ArticleNature communications2019
Regulation of in vivo dynein force production by CDK5 and 14-3-3ε and KIAA0528.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- 14-3-3θ phosphorylation at S232 reduces its interactome and regulates axonal trafficking.Disease models & mechanisms · 2025Article
- A novel 14-3-3θ phosphomimetic mouse model demonstrates social dominance defects.Biology open · 2025Article
- MARK2 phosphorylates KIF13A at a 14-3-3 binding site to polarize vesicular transport of transferrin receptor within dendrites.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The meiotic LINC complex component KASH5 is an activating adaptor for cytoplasmic dynein.The Journal of cell biology · 2023Article
- Review
- ccd-5, a novel cdk-5 binding partner, regulates pioneer axon guidance in the ventral nerve cord of Caenorhabditis elegans.Genetics · 2022Article
- Decreased anterograde transport coupled with sustained retrograde transport contributes to reduced axonal mitochondrial density in tauopathy neurons.Frontiers in molecular neuroscience · 2022Article
- LIS1 and NDEL1 Regulate Axonal Trafficking of Mitochondria in Mature Neurons.Frontiers in molecular neuroscience · 2022Article
- Cdk5 and GSK3β inhibit fast endophilin-mediated endocytosis.Nature communications · 2021Article
- Pac1/LIS1 stabilizes an uninhibited conformation of dynein to coordinate its localization and activity.Nature cell biology · 2020Article
- Lipid droplet motility and organelle contacts.Contact (Thousand Oaks (Ventura County, Calif.))Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Single-molecule cytoplasmic dynein function is well understood, but there are major gaps in mechanistic understanding of cellular dynein regulation. We reported a mode of dynein regulation, force adaptation, where lipid droplets adapt to opposition to motion by increasing the duration and magnitude of force production, and found LIS1 and NudEL to be essential. Adaptation reflects increasing NudEL-LIS1 utilization; here, we hypothesize that such increasing utilization reflects CDK5-mediated NudEL phosphorylation, which increases the dynein-NudEL interaction, and makes force adaptation possible. We report that CDK5, 14-3-3ε, and CDK5 cofactor KIAA0528 together promote NudEL phosphorylation and are essential for force adaptation. By studying the process in COS-1 cells lacking Tau, we avoid confounding neuronal effects of CDK5 on microtubules. Finally, we extend this in vivo regulatory pathway to lysosomes and mitochondria. Ultimately, we show that dynein force adaptation can control the severity of lysosomal tug-of-wars among other intracellular transport functions involving high force.
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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.