학술논문

Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex
Document Type
article
Source
Structure. 25(3)
Subject
Biochemistry and Cell Biology
Biological Sciences
1.1 Normal biological development and functioning
Underpinning research
Generic health relevance
Cell Adhesion
Membrane Glycoproteins
Models
Molecular
Nuclear Magnetic Resonance
Biomolecular
Nuclear Pore
Protein Domains
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Scattering
Small Angle
X-Ray Diffraction
Gp210
NMR
Nup210
Pom152
SAXS
cadherin
electron microscopy
integrative structure determination
nuclear pore complex
nucleoporin
Chemical Sciences
Information and Computing Sciences
Biophysics
Biological sciences
Chemical sciences
Language
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.