A perinuclear α-helix with amphipathic features in Brl1 promotes NPC assembly
Jlenia Vitale, Azqa Khan, Annett Neuner, Elmar Schiebel
Abstract
expression triggers mislocalization of Nup159 and Nup42 and to a lesser extent Nsp1, which localize on the cytoplasmic face of the NPC. The DAH also contributes to the function of Brl1, and AαH has functions independent of DAH. We propose that AαH and DAH in Brl1 promote INM/ONM fusion during NPC assembly.
Topics & Concepts
NucleoporinNuclear poreCell biologyBiologyCytoplasmInner membraneLipid bilayer fusionMutantMembraneMembrane proteinFunction (biology)NLSBiophysicsCell membraneNuclear proteinCell nucleusNuclear localization sequenceNuclear transportTransport proteinNuclear membraneNuclear laminaVesicular Transport ProteinsMutationBuddingFusion proteinPlasma protein bindingViral envelopeProtein structureMembrane curvatureBacterial outer membraneIntegral membrane proteinNuclear Structure and FunctionCellular transport and secretionRNA Research and Splicing