ArticleGenetics2012
Analyses of dynein heavy chain mutations reveal complex interactions between dynein motor domains and cellular dynein functions.
Article in Genetics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- The structure of prevacuolar compartments in Neurospora crassa as observed with super-resolution microscopy.PloS one · 2023Article
- Dynein activation in vivo is regulated by the nucleotide states of its AAA3 domain.Current biology : CB · 2021Article
- Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020Review
- Molecular mechanism of cytoplasmic dynein tension sensing.Nature communications · 2019Article
- Nuclear movement in fungi.Seminars in cell & developmental biology · 2018Review
- A novel mouse model carrying a human cytoplasmic dynein mutation shows motor behavior deficits consistent with Charcot-Marie-Tooth type 2O disease.Scientific reports · 2018Article
- Cytoplasmic dynein and early endosome transport.Cellular and molecular life sciences : CMLS · 2015Review
- Mutation screen reveals novel variants and expands the phenotypes associated with DYNC1H1.Journal of neurology · 2015Article
- A microscopy-based screen employing multiplex genome sequencing identifies cargo-specific requirements for dynein velocity.Molecular biology of the cell · 2014Article
- New mutations in flagellar motors identified by whole genome sequencing in Chlamydomonas.Cilia · 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
- A mouse neurodegenerative dynein heavy chain mutation alters dynein motility and localization in Neurospora crassa.Cytoskeleton (Hoboken, N.J.) · 2012Article
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Authors and funding
6 authors.
Funding
Abstract
Cytoplasmic dynein transports cargoes for a variety of crucial cellular functions. However, since dynein is essential in most eukaryotic organisms, the in-depth study of the cellular function of dynein via genetic analysis of dynein mutations has not been practical. Here, we identify and characterize 34 different dynein heavy chain mutations using a genetic screen of the ascomycete fungus Neurospora crassa, in which dynein is nonessential. Interestingly, our studies show that these mutations segregate into five different classes based on the in vivo localization of the mutated dynein motors. Furthermore, we have determined that the different classes of dynein mutations alter vesicle trafficking, microtubule organization, and nuclear distribution in distinct ways and require dynactin to different extents. In addition, biochemical analyses of dynein from one mutant strain show a strong correlation between its in vitro biochemical properties and the aberrant intracellular function of that altered dynein. When the mutations were mapped to the published dynein crystal structure, we found that the three-dimensional structural locations of the heavy chain mutations were linked to particular classes of altered dynein functions observed in cells. Together, our data indicate that the five classes of dynein mutations represent the entrapment of dynein at five separate points in the dynein mechanochemical and transport cycles. We have developed N. crassa as a model system where we can dissect the complexities of dynein structure, function, and interaction with other proteins with genetic, biochemical, and cell biological studies.
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