ArticlePloS one2013
Dynein and dynactin leverage their bivalent character to form a high-affinity interaction.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 31 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
31 citing papers in PubMed, 45 citations in OpenAlex.
- Exploration of the interaction between dynein intermediate chain and dynactin p150Protein science : a publication of the Protein Society · 2025Article
- Molecular mechanism of dynein-dynactin complex assembly by LIS1.Science (New York, N.Y.) · 2024Article
- Correction: Dynein and Dynactin Leverage Their Bivalent Character to Form a High-Affinity Interaction.PloS one · 2024Article
- Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.Nature communications · 2023Article
- The Role of Inositol Hexakisphosphate Kinase in the Central Nervous System.Biomolecules · 2023Review
- Speech- and language-linked FOXP2 mutation targets protein motors in striatal neurons.Brain : a journal of neurology · 2023Article
- Conserved Roles for the Dynein Intermediate Chain and Ndel1 in Assembly and Activation of Dynein.bioRxiv : the preprint server for biology · 2023Article
- Article
- Nde1 and Ndel1: Outstanding Mysteries in Dynein-Mediated Transport.Frontiers in cell and developmental biology · 2022Review
- Interplay of Disorder and Sequence Specificity in the Formation of Stable Dynein-Dynactin Complexes.Biophysical journal · 2020Article
- Article
- DYNLRB1 is essential for dynein mediated transport and neuronal survival.Neurobiology of disease · 2020Article
- Conformational diversity of dynactin sidearm and domain organization of its subunit p150.Molecular biology of the cell · 2020Article
- The Generation of Dynein Networks by Multi-Layered Regulation and Their Implication in Cell Division.Frontiers in cell and developmental biology · 2020Review
- Inositol hexakisphosphate kinase 3 promotes focal adhesion turnover via interactions with dynein intermediate chain 2.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- The cytoplasmic dynein transport machinery and its many cargoes.Nature reviews. Molecular cell biology · 2018Review
- Nanoparticles engineered to bind cellular motors for efficient delivery.Journal of nanobiotechnology · 2018Article
- A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity.Nature communications · 2018Article
- Article
Corrections and comments
- Erratum issued
Authors and funding
9 authors at 6 institutions in 1 country.
Funding
Abstract
Cytoplasmic dynein and dynactin participate in retrograde transport of organelles, checkpoint signaling and cell division. The principal subunits that mediate this interaction are the dynein intermediate chain (IC) and the dynactin p150(Glued); however, the interface and mechanism that regulates this interaction remains poorly defined. Herein, we use multiple methods to show the N-terminus of mammalian dynein IC, residues 10-44, is sufficient for binding p150(Glued). Consistent with this mapping, monoclonal antibodies that antagonize the dynein-dynactin interaction also bind to this region of the IC. Furthermore, double and triple alanine point mutations spanning residues 6 to 19 in the yeast IC homolog, Pac11, produce significant defects in spindle positioning. Using the same methods we show residues 381 to 530 of p150(Glued) form a minimal fragment that binds to the dynein IC. Sedimentation equilibrium experiments indicate that these individual fragments are predominantly monomeric, but admixtures of the IC and p150(Glued) fragments produce a 2:2 complex. This tetrameric complex is sensitive to salt, temperature and pH, suggesting that the binding is dominated by electrostatic interactions. Finally, circular dichroism (CD) experiments indicate that the N-terminus of the IC is disordered and becomes ordered upon binding p150(Glued). Taken together, the data indicate that the dynein-dynactin interaction proceeds through a disorder-to-order transition, leveraging its bivalent-bivalent character to form a high affinity, but readily reversible interaction.
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What OpenQuestion holds
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.