2010
Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients
Kenniston JA, Lemmon MA. Dynamin GTPase regulation is altered by PH domain mutations found in centronuclear myopathy patients. The EMBO Journal 2010, 29: 3054-3067. PMID: 20700106, PMCID: PMC2944063, DOI: 10.1038/emboj.2010.187.Peer-Reviewed Original ResearchConceptsDynamin GTPase activityPH domain mutationsGTPase activityCNM mutationsConformational changesLarge GTPase dynaminGTP hydrolysis cycleC-terminal α-helixPleckstrin homology domainLow-resolution structureDomain mutationsReceptor-mediated endocytosisGTPase dynaminGTPase regulationPH domainScission functionCellular processesGTPase activationDynaminDomain rearrangementsVesicle invaginationGTPase rateCentronuclear myopathyHydrolysis cycleΑ-helix
1994
Specificity and promiscuity in membrane helix interactions
Lemmon M, Engelman D. Specificity and promiscuity in membrane helix interactions. Quarterly Reviews Of Biophysics 1994, 27: 157-218. PMID: 7984776, DOI: 10.1017/s0033583500004522.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsTransmembrane α-helicesMembrane proteinsΑ-helixMembrane protein foldingMembrane-spanning portionTransmembrane helix associationHelix-helix interactionsParticular helicesProtein foldingHelix associationHelix interactionsProsthetic groupLipid bilayersCharge-charge interactionsStereochemical fitFoldingProteinAccessible statesSpecificityOligomerizationInteractionPromiscuityHelixAssemblyA dimerization motif for transmembrane α–helices
Lemmon M, Treutlein H, Adams P, Brünger A, Engelman D. A dimerization motif for transmembrane α–helices. Nature Structural & Molecular Biology 1994, 1: 157-163. PMID: 7656033, DOI: 10.1038/nsb0394-157.Peer-Reviewed Original ResearchConceptsTransmembrane α-helicesHydrophobic transmembrane α-helicesSpecific helix-helix interactionsΑ-helixIntegral membrane proteinsHelix-helix interactionsHelix-helix interfaceDimerization motifSpecific dimerizationMembrane proteinsHelix associationFunctional analysisAmino acidsSuch motifsLipid bilayersMotifParticular motifsFoldingDimerizationSuch interactionsComplex membranesProteinOligomerizationVariety of systemsInteraction
1992
Helix-helix interactions inside lipid bilayers
Lemmon M, Engelman D. Helix-helix interactions inside lipid bilayers. Current Opinion In Structural Biology 1992, 2: 511-518. PMCID: PMC7133266, DOI: 10.1016/0959-440x(92)90080-q.Peer-Reviewed Original ResearchTransmembrane α-helicesHelix-helix interactionsΑ-helixSingle transmembrane α-helixMechanism of transmembraneIntegral membrane proteinsNumber of proteinsMembrane-bound receptorsTransmembrane helicesInterhelical salt bridgesMembrane proteinsSoluble proteinSuch oligomerizationEndoplasmic reticulumHydrophobic anchorSuch helicesProteinLipid bilayersSalt bridgePacking interactionsOligomerizationSpecific interactionsCrystallographic studiesHelixGolgi