Is the dynein motor a winch?

Burgess, Simon; Knight, Peter J.

doi:10.1016/j.sbi.2004.03.013

Cited by 56 publications

(42 citation statements)

References 43 publications

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“…Movement of the tail relative to the head was also detected in fluorescence resonance energy transfer analysis of cytoplasmic dynein (5,6). Assuming that the observed ADP⅐Vi and no-nucleotide structures correspond to prepowerstroke and postpowerstroke conformations, respectively, the simplest model based on these results is that the stalk acts as a lever arm (3,4,(7)(8)(9), binding to a MT initially with a tilt toward the minus end, and then rotating toward the plus end to move the MT (Fig. 1 A).…”

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confidence: 83%

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Dynein pulls microtubules without rotating its stalk

Ueno

Yasunaga²,

Shingyoji³

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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Dynein is a microtubule motor that powers motility of cilia and flagella. There is evidence that the relative sliding of the doublet microtubules is due to a conformational change in the motor domain that moves a microtubule bound to the end of an extension known as the stalk. A predominant model for the movement involves a rotation of the head domain, with its stalk, toward the microtubule plus end. However, stalks bound to microtubules have been difficult to observe. Here, we present the clearest views so far of stalks in action, by observing sea urchin, outer arm dynein molecules bound to microtubules, with a new method, ''cryopositive stain'' electron microscopy. The dynein molecules in the complex were shown to be active in in vitro motility assays. Analysis of the electron micrographs shows that the stalk angles relative to microtubules do not change significantly between the ADP⅐vanadate and no-nucleotide states, but the heads, together with their stalks, shift with respect to their A-tubule attachments. Our results disagree with models in which the stalk acts as a lever arm to amplify structural changes. The observed movement of the head and stalk relative to the tail indicates a new plausible mechanism, in which dynein uses its stalk as a grappling hook, catching a tubulin subunit 8 nm ahead and pulling on it by retracting a part of the tail (linker).electron microscopy ͉ molecular motor

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confidence: 83%

“…1). A subdomain of the tail, called the linker, docks on the surface of the head, and changes in this interaction were proposed to cause the observed positional change of the tail (3,4). Movement of the tail relative to the head was also detected in fluorescence resonance energy transfer analysis of cytoplasmic dynein (5,6).…”

mentioning

confidence: 99%

Dynein pulls microtubules without rotating its stalk

Ueno

Yasunaga²,

Shingyoji³

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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“…This linker may correspond to a region, 600 amino acids before the first AAA domain, which may affect the ATPase cycle of the AAA1 domain (Gee et al 1997;Vallee and Hook 2006). Taken together, the dynein motor is organized in a unique fashion different from other motors such as kinesins and myosins (King 2000;Asai and Koonce 2001;Burgess and Knight 2004;Koonce and Samso 2004;Vallee and Hook 2006). The structure of the dynein motor is complex and also recent studies on dynein behaviors have added another layer of complexity onto this motor (Mallik et al 2004;Reck-Peterson et al 2006;Ross et al 2006;Toba et al 2006).…”

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confidence: 99%

Point Mutations in the Stem Region and the Fourth AAA Domain of Cytoplasmic Dynein Heavy Chain Partially Suppress the Phenotype of NUDF/LIS1 Loss in Aspergillus nidulans

Zhuang

Zhang²,

Xiang

2007

Genetics

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Cytoplasmic dynein performs multiple cellular tasks but its regulation remains unclear. The dynein heavy chain has a N-terminal stem that binds to other subunits and a C-terminal motor unit that contains six AAA (ATPase associated with cellular activities) domains and a microtubule-binding site located between AAA4 and AAA5. In Aspergillus nidulans, NUDF (a LIS1 homolog) functions in the dynein pathway, and two nudF6 partial suppressors were mapped to the nudA dynein heavy chain locus. Here we identified these two mutations. The nudAL1098F mutation resides in the stem region, and nudAR3086C is in the end of AAA4. These mutations partially suppress the phenotype of nudF deletion but do not suppress the phenotype exhibited by mutants of dynein intermediate chain and Arp1. Surprisingly, the stronger DnudF suppressor, nudAR3086C, causes an obvious decrease in the basal level of dynein's ATPase activity and an increase in dynein's distribution along microtubules. Thus, suppression of the DnudF phenotype may result from mechanisms other than simply the enhancement of dynein's ATPase activity. The fact that a mutation in the end of AAA4 negatively regulates dynein's ATPase activity but partially compensates for NUDF loss indicates the importance of the AAA4 domain in dynein regulation in vivo.

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“…Presence of the dyneins (outer arms) at a regular spacing along the microtubules, see the lower panel [18]. The head contains the ATP hydrolysis site, the stem anchors the dynein to the microtubule doublet and the stalk contains (at its tip) an ATP-sensitive microtubule-binding domain [4]. The conformational change driven by ATP hydrolysis alters the angle between the stem and stalk, which causes (relative) sliding of the microtubules [4].…”

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confidence: 99%

“…The head contains the ATP hydrolysis site, the stem anchors the dynein to the microtubule doublet and the stalk contains (at its tip) an ATP-sensitive microtubule-binding domain [4]. The conformational change driven by ATP hydrolysis alters the angle between the stem and stalk, which causes (relative) sliding of the microtubules [4]. Binding of an ATP molecule causes a weak detachment of the stalk from the microtubule (denoted by [MT,Dyn] in Fig.…”

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confidence: 99%

Emergence of flagellar beating from the collective behavior of individual ATP-powered dyneins

Namdeo

Onck

2016

Phys. Rev. E

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Flagella are hair-like projections form the surface of eukaryotic cells and play an important role in many cellular functions such as cell-motility. The beating of flagella is enabled by their internal architecture, the axoneme, and is powered by a dense distribution of motor proteins, dyneins. The dyneins deliver the required mechanical work through the hydrolysis of ATP. Although the dynein ATP-cycle, the axoneme microstructure and the flagellar beating kinematics are well studied, their integration into a coherent picture of ATP-powered flagellar beating is still lacking. Here we show that a timedelayed negative-work based switching mechanism is able to convert the individual sliding action of hundreds of dyneins into a regular overall beating pattern leading to propulsion. We developed a computational model based on a minimal

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Is the dynein motor a winch?

Cited by 56 publications

References 43 publications

Dynein pulls microtubules without rotating its stalk

Dynein pulls microtubules without rotating its stalk

Point Mutations in the Stem Region and the Fourth AAA Domain of Cytoplasmic Dynein Heavy Chain Partially Suppress the Phenotype of NUDF/LIS1 Loss in Aspergillus nidulans

Emergence of flagellar beating from the collective behavior of individual ATP-powered dyneins

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