ArticleMolecular biology of the cell2005
Interactions between Mad1p and the nuclear transport machinery in the yeast Saccharomyces cerevisiae.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 83 citations in OpenAlex.
- Article
- Ulp1 association with nuclear pore complexes is required for the maintenance of global SUMOylation.Molecular biology of the cell · 2025Article
- Phosphorylation of Mad1 at serine 18 by Mps1 is required for the full virulence of rice blast fungus, Magnaporthe oryzae.Molecular plant pathology · 2024Article
- Fission yeast essential nuclear pore protein Nup211 regulates the expression of genes involved in cytokinesis.PloS one · 2024Article
- An evolutionarily conserved bimodular domain anchors ZC3HC1 and its yeast homologue Pml39p to the nuclear basket.Molecular biology of the cell · 2023Article
- Aurora B phosphorylates Bub1 to promote spindle assembly checkpoint signaling.Current biology : CB · 2022Article
- Spindle assembly checkpoint activation and silencing at kinetochores.Seminars in cell & developmental biology · 2021Review
- Article
- Mapping Proximity Associations of Core Spindle Assembly Checkpoint Proteins.Journal of proteome research · 2021Article
- Multifunctionality of F-rich nucleoporins.Biochemical Society transactions · 2020Review
- Article
- Mps1-mediated release of Mad1 from nuclear pores ensures the fidelity of chromosome segregation.The Journal of cell biology · 2020Article
- CaMad2 Promotes Multiple Aspects of Genome Stability Beyond Its Direct Function in Chromosome Segregation.Genes · 2019Article
- Delineating the contribution of Spc105-bound PP1 to spindle checkpoint silencing and kinetochore microtubule attachment regulation.The Journal of cell biology · 2019Article
- The G2-to-M Transition Is Ensured by a Dual Mechanism that Protects Cyclin B from Degradation by Cdc20-Activated APC/C.Developmental cell · 2019Article
- Effectors of the spindle assembly checkpoint are confined within the nucleus of Saccharomyces cerevisiae.Biology open · 2019Article
- Nup2 performs diverse interphase functions in Aspergillus nidulans.Molecular biology of the cell · 2018Article
- Article
- Regulation of Cenp-F localization to nuclear pores and kinetochores.Cell cycle (Georgetown, Tex.) · 2018Article
- Non-Catalytic Roles of the Topoisomerase IIα C-Terminal Domain.International journal of molecular sciences · 2017Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In addition to its role in nucleocytoplasmic transport, the nuclear pore complex (NPC) acts as a docking site for proteins whose apparent primary cellular functions are unrelated to nuclear transport, including Mad1p and Mad2p, two proteins of the spindle assembly checkpoint (SAC) machinery. To understand this relationship, we have mapped domains of yeast Saccharomyces cerevisiae Mad1p that interact with the nuclear transport machinery, including further defining its interactions with the NPC. We showed that a Kap95p/Kap60p-dependent nuclear localization signal, positioned in the C-terminal third of Mad1p, is required for its efficient targeting to the NPC. At the NPC, Mad1p interacts with Nup53p and a presumed Nup60p/Mlp1p/Mlp2p complex through two coiled coil regions within its N terminus. When the SAC is activated, a portion of Mad1p is recruited to kinetochores through an interaction that is mediated by the C-terminal region of Mad1p and requires energy. We showed using photobleaching analysis that in nocodazole-arrested cells Mad1p rapidly cycles between the Mlp proteins and kinetochores. Our further analysis also showed that only the C terminus of Mad1p is required for SAC function and that the NPC, through Nup53p, may act to regulate the duration of the SAC response.
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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.