ArticleNature communications2020
A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Nanobody-based analysis of RhoGTPase stress response inBiotechnology reports (Amsterdam, Netherlands) · 2026Article
- A tool to pulse-label yeast nuclear pore complexes in imaging and biochemical experiments.eLife · 2026Article
- Docking a flexible basket onto the core of the nuclear pore complex.Nature cell biology · 2024Article
- A checkpoint function for Nup98 in nuclear pore formation suggested by novel inhibitory nanobodies.The EMBO journal · 2024Article
- Structural Classification of CDR-H3 in Single-Domain VMethods in molecular biology (Clifton, N.J.) · 2023Article
- Quantitative analysis of nuclear pore complex organization inLife science alliance · 2022Article
- Highly potent multivalent VHH antibodies against Chikungunya isolated from an alpaca naïve phage display library.Journal of nanobiotechnology · 2022Article
- Cryo-EM structure of the nuclear ring from Xenopus laevis nuclear pore complex.Cell research · 2022Article
- VInternational journal of molecular sciences · 2022Review
- Multivariate mining of an alpaca immune repertoire identifies potent cross-neutralizing SARS-CoV-2 nanobodies.Science advances · 2022Article
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Authors and funding
6 authors.
Funding
Abstract
Nuclear pore complexes (NPCs) are the main conduits for molecular exchange across the nuclear envelope. The NPC is a modular assembly of ~500 individual proteins, called nucleoporins or nups. Most scaffolding nups are organized in two multimeric subcomplexes, the Nup84 or Y complex and the Nic96 or inner ring complex. Working in S. cerevisiae, and to study the assembly of these two essential subcomplexes, we here develop a set of twelve nanobodies that recognize seven constituent nucleoporins of the Y and Nic96 complexes. These nanobodies all bind specifically and with high affinity. We present structures of several nup-nanobody complexes, revealing their binding sites. Additionally, constitutive expression of the nanobody suite in S. cerevisiae detect accessible and obstructed surfaces of the Y complex and Nic96 within the NPC. Overall, this suite of nanobodies provides a unique and versatile toolkit for the study of the NPC.
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