Tau/PTL-1 associates with kinesin-3 KIF1A/UNC-104 and affects the motor's motility characteristics in C. elegans neurons

@article{Tien2011TauPTL1AW,
  title={Tau/PTL-1 associates with kinesin-3 KIF1A/UNC-104 and affects the motor's motility characteristics in C. elegans neurons},
  author={Nai-Wen Tien and Gong-Her Wu and Chih-Chun Hsu and Chien-Yu Chang and O. Wagner},
  journal={Neurobiology of Disease},
  year={2011},
  volume={43},
  pages={495-506}
}
Tauopathies are neurodegenerative diseases based on pathological tau-aggregation including Alzheimer's disease, frontotemporal dementia (FTD) and Pick's disease. In general, cargo (e.g., β-amyloid precursor protein, tau, neurofilaments) accumulation is a commonly observed phenomenon in degenerated neurons. Therefore, it is crucial to investigate the interaction between cargo, microtubule-binding proteins and molecular motors. We report the effect of tau/PTL-1 (protein with tau-like repeats) on… Expand
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30 Citations
Background Citations
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Methods Citations
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30 Citations

Citation Type

Citation Type

UNC-10/SYD-2 complex is sufficient to link kinesin-3 to RAB-3 containing synaptic vesicles in the absence of the motor’s PH domain
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PTL-1 regulates neuronal integrity and lifespan in C. elegans
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Regulation of age-related structural integrity in neurons by protein with tau-like repeats (PTL-1) is cell autonomous
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Characterization of TAG-63 and its role on axonal transport in C. elegans
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Vesicular Axonal Transport is Modified In Vivo by Tau Deletion or Overexpression in Drosophila
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What Renders TAU Toxic
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What rendersTAU toxic
Neuronal protein with tau-like repeats (PTL-1) regulates intestinal SKN-1 nuclear accumulation in response to oxidative stress
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PTP-3 phosphatase promotes intramolecular folding of SYD-2 to inactivate kinesin-3 UNC-104 in neurons.
PTP-3(LAR PTPR) promotes intramolecular folding of SYD-2(liprin-α) to inactivate UNC-104(KIF1A) in neurons
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References

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