Structural basis for two-way communication between dynein and microtubules
The movement of cytoplasmic dynein on microtubule tracks is coordinated by the microtubule-binding domain (MTBD) and the ATPase domain via a coiled-coil stalk. Here authors use NMR and cryo-EM and suggest that the communication between the ATPase-domain and MTBD is achieved by sliding of the stalk α...
Guardado en:
Autores principales: | Noritaka Nishida, Yuta Komori, Osamu Takarada, Atsushi Watanabe, Satoko Tamura, Satoshi Kubo, Ichio Shimada, Masahide Kikkawa |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2020
|
Materias: | |
Acceso en línea: | https://doaj.org/article/d1ea81cf3f6d4a4f9f1f0bbb49e57455 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
She1 affects dynein through direct interactions with the microtubule and the dynein microtubule-binding domain
por: Kari H. Ecklund, et al.
Publicado: (2017) -
Structure of a microtubule-bound axonemal dynein
por: Travis Walton, et al.
Publicado: (2021) -
Local inhibition of microtubule dynamics by dynein is required for neuronal cargo distribution
por: Shaul Yogev, et al.
Publicado: (2017) -
A single protofilament is sufficient to support unidirectional walking of dynein and kinesin.
por: Keitaro Shibata, et al.
Publicado: (2012) -
A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity
por: In-Gyun Lee, et al.
Publicado: (2018)