2009
A PH domain within OCRL bridges clathrin‐mediated membrane trafficking to phosphoinositide metabolism
Mao Y, Balkin DM, Zoncu R, Erdmann KS, Tomasini L, Hu F, Jin MM, Hodsdon ME, De Camilli P. A PH domain within OCRL bridges clathrin‐mediated membrane trafficking to phosphoinositide metabolism. The EMBO Journal 2009, 28: 1831-1842. PMID: 19536138, PMCID: PMC2711190, DOI: 10.1038/emboj.2009.155.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesClathrinCoated VesiclesEndocytosisHeLa CellsHumansModels, MolecularMolecular Sequence DataMutationNuclear Magnetic Resonance, BiomolecularPhosphatidylinositolsPhospholipidsPhosphoric Monoester HydrolasesProtein ConformationProtein Structure, TertiaryRatsSequence AlignmentConceptsPH domainNH2-terminal portionEndocytic clathrin-coated pitsClathrin-binding siteClathrin-coated pitsNMR structure determinationNH2-terminal regionCOOH-terminal regionClathrin-box motifsMembrane traffickingEvolutionary pressureSimilar proteinsINPP5BOCRLSpecialized functionsSequence dissimilarityLowe syndromePhosphoinositide metabolismDent's diseaseHeavy chainMutationsRecruitment efficiencyStructure determinationMetabolismDomain
2006
Solution structure and backbone dynamics of an N‐terminal ubiquitin‐like domain in the GLUT4‐regulating protein, TUG
Tettamanzi MC, Yu C, Bogan JS, Hodsdon ME. Solution structure and backbone dynamics of an N‐terminal ubiquitin‐like domain in the GLUT4‐regulating protein, TUG. Protein Science 2006, 15: 498-508. PMID: 16501224, PMCID: PMC2249771, DOI: 10.1110/ps.051901806.Peer-Reviewed Original ResearchConceptsN-terminal ubiquitin-like domainUbiquitin-like domainC-terminal diglycine motifPotential protein-protein interaction sitesN-terminal UBL domainAcceptor lysine residuesBackbone dynamicsProtein-protein interactionsProtein-protein interaction sitesSpecific cellular processesUbiquitin-proteasome pathwayLack of conservationProtein modification reactionUBL domainCellular processesDiglycine motifExocytic machineryUbiquitin recognitionAcceptor lysinePlasma membraneMolecular basisInsulin stimulationLysine residuesMembrane vesiclesTertiary structure
2004
Consequences of Binding an S-Adenosylmethionine Analogue on the Structure and Dynamics of the Thiopurine Methyltransferase Protein Backbone †
Scheuermann TH, Keeler C, Hodsdon ME. Consequences of Binding an S-Adenosylmethionine Analogue on the Structure and Dynamics of the Thiopurine Methyltransferase Protein Backbone †. Biochemistry 2004, 43: 12198-12209. PMID: 15379558, DOI: 10.1021/bi0492556.Peer-Reviewed Original ResearchConceptsNMR chemical shift mapping experimentsChemical shift mapping experimentsNative structureS-adenosylmethionineProteasomal-dependent pathwayCatalytic mechanismProtein backboneIntracellular degradationIndirect conformational changesS-adenosylmethionine analogPresence of sinefunginBacterial orthologuesChemical shift changesProtein backbone dynamicsPseudomonas syringaeSubstrate recognitionProtein sequencesSAM analoguesConformational changesNMR spectroscopyBackbone dynamicsMapping experimentsBackbone mobilitySinefunginNMR relaxation