ArticleNature communications2017
She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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.
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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- The mechanochemical cycle of reactive full-length human dynein 1.Nature structural & molecular biology · 2025Article
- Application of temperature replica exchange molecular dynamics: Structure of mitotic spindle-associated protein SHE1 and its binding to dynein.Computational and structural biotechnology journal · 2025Article
- MAP9/MAPH-9 supports axonemal microtubule doublets and modulates motor movement.Developmental cell · 2024Article
- Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.Nature communications · 2023Article
- Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport.Nature structural & molecular biology · 2023Article
- Zn2+ decoration of microtubules arrests axonal transport and displaces tau, doublecortin, and MAP2C.The Journal of cell 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
- Analysis of the Structural Mechanism of ATP Inhibition at the AAA1 Subunit of Cytoplasmic Dynein-1 Using a Chemical "Toolkit".International journal of molecular sciences · 2021Article
- The Hec1/Ndc80 tail domain is required for force generation at kinetochores, but is dispensable for kinetochore-microtubule attachment formation and Ska complex recruitment.Molecular biology of the cell · 2020Article
- Pac1/LIS1 stabilizes an uninhibited conformation of dynein to coordinate its localization and activity.Nature cell biology · 2020Article
- A Combinatorial MAP Code Dictates Polarized Microtubule Transport.Developmental cell · 2020Article
- Help or hindrance: how do microtubule-based forces contribute to genome damage and repair?Current genetics · 2020Review
- IGF1R regulates retrograde axonal transport of signalling endosomes in motor neurons.EMBO reports · 2020Article
- Molecular basis for dyneinopathies reveals insight into dynein regulation and dysfunction.eLife · 2019Article
- Astral microtubule forces alter nuclear organization and inhibit DNA repair in budding yeast.Molecular biology of the cell · 2019Article
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Cytoplasmic dynein is an enormous minus end-directed microtubule motor. Rather than existing as bare tracks, microtubules are bound by numerous microtubule-associated proteins (MAPs) that have the capacity to affect various cellular functions, including motor-mediated transport. One such MAP is She1, a dynein effector that polarizes dynein-mediated spindle movements in budding yeast. Here, we characterize the molecular basis by which She1 affects dynein, providing the first such insight into which a MAP can modulate motor motility. We find that She1 affects the ATPase rate, microtubule-binding affinity, and stepping behavior of dynein, and that microtubule binding by She1 is required for its effects on dynein motility. Moreover, we find that She1 directly contacts the microtubule-binding domain of dynein, and that their interaction is sensitive to the nucleotide-bound state of the motor. Our data support a model in which simultaneous interactions between the microtubule and dynein enables She1 to directly affect dynein motility.
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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.