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Depletion of a Microtubule-Associated Motor Protein Induces the Loss of Dendritic Identity
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Dendrites are short stout tapering processes that are rich in ribosomes and Golgi elements, whereas axons are long thin processes of uniform diameter that are deficient in these organelles. It has been hypothesized that the unique morphological and compositional features of axons and dendrites result from their distinct patterns of microtubule polarity orientation. The microtubules within axons are uniformly oriented with their plus ends distal to the cell body, whereas microtubules within dendrites are nonuniformly oriented. The minus-end-distal microtubules are thought to arise via their specific transport into dendrites by the motor protein known as CHO1/MKLP1. According to this model, CHO1/MKLP1 transports microtubules with their minus ends leading into dendrites by generating forces against the plus-end-distal microtubules, thus creating drag on the plus-end-distal microtubules. Here we show that depletion of CHO1/MKLP1 from cultured neurons causes a rapid redistribution of microtubules within dendrites such that minus-end-distal microtubules are chased back to the cell body while plus-end-distal microtubules are redistributed forward. The dendrite grows significantly longer and thinner, loses its taper, and acquires a progressively more axon-like organelle composition. These results suggest that the forces generated by CHO1/MKLP1 are necessary for maintaining the minus-end-distal microtubules in the dendrite, for antagonizing the anterograde transport of the plus-end-distal microtubules, and for sustaining a pattern of microtubule organization necessary for the maintenance of dendritic morphology and composition. Thus, we would conclude that dendritic identity is dependent on forces generated by CHO1/MKLP1.
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Yu et al. reported that MAP2 staining in dendrites becomes indistinguishable from the axon when dendrites lose minus-end-out MTs.
“Consistent with this model, Yu et al. reported that MAP2 staining in dendrites becomes indistinguishable from the axon when dendrites lose minus-end-out MTs (33).”
From Active transport by cytoplasmic dynein sustains dendritic MAP2 localization in developing neurons (2026) · cites this paper as [33]
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Metadata
- Authors
- Yu, W., Cook, C., Sauter, C., Kuriyama, R., Kaplan, P. L., & Baas, P. W.
- Affiliations
- University of Wisconsin–Madison (US)
- University of Minnesota (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2000-08-01
- Volume
- 20
- Issue
- 15
- Pages
- 5782-5791
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6772545
- OpenAlex
- W1583142746
- Cited by
- 116
- References
- 23
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 1 · 2023: 3 · 2022: 6 · 2021: 4 · 2020: 6 · 2019: 3 · 2018: 1 · 2017: 6 · 2016: 4 · 2015: 4 · 2014: 4 · 2013: 2 · 2012: 9
- FWCI
- 2.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- dendritic morphology, microtubule polarity, microtubule transport, microtubule motor proteins, dendritic microtubules, ribosome distribution, anterograde transport
- MeSH terms
- Animals, Axons, Cells, Cultured, Dendrites, Fluorescent Dyes, Isoquinolines, Microscopy, Electron, Microtubule-Associated Proteins, Microtubules, Neurons, Oligonucleotides, Antisense, Neurofilament Proteins, Superior Cervical Ganglion, Molecular Motor Proteins, Cell Size, Rats
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