Dynein structure and power stroke

Burgess, Simon; Walker, Matthew; Sakakibara, Hitoshi; Knight, Peter J.; Oiwa, Kazuhiro

doi:10.1038/nature01377

Cited by 478 publications

(608 citation statements)

References 40 publications

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“…That the Brownian search-and-catch significantly contributes to force generation in myosin-V challenges the theory that biological molecular motors, such as myosin, kinesin and dynein, generate force primarily from a structural change 14,15,40,41 (in the case of myosin-V, this is the lever-arm swing). More likely, the work distribution between the structural change and the Brownian searchand-catch would vary with the molecular motor.…”

Section: Discussionmentioning

confidence: 99%

Switching of myosin-V motion between the lever-arm swing and Brownian search-and-catch

et al. 2012

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motor proteins are force-generating nanomachines that are highly adaptable to their everchanging biological environments and have a high energy conversion efficiency. Here we constructed an imaging system that uses optical tweezers and a DnA handle to visualize elementary mechanical processes of a nanomachine under load. We apply our system to myosin-V, a well-known motor protein that takes 72 nm 'hand-over-hand' steps composed of a 'lever-arm swing' and a 'Brownian search-and-catch'. We find that the lever-arm swing generates a large proportion of the force at low load ( < 0.5 pn), resulting in 3 k B T of work. At high load (1.9 pn), however, the contribution of the Brownian search-and-catch increases to dominate, reaching 13 k B T of work. We believe the ability to switch between these two forcegeneration modes facilitates myosin-V function at high efficiency while operating in a dynamic intracellular environment.1 Soft Biosystem Group, Laboratories for Nanobiology, Graduate School of Frontier Biosciences, Osaka University, 1-3 Yamadaoka, Suita, Osaka 565-0871, Japan. 2 Graduate School of Medicine, Osaka University, 1-3 Yamadaoka, Suita, 565-0871, Japan. switching of myosin-V motion between the lever-arm swing and Brownian search-and-catch

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Section: Discussionmentioning

confidence: 99%

Switching of myosin-V motion between the lever-arm swing and Brownian search-and-catch

et al. 2012

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“…The microtubule-binding site is located at the end of a unique ~10-nm stalk that extends from the side that is opposite the first AAA+ unit. Force generation is proposed to involve a rotation of the entire head 132 (panel a).…”

Section: Box 1 | Properties Of Molecular Motorsmentioning

confidence: 99%

Powering membrane traffic in endocytosis and recycling

Soldati

Schliwa

2006

Nat Rev Mol Cell Biol

314

279

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| Early in evolution, the diversification of membrane-bound compartments that characterize eukaryotic cells was accompanied by the elaboration of molecular machineries that mediate intercompartmental communication and deliver materials to specific destinations. Molecular motors that move on tracks of actin filaments or microtubules mediate the movement of organelles and transport between compartments. The subjects of this review are the motors that power the transport steps along the endocytic and recycling pathways, their modes of attachment to cargo and their regulation.The emergence of eukaryotic cells was accompanied by the development of endomembrane systems that compartmentalize biochemical pathways and biosynthetic processes. An evolutionary trend towards increasing complexity and subcellular specialization necessitated the development of machineries for intercompartmental communication. Molecular assemblies evolved to confer specificity to the interactions of donor and acceptor compartments (budding, sorting, tethering and fusion). Cytoskeletal polymers such as actin filaments and microtubules, which help segregate genetic material and determine cell shape and subcellular architecture, were co-opted as tracks for transport. In animal cells, microtubules support long-range transport, whereas the more flexible actin filaments serve short-range movements both near the cell periphery and in the cell interior. Also, actin filaments can be woven into dense networks of short fibres through the action of crosslinkers and branchpromoting complexes. On the other hand, in many plant cells, bundled actin filaments can form extended tracks for long-distance transport. Owing to the gel-like nature of the cytoplasm, the Brownian movement of organelles is severely restricted and cargoes have to be transported to their destinations at the expense of energy. Furthermore, seemingly random, but motor-dependent, movement is proposed to increase the probability of vesicle collisions and therefore promote fusion events. Movement is powered by three ATP-dependent motors: myosin, kinesin and dynein. Over the course of eukaryotic evolution, these motors have diversified into a large number of families with specific tasks (FIG. 1).Here, we review the involvement of molecular motors in the movement of endosomes and in vesicular trafficking along the endocytic and recycling pathways. These pathways are summarized in FIG. 2. We do not, however,

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“…The neck is angled towards the MT plus end when the motor domain binds to the track, so when the neck is undocked any net movement of the cargo must be towards the minus end. C. Alternative conformations of a dynein monomer (based on images of Burgess et al [32]). The globular ATPase domain (AAA) is shown as a red ring.…”

Section: Discussionmentioning

confidence: 99%

“…The coiled-coil "stalk" (black and blue) ends in a small globular domain that interacts with tubulin [33]. When no nucleotide is added to EM samples, the stalk and stem appear distant from each other but when ADP and vanadate (Vi) are present the AAA domain apparently rotates relative to the stem, bringing the stalk much closer [32]. Only 2D projected views of the two conformations are known at present so it is unclear whether there is a big change in the shape of the motor domain or whether the difference is mainly a rotation to give a different view.…”

Section: Discussionmentioning

confidence: 99%

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Molecular motors: not quite like clockwork

Amos

2008

Cell. Mol. Life Sci.

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Models commonly used to explain the mechanism of myosin motors typically include a powerstroke that is attributed to a conformational change in the motor domain and amplified by a long leverarm that connects the motor domain to the cargo. Similar models have proved less enlightening in the case of microtubule motors, for which it may be more helpful to consider models involving thermally driven mechanisms.

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Dynein structure and power stroke

Cited by 478 publications

References 40 publications

Switching of myosin-V motion between the lever-arm swing and Brownian search-and-catch

Switching of myosin-V motion between the lever-arm swing and Brownian search-and-catch

Powering membrane traffic in endocytosis and recycling

Molecular motors: not quite like clockwork

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