title: Super-resolution 3D tomography of interactions and competition in the nuclear pore complex.
abstract: A selective barrier formed by intrinsically disordered Phe-Gly (FG) nucleoporins (Nups) allows transport receptor (TR)-facilitated translocation of signal-dependent cargos through the nuclear pore complexes (NPCs) of eukaryotic cells. However, the configuration of the FG-Nup barrier and its interactions with multiple TRs in native NPCs remain obscure. Here, we mapped the interaction sites of various TRs or FG segments within the FG-Nup barrier by using high-speed super-resolution microscopy and used these sites to reconstruct the three-dimensional tomography of the native barrier in the NPC. We found that each TR possesses a unique interaction zone within the FG-Nup barrier and that two major TRs, importin β1 and Crm1, outcompete other TRs in binding FG Nups. Moreover, TRs may alter the tomography of the FG-Nup barrier and affect one another's pathways under circumstances of heavy competition.
authors.affiliation: Department of Biology, Temple University, Philadelphia, Pennsylvania, USA.
authors.forename: Jiong
authors.initials: J
authors.lastname: Ma
authors.affiliation: Department of Biology, Temple University, Philadelphia, Pennsylvania, USA.
authors.forename: Alexander
authors.initials: A
authors.lastname: Goryaynov
authors.affiliation: Department of Biology, Temple University, Philadelphia, Pennsylvania, USA.
authors.forename: Weidong
authors.initials: W
authors.lastname: Yang
mesh_terms: D006367:HeLa Cells; D006801:Humans; D021621:Imaging, Three-Dimensional; D022022:Nuclear Pore / Q000737:chemistry* / Q000378:metabolism*; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry / Q000378:metabolism; D029543:Nucleocytoplasmic Transport Proteins / Q000737:chemistry / Q000378:metabolism; D025941:Protein Interaction Mapping; D014054:Tomography / Q000379:methods*
chemical_list: D028861:Nuclear Pore Complex Proteins; D029543:Nucleocytoplasmic Transport Proteins