular basisRegulatory proteinsActin polymerizationATP hydrolysisActin activityNucleotide hydrolysisFilament subunitsEnergetic basisIntracellular conditionsStructure maintenanceSubunit dissociationStability of ATPATPConcentration-dependent mannerStructural differencesForce generationOverview: Actin-Binding Protein Function and Its Relation to Disease Pathology
Krendel M, De La Cruz E. Overview: Actin-Binding Protein Function and Its Relation to Disease Pathology. Protein Reviews 2008, 65-82. DOI: 10.1007/978-0-387-71749-4_5.Peer-Reviewed Original ResearchFundamental cellular processesForm of ATPHydrolysis of ATPActin cytoskeletonProtein functionCellular processesMyosin familyMotor proteinsActin filamentsActin monomersATP moleculesCell membraneDistinct mechanismsPathogenic bacteriaGenerate movementDisease pathologyATPFilamentsForce generationMotilityCytoskeletonOrganellesChemical energyProteinActin
1998
Interactions of Acanthamoeba Profilin with Actin and Nucleotides Bound to Actin †
Vinson V, De La Cruz E, Higgs H, Pollard T. Interactions of Acanthamoeba Profilin with Actin and Nucleotides Bound to Actin †. Biochemistry 1998, 37: 10871-10880. PMID: 9692980, DOI: 10.1021/bi980093l.Peer-Reviewed Original ResearchConceptsMg-ATPAcanthamoeba profilinMg-ADPExchange of ADPRabbit skeletal muscle actinAffinity of profilinSkeletal muscle actinFree barbed endsProfilin bindingSerine 38Nucleotide exchangeBarbed endsCysteine 374Actin monomersProfilinMuscle actinActinUnique siteIntrinsic fluorescenceFluorescence anisotropyATP-actinSubunit/Free actinSame affinityATP