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Related Experiment Video

Updated: Jun 6, 2026

Evaluation of Motor Impairment in C. elegans Models of Amyotrophic Lateral Sclerosis

Evaluation of Motor Impairment in C. elegans Models of Amyotrophic Lateral Sclerosis

Published on: September 2, 2021

A cytoplasmic dynein tail mutation impairs motor processivity.

Kassandra M Ori-McKenney¹, Jing Xu, Steven P Gross

¹Department of Pathology and Cell Biology, Columbia University. New York, NY 10032, USA.

Nature Cell Biology

|November 25, 2010

Summary

This summary is machine-generated.

Mutant dynein tails impair motor function, causing neurodegenerative disease in mice by inhibiting axonal transport. This study reveals how motor deficiencies link to disease progression.

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Evaluation of Motor Impairment in C. elegans Models of Amyotrophic Lateral Sclerosis

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Organelle Transport in Cultured Drosophila Cells: S2 Cell Line and Primary Neurons.

Organelle Transport in Cultured Drosophila Cells: S2 Cell Line and Primary Neurons.

Published on: November 20, 2013

Area of Science:

Molecular biology
Neuroscience
Cell biology

Background:

Mutations in cytoplasmic dynein's tail are linked to neurodegenerative diseases.
The 'Legs at odd angles' (Loa) mouse model exhibits impaired retrograde axonal transport, but the underlying molecular defects remain unclear.

Purpose of the Study:

To investigate the molecular deficiencies in the mutant dynein molecule from Loa mice.
To understand how these deficiencies contribute to neurodegeneration.

Main Methods:

Purification of dynein from wild-type and Loa mutant mice.
Biochemical assays.
Single-molecule analysis.
Live-cell imaging.

Main Results:

Dynein from Loa mutant mice showed significantly inhibited motor run-length both in vitro and in vivo.
Altered motor domain coordination was observed in the mutant dynein.
These findings indicate a direct impact of dynein tail mutations on motor function and processivity.

Conclusions:

The dynein tail plays a crucial role in motor function.
This study provides direct evidence linking single-dynein motor processivity defects to neurodegenerative disease.