Single Molecule Stepping and Structural Dynamics of Myosin X

Sun, Yujie; Satō, Osamu; Ruhnow, Felix; Arsenault, Mark E.; Ikebe, Mitsuo; Goldman, Yale E.

doi:10.1016/j.bpj.2009.12.783

Cited by 38 publications

(81 citation statements)

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“…This finding contradicts the findings of a recent study by Sun et al (16). Careful analysis of the Myo10 constructs used in these studies revealed that the two groups have used Myo10 constructs of slightly different lengths (Fig.…”

Section: Discussioncontrasting

confidence: 87%

“…The most salient implication of this anti-CCmediated Myo10 dimerization model is that the motor should be capable of walking on both single and bundled actin filaments (Fig. 5B), which has been directly demonstrated by in vitro single-molecule-based stepping assays (16). When walking on single actin filaments, Myo10 walked in the well-characterized hand-over-hand mode with a step size of ∼34 nm.…”

Section: Discussionmentioning

confidence: 79%

“…1A). Both in vitro single-molecule-based experiments and in vivo near single-molecule imaging assays have shown that Myo10 is capable of processive movements along actin filaments; thus it is expected that Myo10 can dimerize (15,16). Additionally, the role that Myo10 plays in filopodial induction suggests that it may function as a bundled actin filament-selective motor (17,18).…”

mentioning

confidence: 99%

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Antiparallel coiled-coil–mediated dimerization of myosin X

Lü¹,

Ye²,

Wei³

et al. 2012

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

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Processive movements of unconventional myosins on actin filaments generally require motor dimerization. A commonly accepted myosin dimerization mechanism is via formation of a parallel coiled-coil dimer by a stretch of amino acid residues immediately carboxyl-terminal to the motor's lever-arm domain. Here, we discover that the predicted coiled-coil region of myosin X forms a highly stable, antiparallel coiled-coil dimer (anti-CC). Disruption of the anti-CC either by single-point mutations or by replacement of the anti-CC with a parallel coiled coil with a similar length compromised the filopodial induction activity of myosin X. We further show that the anti-CC and the single α-helical domain of myosin X are connected by a semirigid helical linker. The anti-CC-mediated dimerization may enable myosin X to walk on both single and bundled actin filaments.Myo10 | molecular motor | filopodial growth

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Section: Discussioncontrasting

confidence: 87%

Section: Discussionmentioning

confidence: 79%

mentioning

confidence: 99%

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Antiparallel coiled-coil–mediated dimerization of myosin X

Lü¹,

Ye²,

Wei³

et al. 2012

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

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“…Using surface-immobilized F-actin, Nagy et al (15) showed that myosin-10 is more processive (i.e., walks further before detaching) on fascin-bundled F-actins compared with single F-actins, implying that the two heads might move along by binding alternately on neighboring F-actins, described as a "waddling" movement. Sun et al (18) found that processive motion along a single F-actin is increased if it is held suspended in midsolution, allowing the myosin molecule to take a leftSignificance Filopodia act as organelles for sensing and exploring the environment, as well as producing traction forces during cellular locomotion. Myosin-10 is a molecular motor crucial for intrafilopodial trafficking and filopodia formation.…”

mentioning

confidence: 99%

“…Each ATP-driven step taken by such truncated chimeras of myosin-10 has been reported to be in the range of 18-34 nm long (16)(17)(18)(19). Furthermore, live cell fluorescence imaging studies (20, 21) using a full-length GFP-tagged myosin-10 construct showed that single molecules move in a highly directed manner within the filopodia.…”

mentioning

confidence: 99%

Myosin-10 produces its power-stroke in two phases and moves processively along a single actin filament under low load

Takagi

Farrow

Billington

et al. 2014

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

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Myosin-10 is an actin-based molecular motor that participates in essential intracellular processes such as filopodia formation/ extension, phagocytosis, cell migration, and mitotic spindle maintenance. To study this motor protein's mechano-chemical properties, we used a recombinant, truncated form of myosin-10 consisting of the first 936 amino acids, followed by a GCN4 leucine zipper motif, to force dimerization. Negative-stain electron microscopy reveals that the majority of molecules are dimeric with a head-to-head contour distance of ∼50 nm. In vitro motility assays show that myosin-10 moves actin filaments smoothly with a velocity of ∼310 nm/s. Steady-state and transient kinetic analysis of the ATPase cycle shows that the ADP release rate (∼13 s −1 ) is similar to the maximum ATPase activity (∼12-14 s −1 ) and therefore contributes to rate limitation of the enzymatic cycle. Single molecule optical tweezers experiments show that under intermediate load (∼0.5 pN), myosin-10 interacts intermittently with actin and produces a power stroke of ∼17 nm, composed of an initial 15-nm and subsequent 2-nm movement. At low optical trap loads, we observed staircaselike processive movements of myosin-10 interacting with the actin filament, consisting of up to six ∼35-nm steps per binding interaction. We discuss the implications of this load-dependent processivity of myosin-10 as a filopodial transport motor.actomyosin | stable single alpha-helix | optical trapping | myosin X | myosin-5a

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Role of water in protein folding, oligomerization, amyloidosis and miniprotein

Vajda

Perczel

2014

J. Pept. Sci.

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The essential involvement of water in most fundamental extra-cellular and intracellular processes of proteins is criticallyreviewed and evaluated in this article. The role of water in protein behavior displays structural ambivalence; it can protectthe disordered peptide-chain by hydration or helps the globular chain-folding, but promotes also the protein aggregation, as well (see: diseases). A variety of amyloid diseases begins as benign protein monomers but develops then into toxic amyloid aggregates of fibrils. Our incomplete knowledge of this process emphasizes the essential need to reveal the principles governing this oligomerization. To understand the biophysical basis of the simpler in vitro amyloid formation may help todecipher also the in vivo way. Nevertheless, to ignore the central role of the water's effect among these events means toreceive an uncompleted picture of the true phenomenon. Therefore this review represents a stopgap role, because most published studies-with a few exceptions-have neglected the crucial importance of water in protein research. Thefollowing questions are discussed from the water's viewpoint: 1. interactions between water and proteins, 2. protein hydration/dehydration, 3. folding of proteins and miniproteins, 4. peptide/protein oligomerization, and 5. amyloidosis.

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Single Molecule Stepping and Structural Dynamics of Myosin X

Cited by 38 publications

References 0 publications

Antiparallel coiled-coil–mediated dimerization of myosin X

Antiparallel coiled-coil–mediated dimerization of myosin X

Myosin-10 produces its power-stroke in two phases and moves processively along a single actin filament under low load

Role of water in protein folding, oligomerization, amyloidosis and miniprotein

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