Ontology highlight
ABSTRACT:
SUBMITTER: Uchimura S
PROVIDER: S-EPMC4298687 | biostudies-literature | 2015 Jan
REPOSITORIES: biostudies-literature
Uchimura Seiichi S Fujii Takashi T Takazaki Hiroko H Ayukawa Rie R Nishikawa Yosuke Y Minoura Itsushi I Hachikubo You Y Kurisu Genji G Sutoh Kazuo K Kon Takahide T Namba Keiichi K Muto Etsuko E
The Journal of cell biology 20150112 2
Dynein is a motor protein that moves on microtubules (MTs) using the energy of adenosine triphosphate (ATP) hydrolysis. To understand its motility mechanism, it is crucial to know how the signal of MT binding is transmitted to the ATPase domain to enhance ATP hydrolysis. However, the molecular basis of signal transmission at the dynein-MT interface remains unclear. Scanning mutagenesis of tubulin identified two residues in α-tubulin, R403 and E416, that are critical for ATPase activation and dir ...[more]