Fine tuning a molecular motor: the location of alternative domains in the Drosophila myosin head

Bernstein, Sanford I.; Milligan, Ronald A.

doi:10.1006/jmbi.1997.1160

Cited by 70 publications

(66 citation statements)

References 30 publications

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“…It is interesting to note that residues 509 and 511 represent two of the five relay domain residues that vary among Drosophila muscle myosin isoforms (41). Thus, these residues, particularly residue 509, are likely to serve as modulators of relayconverter interaction.…”

Section: Discussionmentioning

confidence: 99%

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Mapping Interactions between Myosin Relay and Converter Domains That Power Muscle Function

Kronert

Melkani

et al. 2014

Journal of Biological Chemistry

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Background: Dissecting the molecular mechanism of muscle myosin function in vivo has proved difficult. Results: Transgenic fruit flies expressing mutant myosin and potential suppressor mutations suggest interacting amino acids. Conclusion: Communication between a relay domain residue and one in the converter is likely critical to myosin motor function. Significance: The transgenic system allows mapping of putative protein interactions essential for muscle contraction.

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Section: Discussionmentioning

confidence: 99%

“…Arg 759 is present in all versions of the converter. However, residues 509 and 511 vary among the three exon 9-encoded regions (41). This suggests that alternative versions of these residues may modulate relay-converter interaction (22).…”

Section: Putative Interactions Between Myosin Converter Domainmentioning

confidence: 99%

Mapping Interactions between Myosin Relay and Converter Domains That Power Muscle Function

Kronert

Melkani

et al. 2014

Journal of Biological Chemistry

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“…Embryonic and asynchronous muscle myosins differ by alternative splicing at four exons-3, 7, 9, and 11 (Bernstein and Milligan, 1997). The effect of expressing 'wrong' exons in embryonic or asynchronous myosins has been investigated for exons 3, 7, and 11 (briefly reviewed in Murphy and Spudich, 2000).…”

Section: Actin-myosin Interaction and Force Generationmentioning

confidence: 99%

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

125

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This is the second in a series of canonical reviews on invertebrate muscle. We cover here thin and thick filament structure, the molecular basis of force generation and its regulation, and two special properties of some invertebrate muscle, catch and asynchronous muscle. Invertebrate thin filaments resemble vertebrate thin filaments, although helix structure and tropomyosin arrangement show small differences. Invertebrate thick filaments, alternatively, are very different from vertebrate striated thick filaments and show great variation within invertebrates. Part of this diversity stems from variation in paramyosin content, which is greatly increased in very large diameter invertebrate thick filaments. Other of it arises from relatively small changes in filament backbone structure, which results in filaments with grossly similar myosin head placements (rotating crowns of heads every 14.5 nm) but large changes in detail (distances between heads in azimuthal registration varying from three to thousands of crowns). The lever arm basis of force generation is common to both vetebrates and invertebrates, and in some invertebrates this process is understood on the near atomic level. Invertebrate actomyosin is both thin (tropomyosin:troponin) and thick (primarily via direct Ca ++ binding to myosin) filament regulated, and most invertebrate muscles are dually regulated. These mechanisms are well understood on the molecular level, but the behavioral utility of dual regulation is less so. The phosphorylation state of the thick filament associated giant protein, twitchin, has been recently shown to be the molecular basis of catch. The molecular basis of the stretch activation underlying asynchronous muscle activity, however, remains unresolved.

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“…3). Tension rose simultaneously with the length step due to the stretching of fiber elastic components (Huxley and (Bernstein and Milligan, 1997). The regulatory (blue) and essential light chains (light blue) bind to the lever arm, which is linked to the catalytic domain by the converter.…”

Section: Stretch Activationmentioning

confidence: 99%

An embryonic myosin converter domain influences Drosophila indirect flight muscle stretch activation, power generation and flight

Wang

Newhard

Ramanath

et al. 2013

Journal of Experimental Biology

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Stretch activation (SA) is critical to the flight ability of insects powered by asynchronous, indirect flight muscles (IFMs). An essential muscle protein component for SA and power generation is myosin. Which structural domains of myosin are significant for setting SA properties and power generation levels is poorly understood. We made use of the transgenic techniques and unique single muscle myosin heavy chain gene of Drosophila to test the influence of the myosin converter domain on IFM SA and power generation. Replacing the endogenous converter with an embryonic version decreased SA tension and the rate of SA tension generation. The alterations in SA properties and myosin kinetics from the converter exchange caused power generation to drop to 10% of control fiber power when the optimal conditions for control fibers -1% muscle length (ML) amplitude and 150 Hz oscillation frequency -were applied to fibers expressing the embryonic converter (IFI-EC). Optimizing conditions for IFI-EC fiber power production, by doubling ML amplitude and decreasing oscillation frequency by 60%, improved power output to 60% of optimized control fiber power. IFI-EC flies altered their aerodynamic flight characteristics to better match optimal fiber power generation conditions as wing beat frequency decreased and wing stroke amplitude increased. This enabled flight in spite of the drastic changes to fiber mechanical performance.

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Fine tuning a molecular motor: the location of alternative domains in the Drosophila myosin head

Cited by 70 publications

References 30 publications

Mapping Interactions between Myosin Relay and Converter Domains That Power Muscle Function

Mapping Interactions between Myosin Relay and Converter Domains That Power Muscle Function

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

An embryonic myosin converter domain influences Drosophila indirect flight muscle stretch activation, power generation and flight

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