| Structural highlights
Function
[PO152_YEAST] Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. POM152 is important for the de novo assembly of NPCs.[1] [2] [3]
Publication Abstract from PubMed
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 approximately 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.
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex.,Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J Structure. 2017 Mar 7;25(3):434-445. doi: 10.1016/j.str.2017.01.006. Epub 2017, Feb 2. PMID:28162953[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Marelli M, Lusk CP, Chan H, Aitchison JD, Wozniak RW. A link between the synthesis of nucleoporins and the biogenesis of the nuclear envelope. J Cell Biol. 2001 May 14;153(4):709-24. PMID:11352933
- ↑ Nehrbass U, Rout MP, Maguire S, Blobel G, Wozniak RW. The yeast nucleoporin Nup188p interacts genetically and physically with the core structures of the nuclear pore complex. J Cell Biol. 1996 Jun;133(6):1153-62. PMID:8682855
- ↑ Tcheperegine SE, Marelli M, Wozniak RW. Topology and functional domains of the yeast pore membrane protein Pom152p. J Biol Chem. 1999 Feb 19;274(8):5252-8. PMID:9988776
- ↑ Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J. Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure. 2017 Mar 7;25(3):434-445. doi: 10.1016/j.str.2017.01.006. Epub 2017, Feb 2. PMID:28162953 doi:http://dx.doi.org/10.1016/j.str.2017.01.006
|
