ArticleMolecular biology of the cell2012
Dynactin's pointed-end complex is a cargo-targeting module.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 81 citations in OpenAlex.
- Phosphorylation in the dynein light intermediate chain 2 isoform enables Pin1 binding and modulates cargo-adaptor interactions.Journal of structural biology: X · 2026Article
- The Chlamydia effector Dre1 binds dynactin to reposition host organelles during infection.Cell reports · 2025Article
- The landscape of non-reference SINE-VNTR-Alus in amyotrophic lateral sclerosis.Experimental biology and medicine (Maywood, N.J.) · 2025Article
- VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.Cell reports · 2024Article
- Autophagy initiation triggers p150Cellular and molecular life sciences : CMLS · 2024Article
- VezA/vezatin facilitates proper assembly of the dynactin complex in vivo.bioRxiv : the preprint server for biology · 2024Article
- Kinesin-1 autoinhibition facilitates the initiation of dynein cargo transport.The Journal of cell biology · 2023Article
- Conformational transitions of the Spindly adaptor underlie its interaction with Dynein and Dynactin.The Journal of cell biology · 2022Article
- Dynactin 6 deficiency enhances aging-associated dystrophic neurite formation in mouse brains.Neurobiology of aging · 2021Article
- N4BP2L1 interacts with dynactin and contributes to GLUT4 trafficking and glucose uptake in adipocytes.Journal of diabetes investigation · 2021Article
- Dynein activation in vivo is regulated by the nucleotide states of its AAA3 domain.Current biology : CB · 2021Article
- Cryo-EM reveals the complex architecture of dynactin's shoulder region and pointed end.The EMBO journal · 2021Article
- Assembly and Activity of the WASH Molecular Machine: Distinctive Features at the Crossroads of the Actin and Microtubule Cytoskeletons.Frontiers in cell and developmental biology · 2021Review
- The Arp1/11 minifilament of dynactin primes the endosomal Arp2/3 complex.Science advances · 2021Article
- Conformational diversity of dynactin sidearm and domain organization of its subunit p150.Molecular biology of the cell · 2020Article
- Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020Review
- Structural Glycoprotein E2 of Classical Swine Fever Virus Interacts with Host Protein Dynactin Subunit 6 (DCTN6) during the Virus Infectious Cycle.Journal of virology · 2019Article
- LIS1 regulates cargo-adapter-mediated activation of dynein by overcoming its autoinhibition in vivo.The Journal of cell biology · 2019Article
- Dynein activators and adaptors at a glance.Journal of cell science · 2019Review
- Dynein activator Hook1 is required for trafficking of BDNF-signaling endosomes in neurons.The Journal of cell biology · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Dynactin is an essential part of the cytoplasmic dynein motor that enhances motor processivity and serves as an adaptor that allows dynein to bind cargoes. Much is known about dynactin's interaction with dynein and microtubules, but how it associates with its diverse complement of subcellular binding partners remains mysterious. It has been suggested that cargo specification involves a group of subunits referred to as the "pointed-end complex." We used chemical cross-linking, RNA interference, and protein overexpression to characterize interactions within the pointed-end complex and explore how it contributes to dynactin's interactions with endomembranes. The Arp11 subunit, which caps one end of dynactin's Arp1 filament, and p62, which binds Arp11 and Arp1, are necessary for dynactin stability. These subunits also allow dynactin to bind the nuclear envelope prior to mitosis. p27 and p25, by contrast, are peripheral components that can be removed without any obvious impact on dynactin integrity. Dynactin lacking these subunits shows reduced membrane binding. Depletion of p27 and p25 results in impaired early and recycling endosome movement, but late endosome movement is unaffected, and mitotic spindles appear normal. We conclude that the pointed-end complex is a bipartite structural domain that stabilizes dynactin and supports its binding to different subcellular structures.
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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.