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A toolkit to study nuclear transport pathways: nanobody-mediated inhibition of importin β-related nuclear transport receptors (NTRs)

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A toolkit to study nuclear transport pathways: nanobody-mediated inhibition of importin β-related nuclear transport receptors (NTRs) (English shop)

Dilantha Perera (Author)


Extract, PDF (3.9 MB)
Table of Contents, PDF (73 KB)

ISBN-13 (Hard Copy) 9783736978478
ISBN-13 (eBook) 9783736968479
Language English
Page Number 136
Lamination of Cover glossy
Edition 1.
Publication Place Göttingen
Place of Dissertation Universität Göttingen
Publication Date 2023-08-07
General Categorization Dissertation
Departments Biochemistry, molecular biology, gene technology
Keywords eukaryotic cells, nucleus, compartmentalization, nucleocytoplasmic transport, importin, shuttling, nuclear transport receptors (NTRs), nuclear pore complex (NPC), importins, exportins, biportins, export complex, transport pathways, anti-NTR nanobodies, Transportin 1 (TRN1), Exportin 4 (Xpo4), Exportin 7 (Xpo7), CAS, nanobody fusions, impede nuclear pore passage, transport cycle, inhibitor, inhibition, NTR/cargo complexes, FG phase, NTR-meidated transport, permeabilized cells, Ran binding, transport block, nanobodies (Nbs), nucleoporins (Nups), tag-Nbs, NTR blockers, eukaryotische Zellen, Zellkern, Kompartimentierung, nukleozytoplasmatischer Transport, Kerntransportrezeptoren (NTRs), Kernporenkomplex (NPC), Nanokörperfusionen, NTR-vermeideter Transport, permeabilisierte Zellen, NTR-Blocker
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Eukaryotic cells are divided into a nuclear and a cytoplasmic compartment. This separates transcription from translation and makes gene expression dependent on nucleocytoplasmic transport. The members of the importin β superfamily function as shuttling nuclear transport receptors (NTRs) that recognize and actively transport cargoes through nuclear pores. An estimated 5 000 to 10 000 different human proteins are subject to active nuclear transport. Numerous cargo/NTR pairs have been identified, however, we are still far from a complete understanding as it has been very challenging to setup a systematic in vivo analysis that integrates the impact of all transport pathways.

In this study, we obtained anti-NTR nanobodies against TRN1, Xpo4, Xpo7, and CAS. Our aim was to identify nanobodies, and prepare nanobody fusions, that impede nuclear pore-passage of the targeted NTR and thus, interrupt a given transport cycle. These nanobody fusions were observed to inhibit the partition of NTR/cargo complexes into a reconstituted FG phase. We also observed that the nanobodies and nanobody fusions inhibit NTR transport in permeabilized cells.