ArticleThe Journal of biological chemistry2016
Hook Adaptors Induce Unidirectional Processive Motility by Enhancing the Dynein-Dynactin Interaction.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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Who cites it
72 citing papers in PubMed, 122 citations in OpenAlex.
- The roles of cytoplasmic dynein complex in various ocular disorders.Molecular medicine (Cambridge, Mass.) · 2026Review
- The Long Haul: Microtubule Motors as the Essential Supply Line for Neuronal Longevity.Journal of neurochemistry · 2026Review
- HOOK2 downregulation compromises the tumorigenic and stemness properties of ovarian cancer cells by increasing endoplasmic reticulum stress.Cell death & disease · 2026Article
- Adaptor-mediated recruitment of three dyneins to dynactin enhances force generation.Nature cell biology · 2026Article
- The intracellular bacterium Orientia tsutsugamushi uses the autotransporter ScaC to activate BICD adaptors for dynein-based motility.Nature communications · 2025Article
- HIV-1 binds dynein directly to hijack microtubule transport machinery.Science advances · 2025Article
- CCSer2 gates dynein activity at the cell periphery.The Journal of cell biology · 2025Article
- Fat traffic control: S-acylation in axonal transport.Molecular pharmacology · 2025Review
- Fibroblast IRF7-mediated chondrocyte apoptosis affects the progression of collapse in steroid-induced osteonecrosis of the femoral head.Journal of orthopaedic surgery and research · 2025Article
- The Progress in Exploratory Studies of Peripheral Blood Single Nucleated Cells as Seed Cells in Peripheral Nerve Repair.Neural plasticity · 2025Review
- Presynaptic perspective: Axonal transport defects in neurodevelopmental disorders.The Journal of cell biology · 2024Review
- The BICD2 dynein cargo adaptor binds to the HPV16 L2 capsid protein and promotes HPV infection.PLoS pathogens · 2024Article
- Protein homeostasis maintained by HOOK1 levels promotes the tumorigenic and stemness properties of ovarian cancer cells through reticulum stress and autophagy.Journal of experimental & clinical cancer research : CR · 2024Article
- Cargo specificity, regulation, and therapeutic potential of cytoplasmic dynein.Experimental & molecular medicine · 2024Review
- Axonal transport of autophagosomes is regulated by dynein activators JIP3/JIP4 and ARF/RAB GTPases.The Journal of cell biology · 2023Article
- Article
- BICD2 phosphorylation regulates dynein function and centrosome separation in G2 and M.Nature communications · 2023Article
- Axonal transport of autophagosomes is regulated by dynein activators JIP3/JIP4 and ARF/RAB GTPases.bioRxiv : the preprint server for biology · 2023Article
- Article
- Conformational transitions of the Spindly adaptor underlie its interaction with Dynein and Dynactin.The Journal of cell biology · 2022Article
12 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Cytoplasmic dynein drives the majority of minus end-directed vesicular and organelle motility in the cell. However, it remains unclear how dynein is spatially and temporally regulated given the variety of cargo that must be properly localized to maintain cellular function. Recent work has suggested that adaptor proteins provide a mechanism for cargo-specific regulation of motors. Of particular interest, studies in fungal systems have implicated Hook proteins in the regulation of microtubule motors. Here we investigate the role of mammalian Hook proteins, Hook1 and Hook3, as potential motor adaptors. We used optogenetic approaches to specifically recruit Hook proteins to organelles and observed rapid transport of peroxisomes to the perinuclear region of the cell. This rapid and efficient translocation of peroxisomes to microtubule minus ends indicates that mammalian Hook proteins activate dynein rather than kinesin motors. Biochemical studies indicate that Hook proteins interact with both dynein and dynactin, stabilizing the formation of a supramolecular complex. Complex formation requires the N-terminal domain of Hook proteins, which resembles the calponin-homology domain of end-binding (EB) proteins but cannot bind directly to microtubules. Single-molecule motility assays using total internal reflection fluorescence microscopy indicate that both Hook1 and Hook3 effectively activate cytoplasmic dynein, inducing longer run lengths and higher velocities than the previously characterized dynein activator bicaudal D2 (BICD2). Together, these results suggest that dynein adaptors can differentially regulate dynein to allow for organelle-specific tuning of the motor for precise intracellular trafficking.
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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.