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Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex.

Bilokapic S, Schwartz TU
Proc Natl Acad Sci U S A 109 15241-6 (2012)
Related entries: 4fcc, 4fhl, 4fhm

Cited: 49 times
EuropePMC logo PMID: 22955883

Abstract

Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous assemblies composed of multiple copies of ~30 different proteins called nucleoporins. To unravel the basic scaffold underlying the NPC, we have characterized the species-specific scaffold nucleoporin Nup37 and ELY5/ELYS. Both proteins integrate directly via Nup120/160 into the universally conserved heptameric Y-complex, the critical unit for the assembly and functionality of the NPC. We present the crystal structure of Schizosaccharomyces pombe Nup37 in complex with Nup120, a 174-kDa subassembly that forms one of the two short arms of the Y-complex. Nup37 binds near the bend of the L-shaped Nup120 protein, potentially stabilizing the relative orientation of its two domains. By means of reconstitution assays, we pinpoint residues crucial for this interaction. In vivo and in vitro results show that ELY5 binds near an interface of the Nup120-Nup37 complex. Complementary biochemical and cell biological data refine and consolidate the interactions of Nup120 within the current Y-model. Finally, we propose an orientation of the Y-complex relative to the pore membrane, consistent with the lattice model.

Reviews - 4fhn mentioned but not cited (2)

  1. The Structure of the Nuclear Pore Complex (An Update). Lin DH, Hoelz A. Annu Rev Biochem 88 725-783 (2019)
  2. The Structure Inventory of the Nuclear Pore Complex. Schwartz TU. J Mol Biol 428 1986-2000 (2016)

Articles - 4fhn mentioned but not cited (3)

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  2. Structure and gating of the nuclear pore complex. Eibauer M, Pellanda M, Turgay Y, Dubrovsky A, Wild A, Medalia O. Nat Commun 6 7532 (2015)
  3. Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex. Bilokapic S, Schwartz TU. Proc Natl Acad Sci U S A 109 15241-15246 (2012)


Reviews citing this publication (6)

  1. The Nuclear Pore Complex as a Flexible and Dynamic Gate. Knockenhauer KE, Schwartz TU. Cell 164 1162-1171 (2016)
  2. Towards understanding nuclear pore complex architecture and dynamics in the age of integrative structural analysis. Hurt E, Beck M. Curr Opin Cell Biol 34 31-38 (2015)
  3. Functional insights from studies on the structure of the nuclear pore and coat protein complexes. Schwartz T. Cold Spring Harb Perspect Biol 5 a013375 (2013)
  4. Nucleoporins in cardiovascular disease. Burdine RD, Preston CC, Leonard RJ, Bradley TA, Faustino RS. J Mol Cell Cardiol 141 43-52 (2020)
  5. The Role of Nucleoporin Elys in Nuclear Pore Complex Assembly and Regulation of Genome Architecture. Shevelyov YY. Int J Mol Sci 21 E9475 (2020)
  6. Nuclear Import and Export of YAP and TAZ. Kofler M, Kapus A. Cancers (Basel) 15 4956 (2023)

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  13. A short linear motif in scaffold Nup145C connects Y-complex with pre-assembled outer ring Nup82 complex. Teimer R, Kosinski J, von Appen A, Beck M, Hurt E. Nat Commun 8 1107 (2017)
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  36. Significantly high expression of NUP37 leads to poor prognosis of glioma patients by promoting the proliferation of glioma cells. Liu Z, Wang H, Jia Y, Wang J, Wang Y, Bian L, Liu B, Lian X, Zhang B, Ren Z, Zhang W, Dai W, Gao Y. Cancer Med 10 5218-5234 (2021)
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