• Corpus ID: 88524697

The physical parameters of neuronal cargo transport regulated by autoinhibition of kinesin UNC-104

@article{Hayashi2019ThePP,
  title={The physical parameters of neuronal cargo transport regulated by autoinhibition of kinesin UNC-104},
  author={Kumiko Hayashi and Shiori Matsumoto and Miki G. Miyamoto and Shinsuke Niwa},
  journal={arXiv: Biological Physics},
  year={2019}
}
In this review, we focus on the kinesin-3 family molecular motor protein UNC-104 and its regulatory protein ARL-8. UNC-104, originally identified in Caenorhabditis elegans (C. elegans), has a primary role transporting synaptic vesicle precursors (SVPs). Although in vitro single-molecule experiments have been performed to primarily investigate the kinesin motor domain, these have not addressed the in vivo reality of the existence of regulatory proteins, such as ARL-8, that control kinesin… 
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Editorial: Special issue of Biophysical Reviews dedicated to the joint 10th Asian Biophysics Association Symposium and 42nd Australian Society for Biophysics Meeting, Melbourne, Australia, December 2–6, 2018

TLDR
This special issue of Biophysical Reviews is based on the proceedings of the first joint meeting between the ABA and the ASB, held at RMIT University, Melbourne, Australia, from the 2nd to the 6th of December 2018.

References

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Autoinhibition of a Neuronal Kinesin UNC-104/KIF1A Regulates the Size and Density of Synapses.

Synaptic scaffolding protein SYD-2 clusters and activates kinesin-3 UNC-104 in C. elegans

TLDR
A kinesin scaffolding protein is presented that controls both motor clustering along axons and motor motility, resulting in reduced cargo transport efficiency upon loss of interaction, and is mapped by using yeast 2-hybrid and pull-down assays.

The lipid binding pleckstrin homology domain in UNC-104 kinesin is necessary for synaptic vesicle transport in Caenorhabditis elegans.

TLDR
It is shown that a pleckstrin homology (PH) domain in UNC-104 is essential for membrane transport in living C. elegans, that this PH domain binds specifically to phosphatidylinositol-4,5-bisphosphate (PI( 4,5)P(2), and that point mutants in the PH domain that interfere with PI(4, 5)P2) binding in vitro also interfere with UNC- 104 function in vivo.

Direct Visualization of the Movement of the Monomeric Axonal Transport Motor UNC-104 along Neuronal Processes in LivingCaenorhabditis elegans

TLDR
This is the first direct visualization and analysis of the movement of specifically labeled microtubule motor proteins along axons in vivo and it is shown that fluorescent motor proteins moving in both directions along neuronal processes are identified definitely as axons and others as dendrites.

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TLDR
The physical and biophysical properties that influence motor regulation in healthy neurons are discussed and the evidence for the role of transport in neurodegeneration is discussed, highlighting two pathways that may contribute to transport impairment-dependent disease: genetic mutations or variation, and protein aggregation.

Non-invasive force measurement reveals the number of active kinesins on a synaptic vesicle precursor in axonal transport regulated by ARL-8.

TLDR
The number of active UNC-104 molecules hauling a single SVP in axons in the worm Caenorhabditis elegans was counted by applying a newly developed non-invasive force measurement technique, and the distribution of the force acting on a SVP transported by UNC- 104 was spread out over several clusters, implying the presence of several force-producing units (FPUs).

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TLDR
A tug-of-war mechanism based on molecular motors that pull cargos along cytoskeletal filaments is found to be highly cooperative and to exhibit seven different motility regimes depending on the precise values of the single motor parameters.

Mammalian Kinesin-3 Motors Are Dimeric In Vivo and Move by Processive Motility upon Release of Autoinhibition

TLDR
Kinesin-3 motors drive the transport of synaptic vesicles and other membrane-bound organelles in neuronal cells and may be uniquely suited to use both diffuse and processive motility to drive long-distance transport in neurons.

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TLDR
This method can be applied to the observation of any cargo molecule in any cells by modifying the target proteins and/or the cells they are expressed in and can clarify the molecular mechanisms of axonal transport and IFT.