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  Systematic Protein-Protein Interaction Analysis Reveals Intersubcomplex Contacts in the Nuclear Pore Complex

Apelt, L., Knockenhauer, K. E., Leksa, N. C., Benlasfer, N., Schwartz, T. U., & Stelzl, U. (2016). Systematic Protein-Protein Interaction Analysis Reveals Intersubcomplex Contacts in the Nuclear Pore Complex. Molecular and Cellular Proteomics, 15(8), 2594-2606. doi:10.1074/mcp.M115.054627.

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© 2016 American Society for Biochemistry and Molecular Biology
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Apelt, Luise1, Autor           
Knockenhauer, Kevin E. , Autor
Leksa, Nina C. , Autor
Benlasfer, Nouhad1, Autor           
Schwartz, Thomas U. , Autor
Stelzl, Ulrich1, 2, Autor           
Affiliations:
1Molecular Interaction Networks (Ulrich Stelzl), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479660              
2Institute of Pharmaceutical Sciences, Pharmaceutical Chemistry, University of Graz, Graz, Austria, ou_persistent22              

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 Zusammenfassung: The nuclear pore complex (NPC) enables transport across the nuclear envelope. It is one of the largest multiprotein assemblies in the cell, built from about 30 proteins called nucleoporins (Nups), organized into distinct subcomplexes. Structure determination of the NPC is a major research goal. The assembled ∼40-112 MDa NPC can be visualized by cryoelectron tomography (cryo-ET), while Nup subcomplexes are studied crystallographically. Docking the crystal structures into the cryo-ET maps is difficult because of limited resolution. Further, intersubcomplex contacts are not well characterized. Here, we systematically investigated direct interactions between Nups. In a comprehensive, structure-based, yeast two-hybrid interaction matrix screen, we mapped protein-protein interactions in yeast and human. Benchmarking against crystallographic and coaffinity purification data from the literature demonstrated the high coverage and accuracy of the data set. Novel intersubcomplex interactions were validated biophysically in microscale thermophoresis experiments and in intact cells through protein fragment complementation. These intersubcomplex interaction data provide direct experimental evidence toward possible structural arrangements of architectural elements within the assembled NPC, or they may point to assembly intermediates. Our data favors an assembly model in which major architectural elements of the NPC, notably the Y-complex, exist in different structural contexts within the scaffold.

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Sprache(n): eng - English
 Datum: 2016-05-182016-08
 Publikationsstatus: Erschienen
 Seiten: 13
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 Identifikatoren: DOI: 10.1074/mcp.M115.054627
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Titel: Molecular and Cellular Proteomics
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Bethesda, MD : American Society for Biochemistry and Molecular Biology
Seiten: - Band / Heft: 15 (8) Artikelnummer: - Start- / Endseite: 2594 - 2606 Identifikator: ISSN: 1535-9476
CoNE: https://pure.mpg.de/cone/journals/resource/111035577487002