A Ras-like domain in the light intermediate chain bridges the dynein motor to a cargo-binding region
Cytoplasmic dynein, a microtubule-based motor protein, transports many intracellular cargos by means of its light intermediate chain (LIC). In this study, we have determined the crystal structure of the conserved LIC domain, which binds the motor heavy chain, from a thermophilic fungus. We show that...
Main Authors: | Courtney M Schroeder, Jonathan ML Ostrem, Nicholas T Hertz, Ronald D Vale |
---|---|
Format: | Article |
Language: | English |
Published: |
eLife Sciences Publications Ltd
2014-10-01
|
Series: | eLife |
Subjects: | |
Online Access: | https://elifesciences.org/articles/03351 |
Similar Items
-
Adenovirus Recruits Dynein by an Evolutionary Novel Mechanism Involving Direct Binding to pH-Primed Hexon
by: Julian Scherer, et al.
Published: (2011-08-01) -
Kinesin and dynein use distinct mechanisms to bypass obstacles
by: Luke S Ferro, et al.
Published: (2019-09-01) -
Dynein-mediated transport and membrane trafficking control PAR3 polarised distribution
by: Julie Jouette, et al.
Published: (2019-01-01) -
A mathematical understanding of how cytoplasmic dynein walks on microtubules
by: L. Trott, et al.
Published: (2018-01-01) -
Drosophila VCP/p97 Mediates Dynein-Dependent Retrograde Mitochondrial Motility in Axons
by: Ashley E. Gonzalez, et al.
Published: (2020-04-01)