作者: Anthony J. Roberts , Takahide Kon , Peter J. Knight , Kazuo Sutoh , Stan A. Burgess
DOI: 10.1038/NRM3667
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摘要: Fuelled by ATP hydrolysis, dyneins generate force and movement on microtubules in a wealth of biological processes, including ciliary beating, cell division intracellular transport. The large mass complexity dynein motors have made elucidating their mechanisms sizable task. Yet, through combination approaches, X-ray crystallography, cryo-electron microscopy, single-molecule assays biochemical experiments, important progress has been towards understanding how these giant motor proteins work. From studies, model for the mechanochemical cycle is emerging, which nucleotide-driven flexing motions within AAA+ ring alter affinity its microtubule-binding stalk reshape mechanical element to movement.