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Eukaryotic cells have different motor proteins for transporting various cargo within the cell. These motor proteins differ based on the filament they associate with, the direction they move within the cell, and the type of cargo they transport. Motor proteins that associate with microtubules are known as microtubule-associated motor proteins. There are two families of microtubule-associated motor proteins —Kinesins and Dyneins. Both these proteins assist in the transport of cellular...
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Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
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In eukaryotic cells,  cytoskeletal filaments such as actin, microtubules, and intermediate filaments form a mesh-like cytoskeletal network. These filaments serve as tracks for transporting cellular cargo. Specialized motor proteins use the chemical energy stored in adenosine triphosphate (ATP) for this transport. During interphase, microtubules are polarized, with the plus-end towards the cell periphery and the minus-end towards the cell center. Two microtubule-associated motor proteins,...
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Microtubules form through the end-to-end polymerization of tubulin heterodimers. Kinetochore microtubules originate from the spindle poles, and their plus-ends connect with the kinetochores on sister-chromatids. Ndc80 protein complexes, present on the kinetochore, form low-affinity links with the plus end of these kinetochore microtubules.
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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
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Dendrite arborization requires the dynein cofactor NudE.

Ashley L Arthur1, Sihui Z Yang2, Allison M Abellaneda3

  • 1Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.

Journal of Cell Science
|April 25, 2015
PubMed
Summary

The dynein cofactor NudE is crucial for normal dendrite development in neurons. Loss of NudE disrupts Golgi outpost transport and microtubule stability, leading to abnormal dendrite branching.

Keywords:
Dendrite patterningDrosophilaDyneinMicrotubulesNde1Ndel1NudE

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Dynein, a microtubule motor, is vital for neuronal development.
  • Dynein cofactors regulate motor activity, but their roles in neuronal structure are not fully understood.

Purpose of the Study:

  • To investigate the function of the dynein cofactor NudE in neuronal morphogenesis.
  • To elucidate the molecular mechanisms by which NudE influences dendrite development.

Main Methods:

  • Utilized Drosophila melanogaster as a model organism.
  • Examined the effects of NudE loss on dendrite arborization and microtubule dynamics.
  • Investigated the association of NudE with Golgi outposts.
  • Assessed the rescue effects of Lis1 on NudE-deficient neurons.

Main Results:

  • Loss of NudE in Drosophila neurons causes abnormal dendrite arborization.
  • NudE associates with Golgi outposts, suggesting a role in regulating their transport for dendrite branching.
  • NudE deficiency leads to increased microtubule dynamics and altered microtubule stability.
  • Elevated Lis1 levels rescue the dendrite defects observed in NudE-mutant neurons.
  • The C-terminus of NudE is not essential for dendrite morphogenesis but may modulate NudE activity.

Conclusions:

  • NudE plays a critical role in regulating dendrite patterning by influencing Golgi outpost transport and microtubule stability.
  • NudE likely enhances the interaction between Lis1 and dynein, which is essential for proper neuronal architecture.
  • NudE functions as a key regulator of dynein-mediated processes during neuronal development.