Kengan M - Evidence
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Kengan M - Evidence
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The image shows a myosin molecule carrying endorphin on a neuronal filament in the inner part of the parietal cortex of the brain.
The Science Manuscripts of S. Sunkavally. Page 241.
Dis-banded
Just like us, fruit flies are stripy beneath the skin. These sarcomeres – repeating bands of stretchy muscle tissue – contain fibres of myosin (highlighted in green) and actin (purple) griping and pulling at each other – as the sarcomeres shorten, the muscle contracts. This is heart muscle from fruit flies (Drosophila), used to investigate common faults in human heart disease. Compared to healthy muscle at the top, the sarcomeres at the bottom are much looser and swollen – in these hearts, researchers used RNA interference to hamper the activity of a protein called filamin, often shown to be altered in heart diseases like hypertrophic cardiomyopathy. Yet altering its activity in a different way – using CRISPR gene editing to change its structure – did not affect the flies as expected. Further studies might aim to solve this mystery, while altering genes and proteins reveals more about what we do, or perhaps don’t, have in common with Drosophila.
Written by John Ankers
Image from work by Flavie Ader and colleagues
Université Paris Cité, Paris, France
Image originally published with a Creative Commons Attribution – NonCommercial – NoDerivs (CC BY-NC-ND 4.0)
Published in Biology Open, September 2022
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All of the above motors have separate head, neck, and tail domains, as does myosin XI (Figure 1.27). (...) The tail domain usually contains coiled-coil regions for dimerization, and the end of the globular tail domain binds to specific organelles or "cargo" and is called the cargo domain (see Figure 1.27B). (...) The two heads of the dimer then alternately bind to the cytoskeleton and "walk" forward while the neck flexes as ATP is hydrolyzed (see Figure 1.27C).
"Plant Physiology and Development" int'l 6e - Taiz, L., Zeiger, E., Møller, I.M., Murphy, A.
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The cytoskeleton is very pretty 😍
Atomic resolution of muscle contraction
At the molecular level, muscle contraction is defined by myosin molecules pulling actin filaments. New electron cryomicroscopy images with unprecedented resolution taken by researchers at Osaka University reveal unexpectedly large conformational changes in the myosin molecule during the pull. These findings, which can be seen in Nature Communications, provide new insights into how myosin generates force and a paradigm for the construction of nanomachines.
Takashi Fujii, Keiichi Namba. Structure of actomyosin rigour complex at 5.2 Å resolution and insights into the ATPase cycle mechanism. Nature Communications, 2017; 8: 13969 DOI: 10.1038/ncomms13969
This is the architecture of skeletal muscle formed by regular arrays of myosin and actin filaments. Credit: Osaka University