Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published December 26, 2008 | Supplemental Material
Journal Article Open

A Fence-like Coat for the Nuclear Pore Membrane

Abstract

We recently proposed a cylindrical coat for the nuclear pore membrane in the nuclear pore complex (NPC). This scaffold is generated by multiple copies of seven nucleoporins. Here, we report three crystal structures of the nucleoporin pair Seh1•Nup85, which is part of the coat cylinder. The Seh1•Nup85 assembly bears resemblance in its shape and dimensions to that of another nucleoporin pair, Sec13•Nup145C. Furthermore, the Seh1•Nup85 structures reveal a hinge motion that may facilitate conformational changes in the NPC during import of integral membrane proteins and/or during nucleocytoplasmic transport. We propose that Seh1•Nup85 and Sec13•Nup145C form 16 alternating, vertical rods that are horizontally linked by the three remaining nucleoporins of the coat cylinder. Shared architectural and mechanistic principles with the COPII coat indicate a common evolutionary origin and support the notion that the NPC coat represents another class of membrane coats.

Additional Information

© 2008 Elsevier Inc. Under an Elsevier user license. Received 8 September 2008, Revised 21 November 2008, Accepted 2 December 2008, Available online 24 December 2008. We thank O. Dreesen, I. Melčák, V. Nagy, J. Napetschnig, A. Patke, and P. Stavropoulos for discussions and comments on the manuscript; S. Etherton for help with editing the manuscript; D. King for mass spectrometry analysis; P. Stavropoulos and E. Hurt for providing material; and J. Champagne for assistance with the light scattering analysis. In addition, we thank C. Ralston (ALS), M. Becker and R. Fischetti (GM/CA-CAT), K. Rajashankar and N. Sukumar (NE-CAT), and W. Shi (NSLS) for support during data collection. N-terminal protein sequencing was performed by the Protein Center of the Rockefeller University; analytical ultracentrifugation was carried out by the Wadsworth Center Biochemistry Core Facility. E.W.D. is the Dale F. and Betty Ann Frey Fellow of the Damon Runyon Cancer Research Foundation, DRG-1977-08. A.H. was supported by a grant from the Leukemia and Lymphoma Society. Accession Numbers: The atomic coordinates and structure factors of the three crystal structures have been deposited to the Protein Data Bank with the accession codes 3F3F, 3F3G, and 3F3P.

Attached Files

Supplemental Material - 1-s2.0-S109727650800840X-mmc1.pdf

Supplemental Material - 1-s2.0-S109727650800840X-mmc2.mov

Supplemental Material - 1-s2.0-S109727650800840X-mmc3.mov

Supplemental Material - 1-s2.0-S109727650800840X-mmc4.mov

Supplemental Material - 1-s2.0-S109727650800840X-mmc5.mov

Supplemental Material - 1-s2.0-S109727650800840X-mmc6.mov

Supplemental Material - 1-s2.0-S109727650800840X-mmc7.mov

Files

1-s2.0-S109727650800840X-mmc1.pdf
Files (52.0 MB)
Name Size Download all
md5:7cbdc6bac6bcbe58854c6d74bb9b4f86
10.3 MB Download
md5:848c62d3f472913ab9c483d269a62d0c
5.8 MB Download
md5:8ad2eb9e81b2ee5a1368ca1dc783c65e
5.3 MB Download
md5:7683511dbaf8957f25d000e769e69656
12.7 MB Preview Download
md5:51ed1cb4fd78615f25ae72ced8972033
7.9 MB Download
md5:6531aee584595069f1458fcb2a4fc57d
4.0 MB Download
md5:c6e111e12d03e82e0a0a5370e83807e5
6.0 MB Download

Additional details

Created:
August 22, 2023
Modified:
October 20, 2023