@article{e9efa62f108a404c9ae06d6972592473,
title = "Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex",
abstract = "The membrane ring that equatorially circumscribes the nuclear pore complex (NPC) in the perinuclear lumen of the nuclear envelope is composed largely of Pom152 in yeast and its ortholog Nup210 (or Gp210) in vertebrates. Here, we have used a combination of negative-stain electron microscopy, nuclear magnetic resonance, and small-angle X-ray scattering methods to determine an integrative structure of the ∼120 kDa luminal domain of Pom152. Our structural analysis reveals that the luminal domain is formed by a flexible string-of-pearls arrangement of nine repetitive cadherin-like Ig-like domains, indicating an evolutionary connection between NPCs and the cell adhesion machinery. The 16 copies of Pom152 known to be present in the yeast NPC are long enough to form the observed membrane ring, suggesting how interactions between Pom152 molecules help establish and maintain the NPC architecture.",
keywords = "Gp210, NMR, Nup210, Pom152, SAXS, cadherin, electron microscopy, integrative structure determination, nuclear pore complex, nucleoporin",
author = "Paula Upla and Kim, {Seung Joong} and Parthasarathy Sampathkumar and Kaushik Dutta and Cahill, {Sean M.} and Chemmama, {Ilan E.} and Rosemary Williams and Bonanno, {Jeffrey B.} and Rice, {William J.} and Stokes, {David L.} and David Cowburn and Almo, {Steven C.} and Andrej Sali and Rout, {Michael P.} and Javier Fernandez-Martinez",
note = "Funding Information: We thank NYULMC OCS Microscopy Core for assistance with negative-stain EM, NYSGRC for providing samples for SAXS and NMR analyses; and T. Matsui and T.M. Weiss at SSRL, SLAC National Accelerator Laboratory, for assistance with collecting SAXS data. The instrumentation in the Einstein NMR Resource is supported by the Albert Einstein College of Medicine, and the Bruker 600 NMR instrument was purchased using funds from NIH award 1S10OD016305. Some of the NMR experiments were performed at the New York Structural Biology Center, which is a STAR center supported by the New York Office of Science, Technology and Academic Research. The New York Structural Biology Center is supported by grant number 349247 from the Simons Foundation. Support was provided by NSF GRF (no. 1650113) (I.E.C.); and NIH grants U54 RR022220 to B.C., A.S., and M.R.; R01 GM112108 to M.R.; U54GM094662 to S.C.A; GM 117212 to D.C.; P41 GM109824 to M.R., A.S., and B.C.; U01GM098256 to M.P.R.; P41 GM103314 to B.C.; and R01 GM083960 to A.S. Publisher Copyright: {\textcopyright} 2017 Elsevier Ltd",
year = "2017",
month = mar,
day = "7",
doi = "10.1016/j.str.2017.01.006",
language = "English (US)",
volume = "25",
pages = "434--445",
journal = "Structure with Folding & design",
issn = "0969-2126",
publisher = "Cell Press",
number = "3",
}