ArticleCytoskeleton (Hoboken, N.J.)2011
Quantitative analysis of Pac1/LIS1-mediated dynein targeting: Implications for regulation of dynein activity in budding yeast.
Article in Cytoskeleton (Hoboken, N.J.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
41 citing papers in PubMed, 68 citations in OpenAlex.
- Cryptococcus neoformans Slu7 ensures nuclear positioning during mitotic progression through RNA splicing.PLoS genetics · 2024Article
- Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.Nature communications · 2023Article
- Lis1 relieves cytoplasmic dynein-1 autoinhibition by acting as a molecular wedge.Nature structural & molecular biology · 2023Article
- Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport.Nature structural & molecular biology · 2023Article
- Conserved Roles for the Dynein Intermediate Chain and Ndel1 in Assembly and Activation of Dynein.bioRxiv : the preprint server for biology · 2023Article
- The microtubule-associated protein She1 coordinates directional spindle positioning by spatially restricting dynein activity.Journal of cell science · 2021Article
- Modeling a disease-correlated tubulin mutation in budding yeast reveals insight into MAP-mediated dynein function.Molecular biology of the cell · 2021Article
- Article
- Pac1/LIS1 stabilizes an uninhibited conformation of dynein to coordinate its localization and activity.Nature cell biology · 2020Article
- Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020Review
- Molecular basis for dyneinopathies reveals insight into dynein regulation and dysfunction.eLife · 2019Article
- Spatio-temporal regulation of nuclear division by Aurora B kinase Ipl1 in Cryptococcus neoformans.PLoS genetics · 2019Article
- Nuclear movement in fungi.Seminars in cell & developmental biology · 2018Review
- Cortical dynein pulling mechanism is regulated by differentially targeted attachment molecule Num1.eLife · 2018Article
- The TOG protein Stu2/XMAP215 interacts covalently and noncovalently with SUMO.Cytoskeleton (Hoboken, N.J.) · 2018Article
- The role of mitochondria in anchoring dynein to the cell cortex extends beyond clustering the anchor protein.Cell cycle (Georgetown, Tex.) · 2018Article
- Article
- Microtubule cross-linking activity of She1 ensures spindle stability for spindle positioning.The Journal of cell biology · 2017Article
- Dynein is regulated by the stability of its microtubule track.The Journal of cell biology · 2017Article
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
LIS1 is a critical regulator of dynein function during mitosis and organelle transport. Here, we investigated how Pac1, the budding yeast LIS1 homologue, regulates dynein targeting and activity during nuclear migration. We show that Pac1 and Dyn1 (dynein heavy chain) are dependent upon each other and upon Bik1 (budding yeast CLIP-170 homologue) for plus end localization, whereas Bik1 is independent of either. Dyn1, Pac1 and Bik1 interact in vivo at the plus ends, where an excess amount of Bik1 recruits approximately equal amounts of Pac1 and Dyn1. Overexpression of Pac1 enhanced plus end targeting of Dyn1 and vice versa, while affinity-purification of Dyn1 revealed that it exists in a complex with Pac1 in the absence of Bik1, leading us to conclude that the Pac1-Dyn1 complex preassembles in the cytoplasm prior to loading onto Bik1-decorated plus ends. Strikingly, we found that Pac1-overexpression augments cortical dynein activity through a mechanism distinct from loss of She1, a negative regulator of dynein-dynactin association. While Pac1-overexpression enhances the frequency of cortical targeting for dynein and dynactin, the stoichiometry of these complexes remains relatively unchanged at the plus ends compared to that in wild-type cells (∼3 dynein to 1 dynactin). Loss of She1, however, enhances dynein-dynactin association at the plus ends and the cell cortex, resulting in an apparent 1:1 stoichiometry. Our results reveal differential regulation of cortical dynein activity by She1 and Pac1, and provide a potentially new regulatory step in the off-loading model for dynein function.
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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.