Antiparallel coiled-coil–mediated dimerization of myosin X

Lü, Qing; Ye, Fei; Wei, Zhiyi; Wen, Zilong; Zhang, Mingjie

doi:10.1073/pnas.1208642109

Cited by 63 publications

(97 citation statements)

References 26 publications

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“…Although the structures of many antiparallel coiled coils have been reported, most of them are intramolecular structures folding at a flexible hinge (26 -28). Those that are formed intermolecularly are mostly heterodimers (29), and homodimeric antiparallel coiled coils are usually very short (30,31). One exception is Rad50, which was found to form an 80-nm-long homodimeric antiparallel coiled coil upon ATP binding (32); but the Rad50 dimer does not assemble into filamentous polymers.…”

Section: Discussionmentioning

confidence: 99%

Assembly Mechanism of Trypanosoma brucei BILBO1, a Multidomain Cytoskeletal Protein

Vidilaseris

Shimanovskaya

Esson

et al. 2014

Journal of Biological Chemistry

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Background: TbBILBO1 is the only known protein component of the flagellar pocket collar, but its assembly remains unknown. Results: Structural dissections of the three different domains of TbBILBO1 revealed their roles in protein assembly. Conclusion: TbBILBO1 forms a linear filament that interacts laterally to form a fibrous bundle. Significance: The data show how two types of coiled coil act together to assemble TbBILBO1 into long filaments.

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Section: Discussionmentioning

confidence: 99%

Assembly Mechanism of Trypanosoma brucei BILBO1, a Multidomain Cytoskeletal Protein

Vidilaseris

Shimanovskaya

Esson

et al. 2014

Journal of Biological Chemistry

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“…At present, the resolution of our negatively stained EMs, obtained using recombinant M10HMM with the leucine zipper sequence after amino acid 936, does not allow us to discern the tail structure directly. We know that the majority of molecules dimerize into two-headed motors, and our structural models [based on the published structures Protein Data Bank (PDB) ID code 2LW9 (25) and 2ZTA (55), as shown in Fig. S2 A and B] indicate that the APCC motif can still form, but it is not clear if the region is instead triggered to form a parallel coiled-coil or some other conformation altogether.…”

Section: Discussionmentioning

confidence: 99%

“…Another potentially novel feature of myosin-10 has been the recent finding that a 52-residue fragment of the molecule (amino acids 883-934) forms an APCC dimer (25). However, it is worth noting that earlier work using a 93 amino acid peptide from the coiled-coil forming region of scallop muscle myosin-2 also gave rise to an APCC structure (53), but this was known to form a parallel coiled-coil in the context of the full-length molecule (54).…”

Section: Discussionmentioning

confidence: 99%

“…However, recent structural, biochemical, and molecular modeling studies (12,23,24) indicate that myosin-10 has a 70-amino acid residue-long (amino acids 813-882) SAH domain immediately following its three IQ motifs, which might serve to extend the lever arm. A structural study (25) using a peptide corresponding to amino acid residues 883-934 showed this later region can form a relatively low affinity (K d = 0.6 μM) APCC. The authors postulated that the APCC region might mediate dimerization of myosin-10 heavy chains within the filopodia, where the local concentration is highest.…”

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confidence: 99%

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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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“…8C and Table S2) was again similar to that in the DdMyo7 rescue cells. Although myosin motor activity is critical for filopod initiation, the ability of motor-Pro1-MyTH4a to promote filopod formation could be explained by interactions of MyTH4a with yetunidentified target proteins and/or conformational stability provided by the globular MyTH4 domain, favoring recruitment, clustering of myosin motors, or dimerization of the extended lever arm and post-lever arm region (44). Substitution of mCherry for MyTH4a did not support filopod formation (Fig.…”

Section: Lml Vt E S L T Rgt Ky Vf Nt Sqas Mbmyo22 1984 Aeamyo22 2218 mentioning

confidence: 99%

MyTH4-FERM myosins have an ancient and conserved role in filopod formation

Petersen

Goodson

Arthur

et al. 2016

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

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The formation of filopodia in Metazoa and Amoebozoa requires the activity of myosin 10 (Myo10) in mammalian cells and of Dictyostelium unconventional myosin 7 (DdMyo7) in the social amoeba Dictyostelium. However, the exact roles of these MyTH4-FERM myosins (myosin tail homology 4-band 4.1, ezrin, radixin, moesin; MF) in the initiation and elongation of filopodia are not well defined and may reflect conserved functions among phylogenetically diverse MF myosins. Phylogenetic analysis of MF myosin domains suggests that a single ancestral MF myosin existed with a structure similar to DdMyo7, which has two MF domains, and that subsequent duplications in the metazoan lineage produced its functional homolog Myo10. The essential functional features of the DdMyo7 myosin were identified using quantitative live-cell imaging to characterize the ability of various mutants to rescue filopod formation in myo7-null cells. The two MF domains were found to function redundantly in filopod formation with the C-terminal FERM domain regulating both the number of filopodia and their elongation velocity. DdMyo7 mutants consisting solely of the motor plus a single MyTH4 domain were found to be capable of rescuing the formation of filopodia, establishing the minimal elements necessary for the function of this myosin. Interestingly, a chimeric myosin with the Myo10 MF domain fused to the DdMyo7 motor also was capable of rescuing filopod formation in the myo7-null mutant, supporting fundamental functional conservation between these two distant myosins. Together, these findings reveal that MF myosins have an ancient and conserved role in filopod formation.C ells interact with their environment through protrusions such as filopodia that form in response to extracellular cues and mediate initial contact with the substrate. Filopodia are slender, actin-filled membrane projections that are highly dynamic, growing and shrinking from peripheral regions of cells, such as lamellipodia and the dorsal surface (1). A wide variety of cell types including amoebae such as Dictyostelium discoideum (2) and Acanthamoeba (3), as well as mammalian vascular endothelial cells (4) and developing neurons (5), extend filopodia. Filopodia are typically 1-10 μm long and 0.1-0.3 μm in diameter and have a core of 10-30 parallel actin filaments with a protein-rich complex at their tip (1, 6, 7). Modified forms of filopodia such as dendritic spines, cytonemes, and tunneling nanotubes promote intercellular communication during multicellular development (8-10). Defects in filopod formation alter cell spreading and adhesion (2, 11, 12), whereas overproduction of filopodia or filopodia-like protrusions is associated with increased invasiveness of metastatic cancer cells (13)(14)(15).Filopod elongation is triggered by small GTPase activity (1, 16) and is driven by the activity of actin elongation factors including vasodilator-stimulated phosphoprotein (VASP) and formins, and the actin core is stabilized by actin cross-linking proteins (1). A MyTH4-FERM (myosin tail homology ...

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Antiparallel coiled-coil–mediated dimerization of myosin X

Cited by 63 publications

References 26 publications

Assembly Mechanism of Trypanosoma brucei BILBO1, a Multidomain Cytoskeletal Protein

Assembly Mechanism of Trypanosoma brucei BILBO1, a Multidomain Cytoskeletal Protein

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

MyTH4-FERM myosins have an ancient and conserved role in filopod formation

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