ArticleThe EMBO journal2003
Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
46 citing papers in PubMed, 97 citations in OpenAlex.
- The importin-alpha superfamily engages in ethylene signaling by shuttling ETHYLENE INSENSITIVE 2 from the endoplasmic reticulum to the nucleus.The FEBS journal · 2026Article
- Yeast 26S proteasome nuclear import is coupled to nucleus-specific degradation of the karyopherin adaptor protein Sts1.Scientific reports · 2024Article
- Article
- Nup50 plays more than one instrument.Cell cycle (Georgetown, Tex.) · 2022Article
- Dissecting the roles of Cse1 and Nup2 in classical NLS-cargo release in vivo.Traffic (Copenhagen, Denmark) · 2020Article
- Comparative study of the interactions between fungal transcription factor nuclear localization sequences with mammalian and fungal importin-alpha.Scientific reports · 2020Article
- The Structure of the Nuclear Pore Complex (An Update).Annual review of biochemistry · 2019Review
- Nup2 performs diverse interphase functions in Aspergillus nidulans.Molecular biology of the cell · 2018Article
- Mitotic nuclear pore complex segregation involves Nup2 inThe Journal of cell biology · 2017Article
- The Nucleoporin Nup2 Contains a Meiotic-Autonomous Region that Promotes the Dynamic Chromosome Events of Meiosis.Genetics · 2017Article
- The nuclear pore complex: understanding its function through structural insight.Nature reviews. Molecular cell biology · 2017Review
- Deciphering the Structure and Function of Nuclear Pores Using Single-Molecule Fluorescence Approaches.Journal of molecular biology · 2016Review
- Structure of importin-α bound to a non-classical nuclear localization signal of the influenza A virus nucleoprotein.Scientific reports · 2015Article
- Distinctive Properties of the Nuclear Localization Signals of Inner Nuclear Membrane Proteins Heh1 and Heh2.Structure (London, England : 1993) · 2015Article
- Nup2 requires a highly divergent partner, NupA, to fulfill functions at nuclear pore complexes and the mitotic chromatin region.Molecular biology of the cell · 2015Article
- Nucleoporin FG domains facilitate mRNP remodeling at the cytoplasmic face of the nuclear pore complex.Genetics · 2014Article
- Design rules for selective binding of nuclear localization signals to minor site of importin α.PloS one · 2014Article
- New twist to nuclear import: When two travel together.Communicative & integrative biology · 2013Article
- Choreography of importin-α/CAS complex assembly and disassembly at nuclear pores.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Crystal structure of rice importin-α and structural basis of its interaction with plant-specific nuclear localization signals.The Plant cell · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The yeast nucleoporin Nup2p is associated primarily with the nuclear basket of nuclear pore complexes and is required for efficient importin-alpha:beta-mediated nuclear protein import as well as efficient nuclear export of Kap60p/importin-alpha. Residues 1-51 of Nup2p bind tightly to Kap60p and are required for Nup2p function in vivo. We have determined the 2.6 A resolution crystal structure of a complex between this region of Nup2p and the armadillo repeat domain of Kap60p. Nup2p binds along the inner concave groove of Kap60p, but its interaction interface is different from that employed for nuclear localization signal (NLS) recognition although there is some overlap between them. Nup2p binds Kap60p more strongly than NLSs and accelerates release of NLSs from Kap60p. Nup2p itself is released from Kap60p by Cse1p:RanGTP only in the presence of the importin-beta binding (IBB) domain of Kap60p. These data indicate that Nup2p increases the overall rate of nuclear trafficking by coordinating nuclear import termination and importin recycling as a concerted process.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.