Upla Paula, Kim Seung Joong, Sampathkumar Parthasarathy, Dutta Kaushik, Cahill Sean M, Chemmama Ilan E, Williams Rosemary, Bonanno Jeffrey B, Rice William J, Stokes David L, Cowburn David, Almo Steven C, Sali Andrej, Rout Michael P, Fernandez-Martinez Javier
Skirball Institute and Department of Cell Biology, New York University School of Medicine, New York, NY 10016, USA; Laboratory of Cellular and Structural Biology, The Rockefeller University, Box 213, 1230 York Avenue, New York, NY 10065, USA.
Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, California Institute for Quantitative Biosciences, UCSF MC 2552, Byers Hall at Mission Bay, 1700 4th Street, Suite 503B, University of California, San Francisco, San Francisco, CA 94158, USA.
Structure. 2017 Mar 7;25(3):434-445. doi: 10.1016/j.str.2017.01.006. Epub 2017 Feb 2.
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.
在核膜核周腔中环绕核孔复合体（NPC）赤道的膜环主要由酵母中的Pom152及其在脊椎动物中的直系同源物Nup210（或Gp210）组成。在这里，我们结合使用负染色电子显微镜、核磁共振和小角X射线散射方法来确定Pom152约120 kDa腔结构域的综合结构。我们的结构分析表明，腔结构域由九个重复的钙黏蛋白样免疫球蛋白样结构域的柔性珠链排列形成，这表明NPC与细胞黏附机制之间存在进化联系。已知存在于酵母NPC中的16个Pom152拷贝足够长，可以形成观察到的膜环，这表明Pom152分子之间的相互作用有助于建立和维持NPC结构。
