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    Interacting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals

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    Authors
    Lee, Kyounghwan
    Sulbaran, Guidenn
    Yang, Shixin
    Mun, Ji Young
    Alamo, Lorenzo
    Pinto, Antonio
    Sato, Osamu
    Ikebe, Mitsuo
    Liu, Xiong
    Korn, Edward D.
    Sarsoza, Floyd
    Bernstein, Sanford I.
    Padron, Raul
    Craig, Roger
    Show allShow less
    UMass Chan Affiliations
    Craig Lab
    Department of Radiology
    Department of Cell and Developmental Biology
    Document Type
    Journal Article
    Publication Date
    2018-02-01
    Keywords
    evolution
    interacting-heads motif
    muscle
    myosin II
    myosin regulation
    Biochemistry
    Cell Biology
    Cellular and Molecular Physiology
    
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    Link to Full Text
    https://doi.org/10.1073/pnas.1715247115
    Abstract
    Electron microscope studies have shown that the switched-off state of myosin II in muscle involves intramolecular interaction between the two heads of myosin and between one head and the tail. The interaction, seen in both myosin filaments and isolated molecules, inhibits activity by blocking actin-binding and ATPase sites on myosin. This interacting-heads motif is highly conserved, occurring in invertebrates and vertebrates, in striated, smooth, and nonmuscle myosin IIs, and in myosins regulated by both Ca(2+) binding and regulatory light-chain phosphorylation. Our goal was to determine how early this motif arose by studying the structure of inhibited myosin II molecules from primitive animals and from earlier, unicellular species that predate animals. Myosin II from Cnidaria (sea anemones, jellyfish), the most primitive animals with muscles, and Porifera (sponges), the most primitive of all animals (lacking muscle tissue) showed the same interacting-heads structure as myosins from higher animals, confirming the early origin of the motif. The social amoeba Dictyostelium discoideum showed a similar, but modified, version of the motif, while the amoeba Acanthamoeba castellanii and fission yeast (Schizosaccharomyces pombe) showed no head-head interaction, consistent with the different sequences and regulatory mechanisms of these myosins compared with animal myosin IIs. Our results suggest that head-head/head-tail interactions have been conserved, with slight modifications, as a mechanism for regulating myosin II activity from the emergence of the first animals and before. The early origins of these interactions highlight their importance in generating the inhibited (relaxed) state of myosin in muscle and nonmuscle cells.
    Source

    Proc Natl Acad Sci U S A. 2018 Feb 27;115(9):E1991-E2000. doi: 10.1073/pnas.1715247115. Epub 2018 Feb 14. Link to article on publisher's site

    DOI
    10.1073/pnas.1715247115
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/48265
    PubMed ID
    29444861
    Related Resources

    Link to Article in PubMed

    Rights
    © 2018. Published under the PNAS license, http://www.pnas.org/page/authors/licenses.
    ae974a485f413a2113503eed53cd6c53
    10.1073/pnas.1715247115
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    Radiology Publications
    Padrón-Craig Lab

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