ArticleMolecular and cellular biology2000
Nup2p, a yeast nucleoporin, functions in bidirectional transport of importin alpha.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 87 citations in OpenAlex.
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Mechanisms of NAT10 as ac4C writer in diseases.Molecular therapy. Nucleic acids · 2023Review
- Nup50 plays more than one instrument.Cell cycle (Georgetown, Tex.) · 2022Article
- Article
- The nucleoporin Nup50 activates the Ran guanine nucleotide exchange factor RCC1 to promote NPC assembly at the end of mitosis.The EMBO journal · 2021Article
- A nuclear pore sub-complex restricts the propagation of Ty retrotransposons by limiting their transcription.PLoS genetics · 2021Article
- Dissecting the roles of Cse1 and Nup2 in classical NLS-cargo release in vivo.Traffic (Copenhagen, Denmark) · 2020Article
- Review
- SUMOylation of the nuclear pore complex basket is involved in sensing cellular stresses.Journal of cell science · 2019Article
- Nup2 performs diverse interphase functions in Aspergillus nidulans.Molecular biology of the cell · 2018Article
- The yeast Ty1 retrotransposon requires components of the nuclear pore complex for transcription and genomic integration.Nucleic acids research · 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
- Deciphering the Structure and Function of Nuclear Pores Using Single-Molecule Fluorescence Approaches.Journal of molecular biology · 2016Review
- 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
- 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
- Sumoylation regulates Kap114-mediated nuclear transport.The EMBO journal · 2012Article
- Nucleoporin Nup50 stabilizes closed conformation of armadillo repeat 10 in importin α5.The Journal of biological chemistry · 2012Article
- Ran-dependent nuclear export mediators: a structural perspective.The EMBO journal · 2011Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Import of proteins containing a classical nuclear localization signal (NLS) into the nucleus is mediated by importin alpha and importin beta. Srp1p, the Saccharomyces cerevisiae homologue of importin alpha, returns from the nucleus in a complex with its export factor Cse1p and with Gsp1p (yeast Ran) in its GTP-bound state. We studied the role of the nucleoporin Nup2p in the transport cycle of Srp1p. Cells lacking NUP2 show a specific defect in both NLS import and Srp1p export, indicating that Nup2p is required for efficient bidirectional transport of Srp1p across the nuclear pore complex (NPC). Nup2p is located at the nuclear side of the central gated channel of the NPC and provides a binding site for Srp1p via its amino-terminal domain. We show that Nup2p effectively releases the NLS protein from importin alpha-importin and beta and strongly binds to the importin heterodimer via Srp1p. Kap95p (importin beta) is released from this complex by a direct interaction with Gsp1p-GTP. These data suggest that besides Gsp1p, which disassembles the NLS-importin alpha-importin beta complex upon binding to Kap95p in the nucleus, Nup2p can also dissociate the import complex by binding to Srp1p. We also show data indicating that Nup1p, a relative of Nup2p, plays a similar role in termination of NLS import. Cse1p and Gsp1p-GTP release Srp1p from Nup2p, which suggests that the Srp1p export complex can be formed directly at the NPC. The changed distribution of Cse1p at the NPC in nup2 mutants also supports a role for Nup2p in Srp1p export from the nucleus.
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