Peer-reviewedCC BYMolecular Cell
How the TREX-2 complex associates with the nuclear pore
9 affiliations
- 1Department of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, 60438 Frankfurt am Main, Germany; European Molecular Biology Laboratory Hamburg, Notkestraße 85, 22607 Hamburg, Germany
- 2Department of Structural Biology, Leibniz - Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Roessle-Str. 10, 13125 Berlin, Germany; Absea Biotechnology GmbH, Robert-Roessle-Str. 10, 13125 Berlin, Germany
- 3Department of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, 60438 Frankfurt am Main, Germany; IMPRS on Cellular Biophysics, Max-von-Laue-Straße 3, 60438 Frankfurt am Main, Germany
- 4Department of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, 60438 Frankfurt am Main, Germany
- 5Department of Structural Biology, Leibniz - Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Roessle-Str. 10, 13125 Berlin, Germany
- 6Department of Infectious Diseases, Virology, University of Heidelberg, 69120 Heidelberg, Germany; German Center for Infection Research, partner site Heidelberg, 69120 Heidelberg, Germany
- 7Department of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, 60438 Frankfurt am Main, Germany; Cluster of Excellence SubCellular Architecture of Life (SCALE), Goethe University, Frankfurt, Germany
- 8Department of Structural Biology, Leibniz - Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Roessle-Str. 10, 13125 Berlin, Germany; Absea Biotechnology GmbH, Robert-Roessle-Str. 10, 13125 Berlin, Germany; Charité - Universitätsmedizin Berlin, Charitépl. 1, 10117 Berlin, Germany. Electronic address: [email protected]
- 9Department of Molecular Sociology, Max Planck Institute of Biophysics, Max-von-Laue-Straße 3, 60438 Frankfurt am Main, Germany; Cluster of Excellence SubCellular Architecture of Life (SCALE), Goethe University, Frankfurt, Germany; Institute of Biochemistry, Goethe University Frankfurt, 60438 Frankfurt am Main, Germany. Electronic address: [email protected]
Abstract
Nuclear pore complexes (NPCs) control nucleocytoplasmic transport in eukaryotes, yet their architecture remains incompletely understood. Here, we report a substantially extended structure of the human NPC, obtained by combining cryo-electron tomography, crosslinking mass spectrometry, and AI-assisted integrative modeling. We resolve the molecular arrangement of translocated promoter region (TPR), NUP153, NUP50, and ZC3HC1 and reveal that five additional proteins-TMEM209, SMPD4, GANP, Centrin-2, and ENY2-are incorporated into the NPC. Unexpectedly, GANP, Centrin-2, and ENY2, core members of the TREX-2 mRNA export complex, are built into the nuclear ring. This finding establishes TREX-2 not as a transiently associated factor, but as an integral NPC module, positioning it opposite of the cytoplasmic NUP214 mRNA export platform. Together, our results redefine the molecular composition of the inner ring, nuclear ring, and nuclear basket. They suggest a direct structural basis that couples TREX-2-mediated messenger ribonucleoprotein particle (mRNP) remodeling to NPC-facilitated transport.
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BibTeX
@article{obarskakosinska2026trex2,
title = {{How the TREX-2 complex associates with the nuclear pore}},
author = {Agnieszka Obarska-Kosińska and Ying Zhu and Katharina Geißler and Remus R. E. Rosenkranz and Nanako Yokoyama and Jan Philipp Kreysing and Huaipeng Xing and Desislava Glushkova and Marta Anna Kubańska and Stefanie Böhm and Hans‐Georg Kräusslich and Beata Turoňová and Fan Liu and Martin Beck},
journal = {Molecular Cell},
year = {2026},
month = oct,
doi = {10.1016/j.molcel.2026.10.006},
url = {https://doi.org/10.1016/j.molcel.2026.10.006},
note = {CC BY},
}
RIS
TY - JOUR
TI - How the TREX-2 complex associates with the nuclear pore
AU - Agnieszka Obarska-Kosińska
AU - Ying Zhu
AU - Katharina Geißler
AU - Remus R. E. Rosenkranz
AU - Nanako Yokoyama
AU - Jan Philipp Kreysing
AU - Huaipeng Xing
AU - Desislava Glushkova
AU - Marta Anna Kubańska
AU - Stefanie Böhm
AU - Hans‐Georg Kräusslich
AU - Beata Turoňová
AU - Fan Liu
AU - Martin Beck
PY - 2026
DA - 2026/10/01
JO - Molecular Cell
DO - 10.1016/j.molcel.2026.10.006
UR - https://doi.org/10.1016/j.molcel.2026.10.006
AB - Nuclear pore complexes (NPCs) control nucleocytoplasmic transport in eukaryotes, yet their architecture remains incompletely understood. Here, we report a substantially extended structure of the human NPC, obtained by combining cryo-electron tomography, crosslinking mass spectrometry, and AI-assisted integrative modeling. We resolve the molecular arrangement of translocated promoter region (TPR), NUP153, NUP50, and ZC3HC1 and reveal that five additional proteins-TMEM209, SMPD4, GANP, Centrin-2, and ENY2-are incorporated into the NPC. Unexpectedly, GANP, Centrin-2, and ENY2, core members of the TREX-2 mRNA export complex, are built into the nuclear ring. This finding establishes TREX-2 not as a transiently associated factor, but as an integral NPC module, positioning it opposite of the cytoplasmic NUP214 mRNA export platform. Together, our results redefine the molecular composition of the inner ring, nuclear ring, and nuclear basket. They suggest a direct structural basis that couples TREX-2-mediated messenger ribonucleoprotein particle (mRNP) remodeling to NPC-facilitated transport.
SN - 1097-2765
SN - 1097-4164
ER -