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 Oliver Ingvar Wagner},
  journal={Neurobiology of Disease},
  year={2011},
  volume={43},
  pages={495-506}
}
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UNC-10/SYD-2 complex is sufficient to link kinesin-3 UNC-104 to RAB-3 containing synaptic vesicles in the absence of the motor’s PH domain
TLDR
Results from RT-PCR and Western blot experiments favor a genetic relation between SYD-2, UNC-10 and RAB-3, as well as co-immunoprecipitation assays revealed changes in binding affinities between SYd-2 and UNC-104 depending on the presence or absence ofUNC-10 or R AB-3.
The Microtubule Associated Protein Tau Regulates KIF1A Pausing Behavior and Motility
TLDR
A new mechanism of Tau-mediated motility regulation is introduced, providing insight on how disruptions in axonal transport can lead to disease state pathology.
PTL-1 regulates neuronal integrity and lifespan in C. elegans
TLDR
PTL-1 is the sole Caenorhabditis elegans homolog of tau and MAP2, which are members of the mammalian family of microtubule-associated proteins (MAPs) and is important for the maintenance of neuronal health as animals age, as well as in the regulation of whole organism lifespan.
Regulation of age-related structural integrity in neurons by protein with tau-like repeats (PTL-1) is cell autonomous
TLDR
It is demonstrated that the regulation of neuronal ageing by PTL-1 occurs via a cell-autonomous mechanism, and that, at least for a specific group of mechanosensory neurons, premature neuronal ageing and organismal ageing can be decoupled.
Characterization of TAG-63 and its role on axonal transport in C. elegans
TLDR
TAG-63 is characterized as a NF-like protein with sequence homologies to human NEFH carrying various coiled coils as well as clustered phosphorylation sites and exhibits features of NFL such as a molecular weight of around 70 kD, the lack of KSP repeats and the ability to form 10 nm filamentous structures in transmission electron micrographs.
Vesicular Axonal Transport is Modified In Vivo by Tau Deletion or Overexpression in Drosophila
TLDR
It is shown that loss of Tau in tau mutants not only leads to a decrease in axonal microtubule density, but also impairs axonal vesicular transport, albeit to a lesser extent compared to the effects of an excess of Tau.
What Renders TAU Toxic
TLDR
The non-axonal localization of TAU, the role phosphorylation has in TAU toxicity and how TAU impairs mitochondrial functions are discussed, and the knock-out of the TAU/MAP2 homolog PTL-1 in worms is discussed.
What rendersTAU toxic
TAU is a microtubule-associated protein that under pathological conditions such asAlzheimer’s disease (AD) forms insoluble, filamentous aggregates. When 20years afterTAU’s discovery the first TAU…
Neuronal protein with tau-like repeats (PTL-1) regulates intestinal SKN-1 nuclear accumulation in response to oxidative stress
TLDR
The data suggest that PTL‐1 functions via neurons to modulate SKN‐1, clarifying the role of this protein in the stress response and longevity and testing lifespan and found that P TL‐1 and SKN-1 regulate longevity via similar processes.
PTP-3 phosphatase promotes intramolecular folding of SYD-2 to inactivate kinesin-3 UNC-104 in neurons.
TLDR
Intramolecular FRET analysis in living nematodes demonstrates that SYD-2 largely exists in an open conformation state in ptp-3 mutants, and epistatic analysis revealed that PTP-3 is upstream of SYd-2 to regulate its intramolescular folding.
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