Toward a more complete 3-D structure of the nuclear pore complex - PubMed (original) (raw)
Toward a more complete 3-D structure of the nuclear pore complex
M Jarnik et al. J Struct Biol. 1991 Dec.
Abstract
The nuclear pore complex (NPC) is a large supramolecular assembly embedded in the double-membraned nuclear envelope (NE) that plays a pivotal role in the exchange of macromolecules and particles between the nucleus and the cytoplasm. Applying various methods of sample preparation to Xenopus laevis whole nuclei and isolated NEs in combination with conventional transmission electron microscopy and digital image processing, we have characterized several distinct components of the NPC, including massive cytoplasmic and more tenuous nuclear rings, NPCs devoid of their cytoplasmic or both rings, and prominent "knobs" that protrude from the periphery of the NPC proper into the lumen of the NE. Moreover, by quick freezing/freeze drying/rotary metal shadowing isolated NEs, we have visualized two distinct types of NPC-associated filaments: (1) eight short, highly twisted filaments that project from the cytoplasmic ring and sometimes collapse into short cylinders; and (2) eight long, thin filaments that protrude from the nuclear ring and whose ends join to form a distal ring centered above the NPC such that the assembly resembles a "fishtrap." These nuclear fishtraps are sensitive to divalent cations: removal unfolds them and addition reforms them. The significance of these various structural components in terms of current NPC models is discussed, and the emerging asymmetry of the NPC relative to its nuclear and cytoplasmic face is stressed.
Similar articles
- Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex.
Zhu X, Huang G, Zeng C, Zhan X, Liang K, Xu Q, Zhao Y, Wang P, Wang Q, Zhou Q, Tao Q, Liu M, Lei J, Yan C, Shi Y. Zhu X, et al. Science. 2022 Jun 10;376(6598):eabl8280. doi: 10.1126/science.abl8280. Epub 2022 Jun 10. Science. 2022. PMID: 35679404 - Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components.
Reichelt R, Holzenburg A, Buhle EL Jr, Jarnik M, Engel A, Aebi U. Reichelt R, et al. J Cell Biol. 1990 Apr;110(4):883-94. doi: 10.1083/jcb.110.4.883. J Cell Biol. 1990. PMID: 2324201 Free PMC article. - Interactions and three-dimensional localization of a group of nuclear pore complex proteins.
Panté N, Bastos R, McMorrow I, Burke B, Aebi U. Panté N, et al. J Cell Biol. 1994 Aug;126(3):603-17. doi: 10.1083/jcb.126.3.603. J Cell Biol. 1994. PMID: 8045926 Free PMC article. - Function and assembly of nuclear pore complex proteins.
Bodoor K, Shaikh S, Enarson P, Chowdhury S, Salina D, Raharjo WH, Burke B. Bodoor K, et al. Biochem Cell Biol. 1999;77(4):321-9. Biochem Cell Biol. 1999. PMID: 10546895 Review. - Molecular dissection of the nuclear pore complex.
Panté N, Aebi U. Panté N, et al. Crit Rev Biochem Mol Biol. 1996 Apr;31(2):153-99. doi: 10.3109/10409239609106583. Crit Rev Biochem Mol Biol. 1996. PMID: 8740526 Review.
Cited by
- An evolutionarily conserved bimodular domain anchors ZC3HC1 and its yeast homologue Pml39p to the nuclear basket.
Gunkel P, Iino H, Krull S, Cordes VC. Gunkel P, et al. Mol Biol Cell. 2023 May 1;34(5):ar40. doi: 10.1091/mbc.E22-09-0402. Epub 2023 Mar 1. Mol Biol Cell. 2023. PMID: 36857168 Free PMC article. - Nup358/RanBP2 attaches to the nuclear pore complex via association with Nup88 and Nup214/CAN and plays a supporting role in CRM1-mediated nuclear protein export.
Bernad R, van der Velde H, Fornerod M, Pickersgill H. Bernad R, et al. Mol Cell Biol. 2004 Mar;24(6):2373-84. doi: 10.1128/MCB.24.6.2373-2384.2004. Mol Cell Biol. 2004. PMID: 14993277 Free PMC article. - Calmodulin activates nuclear protein import: a link between signal transduction and nuclear transport.
Sweitzer TD, Hanover JA. Sweitzer TD, et al. Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14574-9. doi: 10.1073/pnas.93.25.14574. Proc Natl Acad Sci U S A. 1996. PMID: 8962094 Free PMC article. - Nup120p: a yeast nucleoporin required for NPC distribution and mRNA transport.
Aitchison JD, Blobel G, Rout MP. Aitchison JD, et al. J Cell Biol. 1995 Dec;131(6 Pt 2):1659-75. doi: 10.1083/jcb.131.6.1659. J Cell Biol. 1995. PMID: 8557736 Free PMC article.