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Cited by 144Alzheimer's disease research and treatmentsMicrotubule and mitosis dynamicsNeuroscience and Neuropharmacology Research

Sorting mechanisms of Tau and MAP2 in neurons: Suppressed axonal transit of MAP2 and locally regulated microtubule binding

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Kanai, Yoshimitsu, Hirokawa, Nobutaka·1995·Neuron
DOI 10.1016/0896-6273(95)90298-8
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Abstract

Tau is abundant in the axon, whereas MAP2 is found in the cell body and dendrites. To understand their differential localization, we performed transfection studies on primary cultured neurons using tagged tau, MAP2, MAP2C, and their chimeric/deletion mutants. We found that MAP2 was prevented from entering the axon by its N-terminal projection domain and that microtubule binding of tau was stronger in the axon than in the cell body and dendrites, whereas that of MAP2/MAP2C was tighter in the cell body and dendrites than in the axon. These binding properties were determined by their microtubule-binding domains and were suggested to be regulated by phosphorylation, at least in the case of tau. Thus, the suppressed axonal transit of MAP2 and locally regulated microtubule binding may play important roles for their sorting in neurons.

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68 of 68 references verified0 citation errors · 0 not checkable

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  • Kanai et al. reported that the projection domain (PD) of MAP2 prevents MAP2 from entering the axon, resulting in somatodendritic localization of HMW MAP2.

    “Kanai et al. (6) also reported that the projection domain (PD) of MAP2, which exists only in MAP2A and B, prevents MAP2 from entering the axon, resulting in the somatodendritic localization of HMW MAP2”

    From Active transport by cytoplasmic dynein sustains dendritic MAP2 localization in developing neurons (2026) · cites this paper as [6]

  • Tau is highly expressed in neurons in the mammalian brain and normally localizes predominantly to axons as an important regulator of axonal transport.

    “Tau is highly expressed in neurons in the mammalian brain, and normally localizes predominantly to axons as an important regulator of axonal transport [124–126].”

    From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [125]

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Authors
Kanai, Y., & Hirokawa, N.
Affiliations
The University of Tokyo (JP)
ORCID
Venue
Neuron
Publisher
Elsevier BV
Published
1995-02
Volume
14
Issue
2
Pages
421-432
ISSN
0896-6273 (ISSN-L)
DOI
10.1016/0896-6273(95)90298-8
OpenAlex
W2039754449
Cited by
144
References
70
Citations by year
2026: 4 · 2025: 2 · 2024: 3 · 2023: 7 · 2022: 2 · 2021: 4 · 2020: 5 · 2019: 7 · 2018: 4 · 2017: 5 · 2016: 4 · 2015: 7 · 2014: 6 · 2013: 4 · 2012: 6
FWCI
5.86
Type
journal article
Language
en
Open access
Licence
Locations
  • Neuron (publishedVersion)
  • PubMed (publishedVersion)
Funders
Ministry of Education, Culture, Sports, Science and Technology
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
Keywords
tau protein, MAP2, MAP2c, axonal transport, microtubule binding, projection domain, tau phosphorylation, neuronal cytoskeleton, chimeric mutants
MeSH terms
Amino Acid Sequence, Animals, Axons, Cells, Cultured, Dendrites, Embryo, Mammalian, Fluorescent Antibody Technique, Microtubule-Associated Proteins, Microtubules, Molecular Sequence Data, Neurons, Protein Binding, Sheep, Spinal Cord, Transfection, Proto-Oncogene Proteins c-myc, tau Proteins, Sequence Homology, Amino Acid, In Situ Hybridization, Mice

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