ArticleMolecular biology of the cell2013
The yeast dynein Dyn2-Pac11 complex is a dynein dimerization/processivity factor: structural and single-molecule characterization.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 28 citations in OpenAlex.
- Review
- Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.Nature communications · 2023Article
- Conserved Roles for the Dynein Intermediate Chain and Ndel1 in Assembly and Activation of Dynein.bioRxiv : the preprint server for biology · 2023Article
- Single-Molecule Studies on the Motion and Force Generation of the Kinesin-3 Motor KIF1A.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The regulatory function of the AAA4 ATPase domain of cytoplasmic dynein.Nature communications · 2020Article
- LIS1 regulates cargo-adapter-mediated activation of dynein by overcoming its autoinhibition in vivo.The Journal of cell biology · 2019Article
- Molecular mechanism of cytoplasmic dynein tension sensing.Nature communications · 2019Article
- Structural atlas of dynein motors at atomic resolution.Biophysical reviews · 2018Review
- A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity.Nature communications · 2018Article
- Combining Structure-Function and Single-Molecule Studies on Cytoplasmic Dynein.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis.The Journal of cell biology · 2017Article
- The Anchored Flexibility Model in LC8 Motif Recognition: Insights from the Chica Complex.Biochemistry · 2016Article
- Interactions of Yeast Dynein with Dynein Light Chain and Dynactin: GENERAL IMPLICATIONS FOR INTRINSICALLY DISORDERED DUPLEX SCAFFOLDS IN MULTIPROTEIN ASSEMBLIES.The Journal of biological chemistry · 2015Article
- Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds.FEBS letters · 2015Review
- Cytoplasmic dynein and early endosome transport.Cellular and molecular life sciences : CMLS · 2015Review
- Control of cytoplasmic dynein force production and processivity by its C-terminal domain.Nature communications · 2015Article
- Autoregulatory mechanism for dynactin control of processive and diffusive dynein transport.Nature cell biology · 2014Article
- The mechanism of dynein light chain LC8-mediated oligomerization of the Ana2 centriole duplication factor.The Journal of biological chemistry · 2014Article
- Preliminary crystallographic studies of a Schistosoma mansoni antigen (Sm21.7) dynein light-chain (DLC) domain.Acta crystallographica. Section F, Structural biology communications · 2014Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Cytoplasmic dynein is the major microtubule minus end-directed motor. Although studies have probed the mechanism of the C-terminal motor domain, if and how dynein's N-terminal tail and the accessory chains it binds regulate motor activity remain to be determined. Here, we investigate the structure and function of the Saccharomyces cerevisiae dynein light (Dyn2) and intermediate (Pac11) chains in dynein heavy chain (Dyn1) movement. We present the crystal structure of a Dyn2-Pac11 complex, showing Dyn2-mediated Pac11 dimerization. To determine the molecular effects of Dyn2 and Pac11 on Dyn1 function, we generated dyn2Δ and dyn2Δpac11Δ strains and analyzed Dyn1 single-molecule motor activity. We find that the Dyn2-Pac11 complex promotes Dyn1 homodimerization and potentiates processivity. The absence of Dyn2 and Pac11 yields motors with decreased velocity, dramatically reduced processivity, increased monomerization, aggregation, and immobility as determined by single-molecule measurements. Deleting dyn2 significantly reduces Pac11-Dyn1 complex formation, yielding Dyn1 motors with activity similar to Dyn1 from the dyn2Δpac11Δ strain. Of interest, motor phenotypes resulting from Dyn2-Pac11 complex depletion bear similarity to a point mutation in the mammalian dynein N-terminal tail (Loa), highlighting this region as a conserved, regulatory motor element.
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