Cell complexity: dynein movement explained (Introduction)

by David Turell , Tuesday, January 13, 2015, 00:49 (3604 days ago) @ David Turell

Kinesin and dynein move cargo in cells along microtubules. Kinesin movment is understood, but dynein is still being fully studied:-"They showed that two specific amino acid residues on the microtubule structure, R403 and E416, are key to turning on the switch that is critical for the activation of the dynein motor—demonstrating that when mutations in these sequences are present, the dynein fails to achieve directional movement on the microtubule, ending up simply moving back and forth in a random fashion. This lends weight to the idea, that has been generally accepted, that the motion of molecular motors is basically driven by random, Brownian motion, and that motors are able to move in one direction thanks to subtle changes in the strength of bonds at the motor-microtubule interface.-"Additionally, the group discovered that turning on the mechanical switch at the motor-microtubule interface leads to ATP hydrolysis. Their results altogether indicate that the subtle structural changes in the bonds at the interface are transmitted through a small change in the structure of the stalk—there are two coils that link the two binding regions, and a small shift in the configuration of the coils gives the cue for ATP hydrolysis at the ATP binding site."-
 Read more at: http://phys.org/news/2015-01-revealing-molecular-motor.html#jCp-These transport molecules literally walk along the tubules to carry cargo from one part of the cell to another. Just like a factory assembly line. God got there first before Henry Ford.