2020
Nucleoplasmic signals promote directed transmembrane protein import simultaneously via multiple channels of nuclear pores
Mudumbi KC, Czapiewski R, Ruba A, Junod SL, Li Y, Luo W, Ngo C, Ospina V, Schirmer EC, Yang W. Nucleoplasmic signals promote directed transmembrane protein import simultaneously via multiple channels of nuclear pores. Nature Communications 2020, 11: 2184. PMID: 32366843, PMCID: PMC7198523, DOI: 10.1038/s41467-020-16033-x.Peer-Reviewed Original ResearchConceptsMembrane proteinsInner nuclear membrane proteinCentral channelEukaryotic transmembrane proteinsNuclear membrane proteinsNuclear localization signalNuclear pore complexCertain membrane proteinsCentral outstanding questionsSingle-molecule microscopyProtein importProtein translocationLocalization signalPore complexNuclear transportBlock translocationTransmembrane proteinNuclear poresSuch proteinsProtein targetsNuclear membraneProteinTranslocationOutstanding questionsChannel transport
2016
Probing Protein Distribution Along the Nuclear Envelope In Vivo by Using Single-Point FRAP
Mudumbi K, Yang W. Probing Protein Distribution Along the Nuclear Envelope In Vivo by Using Single-Point FRAP. Methods In Molecular Biology 2016, 1411: 113-122. PMID: 27147037, PMCID: PMC10099394, DOI: 10.1007/978-1-4939-3530-7_6.Peer-Reviewed Original ResearchConceptsNuclear envelope transmembrane proteinsNuclear membrane proteinsEnvelope transmembrane proteinsInner nuclear membraneNuclear envelope membranesWeeks-long processEnvelope membraneMembrane proteinsTransmembrane proteinNuclear envelopeNuclear membraneProtein distributionFluorescence recoveryStaining of cellsProteinMembraneElectron microscopy
2013
The Pathogenic A391E Mutation in FGFR3 Induces a Structural Change in the Transmembrane Domain Dimer
Mudumbi K, Julius A, Herrmann J, Li E. The Pathogenic A391E Mutation in FGFR3 Induces a Structural Change in the Transmembrane Domain Dimer. The Journal Of Membrane Biology 2013, 246: 487-493. PMID: 23727984, DOI: 10.1007/s00232-013-9563-6.Peer-Reviewed Original ResearchConceptsFGFR3 transmembrane domainFibroblast growth factor receptor 3Transmembrane domainA391E mutationSingle-pass membrane proteinCytosolic kinase domainTransmembrane domain dimerReceptor tyrosine kinase familyTyrosine kinase familyGrowth factor receptor 3TMD dimersCytosolic domainKinase familyTransmembrane proteinMembrane proteinsKinase domainDomain dimerExtracellular domainGenetic studiesDistinct domainsActivity assaysStable dimerCranial dysplasiaMutationsMotif