Structure, Dynamics, Evolution, and Function of a Major Scaffold Component in the Nuclear Pore Complex

Sampathkumar, Parthasarathy; Kim, Seung Joong; Upla, Paula; Rice, William J.; Phillips, Jeremy; Timney, Benjamin L.; Pieper, Ursula; Bonanno, Jeffrey B.; Fernandez-Martinez, Javier; Hakhverdyan, Zhanna; Ketaren, Natalia E.; Matsui, Tsutomu; Weiss, Thomas M.; Stokes, David L.; Sauder, J. Michael; Burley, Stephen K.; Sali, Andrej; Rout, Michael P.; Almo, Steven C.

doi:10.1016/j.str.2013.02.005

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Structure, Dynamics, Evolution, and Function of a Major Scaffold Component in the Nuclear Pore Complex

Published Date:

Mar 14 2013

Publisher's site:

http://dx.doi.org/10.1016/j.str.2013.02.005 New Site Icon

Source:

Structure. 2013; 21(4):560-571.

[PDF - 3.09 MB]

Details:

Personal Authors:

Sampathkumar, Parthasarathy ; Kim, Seung Joong ; Upla, Paula ; Rice, William J. ; Phillips, Jeremy ; ... More ▼

Keywords:

[+]

Pubmed ID:

23499021

Pubmed Central ID:

PMC3755625

Description:

The nuclear pore complex, composed of proteins termed nucleoporins (Nups), is responsible for nucleocytoplasmic transport in eukaryotes. Nuclear pore complexes (NPCs) form an annular structure composed of the nuclear ring, cytoplasmic ring, a membrane ring, and two inner rings. Nup192 is a major component of the NPC's inner ring. We report the crystal structure of Saccharomyces cerevisiae Nup192 residues 2-960 [ScNup192(2-960)], which adopts an α-helical fold with three domains (i.e., D1, D2, and D3). Small angle X-ray scattering and electron microscopy (EM) studies reveal that ScNup192(2-960) could undergo long-range transition between "open" and "closed" conformations. We obtained a structural model of full-length ScNup192 based on EM, the structure of ScNup192(2-960), and homology modeling. Evolutionary analyses using the ScNup192(2-960) structure suggest that NPCs and vesicle-coating complexes are descended from a common membrane-coating ancestral complex. We show that suppression of Nup192 expression leads to compromised nuclear transport and hypothesize a role for Nup192 in modulating the permeability of the NPC central channel.

Document Type:

Journal Article

Collection(s):

CDC Public Access

Funding:

C06 RR017528-01-CEM/CE/NCIPC CDC HHS/United States
P30-EB-009998/EB/NIBIB NIH HHS/United States
P41GM103393/GM/NIGMS NIH HHS/United States
P41RR001209/RR/NCRR NIH HHS/United States
R01 GM062427/GM/NIGMS NIH HHS/United States
R01 GM071329/GM/NIGMS NIH HHS/United States
R01 GM083960/GM/NIGMS NIH HHS/United States
R01 GM083960/GM/NIGMS NIH HHS/United States
U01 GM098256/GM/NIGMS NIH HHS/United States
U01 GM098256/GM/NIGMS NIH HHS/United States
U54 GM074945/GM/NIGMS NIH HHS/United States
U54 GM094662/GM/NIGMS NIH HHS/United States
U54 GM103511/GM/NIGMS NIH HHS/United States
U54 GM103511/GM/NIGMS NIH HHS/United States

Supporting Files:

NIHMS458017-supplement-1.pdf	application/pdf
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