Unknown

Dataset Information

0

Functions and mechanics of dynein motor proteins.


ABSTRACT: Fuelled by ATP hydrolysis, dyneins generate force and movement on microtubules in a wealth of biological processes, including ciliary beating, cell division and intracellular transport. The large mass and complexity of dynein motors have made elucidating their mechanisms a sizable task. Yet, through a combination of approaches, including X-ray crystallography, cryo-electron microscopy, single-molecule assays and biochemical experiments, important progress has been made towards understanding how these giant motor proteins work. From these studies, a model for the mechanochemical cycle of dynein is emerging, in which nucleotide-driven flexing motions within the AAA+ ring of dynein alter the affinity of its microtubule-binding stalk and reshape its mechanical element to generate movement.

SUBMITTER: Roberts AJ 

PROVIDER: S-EPMC3972880 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

Functions and mechanics of dynein motor proteins.

Roberts Anthony J AJ   Kon Takahide T   Knight Peter J PJ   Sutoh Kazuo K   Burgess Stan A SA  

Nature reviews. Molecular cell biology 20130925 11


Fuelled by ATP hydrolysis, dyneins generate force and movement on microtubules in a wealth of biological processes, including ciliary beating, cell division and intracellular transport. The large mass and complexity of dynein motors have made elucidating their mechanisms a sizable task. Yet, through a combination of approaches, including X-ray crystallography, cryo-electron microscopy, single-molecule assays and biochemical experiments, important progress has been made towards understanding how  ...[more]

Similar Datasets

| S-EPMC3415999 | biostudies-literature
| S-EPMC6600642 | biostudies-literature
| S-EPMC2866193 | biostudies-literature
| S-EPMC8592121 | biostudies-literature
| S-EPMC6933798 | biostudies-literature
| S-EPMC7090908 | biostudies-literature
| S-EPMC5816248 | biostudies-literature
| S-EPMC3237626 | biostudies-literature
| S-EPMC3169322 | biostudies-literature
| S-EPMC4269335 | biostudies-literature