ArticleJournal of cell science2020
Overexpression of Mdm36 reveals Num1 foci that mediate dynein-dependent microtubule sliding in budding yeast.
Article in Journal of cell science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed, 10 citations in OpenAlex.
- Mitochondrial anchor protein Num11 is key to pathogenicity ofVirulence · 2025Article
- Mitochondria-plasma membrane contact sites regulate the ER-mitochondria encounter structure.Journal of cell science · 2025Article
- Mitochondria-ER-PM contacts regulate mitochondrial division and PI(4)P distribution.The Journal of cell biology · 2024Article
- Loss of Num1-mediated cortical dynein anchoring negatively impacts respiratory growth.Journal of cell science · 2022Article
- Hierarchical integration of mitochondrial and nuclear positioning pathways by the Num1 EF hand.Molecular biology of the cell · 2022Article
- Mitochondria-Plasma Membrane Contact Sites: Emerging Regulators of Mitochondrial Form and Function.Contact (Thousand Oaks (Ventura County, Calif.))Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The current model for spindle positioning requires attachment of the microtubule (MT) motor cytoplasmic dynein to the cell cortex, where it generates pulling force on astral MTs to effect spindle displacement. How dynein is anchored by cortical attachment machinery to generate large spindle-pulling forces remains unclear. Here, we show that cortical clustering of Num1, the yeast dynein attachment molecule, is limited by its assembly factor Mdm36. Overexpression of Mdm36 results in an overall enhancement of Num1 clustering but reveals a population of dim Num1 clusters that mediate dynein anchoring at the cell cortex. Direct imaging shows that bud-localized, dim Num1 clusters containing around only six Num1 molecules mediate dynein-dependent spindle pulling via a lateral MT sliding mechanism. Mutations affecting Num1 clustering interfere with mitochondrial tethering but do not interfere with the dynein-based spindle-pulling function of Num1. We propose that formation of small ensembles of attachment molecules is sufficient for dynein anchorage and cortical generation of large spindle-pulling forces.This article has an associated First Person interview with the first author of the paper.
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Registered trials
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