ArticleCytoskeleton (Hoboken, N.J.)2012
A mouse neurodegenerative dynein heavy chain mutation alters dynein motility and localization in Neurospora crassa.
Article in Cytoskeleton (Hoboken, N.J.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- A force-sensitive mutation reveals a non-canonical role for dynein in anaphase progression.The Journal of cell biology · 2024Article
- The structure of prevacuolar compartments in Neurospora crassa as observed with super-resolution microscopy.PloS one · 2023Article
- A mathematical understanding of how cytoplasmic dynein walks on microtubules.Royal Society open science · 2018Article
- DYNC1H1 mutations associated with neurological diseases compromise processivity of dynein-dynactin-cargo adaptor complexes.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Characterization of a Novel Prevacuolar Compartment in Neurospora crassa.Eukaryotic cell · 2015Article
- Cytoplasmic dynein and early endosome transport.Cellular and molecular life sciences : CMLS · 2015Review
- Cytoplasmic dynein heavy chain: the servant of many masters.Trends in neurosciences · 2013Review
- The yeast dynein Dyn2-Pac11 complex is a dynein dimerization/processivity factor: structural and single-molecule characterization.Molecular biology of the cell · 2013Article
- Identification of a novel site in the tail of dynein heavy chain important for dynein function in vivo.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Cytoplasmic dynein is responsible for the transport and delivery of cargoes in organisms ranging from humans to fungi. Dysfunction of dynein motor machinery due to mutations in dynein or its activating complex dynactin can result in one of several neurological diseases in mammals. The mouse Legs at odd angles (Loa) mutation in the tail domain of the dynein heavy chain has been shown to lead to progressive neurodegeneration in mice. The mechanism by which the Loa mutation affects dynein function is just beginning to be understood. In this work, we generated the dynein tail mutation observed in Loa mice into the Neurospora crassa genome and utilized cell biological and complementing biochemical approaches to characterize how that tail mutation affected dynein function. We determined that the Loa mutation exhibits several subtle defects upon dynein function in N. crassa that were not seen in mice, including alterations in dynein localization, impaired velocity of vesicle transport, and in the biochemical properties of purified motors. Our work provides new information on the role of the tail domain on dynein function and points out areas of future research that will be of interest to pursue in mammalian systems.
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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.