Related Experiment Video
Updated: Feb 18, 2026

Measuring Axonal Cargo Transport in Mouse Primary Cortical Cultured Neurons
Published on: February 24, 2023
Cone myoid elongation involves unidirectional microtubule movement mediated by dynein-1
Tylor R Lewis1, Mariusz Zareba2, Brian A Link1
1Department of Cell Biology, Neurobiology, and Anatomy, Medical College of Wisconsin, Milwaukee, WI 53226.
Abstract:
Teleosts and amphibians exhibit retinomotor movements, morphological changes in photoreceptors regulated by light and circadian rhythms. Cone myoid elongation occurs during dark adaptation, leading to the positioning of the cone outer segment closer to the retinal pigment epithelium. Although it has been shown that microtubules are essential for cone myoid elongation, the underlying mechanism has not been established. In this work, we generated a transgenic line of zebrafish expressing a photoconvertible form of α-tubulin (tdEOS-tubulin) specifically in cone photoreceptors. Using superresolution structured illumination microscopy in conjunction with both pharmacological and genetic manipulation, we show that cytoplasmic dynein-1, which localizes to the junction between the ellipsoid and myoid, functions to shuttle microtubules from the ellipsoid into the myoid during the course of myoid elongation. We propose a novel model by which stationary complexes of cytoplasmic dynein-1 are responsible for the shuttling of microtubules between the ellipsoid and myoid is the underlying force for the morphological change of myoid elongation.
Related Concept Videos
The Movement of Organelles and Vesicles
Mechanism of Ciliary Motion
The cilia are made up of microtubules in a 9+2 arrangement, with nine microtubule doublet ring bundles, surrounding a pair of central singlet microtubule bundles. The doublet microtubule bundles are...
Microtubule Associated Motor Proteins
Microtubules in Cell Motility
Microtubules
Microtubules
Microtubules have two structurally similar globular protein subunits: α and β tubulins. In the cytosol, the α and β tubulins form a heterodimer....

