Show simple item record

dc.contributor.authorLee, Kyounghwan
dc.contributor.authorSulbaran, Guidenn
dc.contributor.authorYang, Shixin
dc.contributor.authorMun, Ji Young
dc.contributor.authorAlamo, Lorenzo
dc.contributor.authorPinto, Antonio
dc.contributor.authorSato, Osamu
dc.contributor.authorIkebe, Mitsuo
dc.contributor.authorLiu, Xiong
dc.contributor.authorKorn, Edward D.
dc.contributor.authorSarsoza, Floyd
dc.contributor.authorBernstein, Sanford I.
dc.contributor.authorPadrón, Raúl
dc.contributor.authorCraig, Roger
dc.date2022-08-11T08:10:47.000
dc.date.accessioned2022-08-23T17:20:16Z
dc.date.available2022-08-23T17:20:16Z
dc.date.issued2018-02-01
dc.date.submitted2018-03-07
dc.identifier.citation<p>Proc Natl Acad Sci U S A. 2018 Feb 27;115(9):E1991-E2000. doi: 10.1073/pnas.1715247115. Epub 2018 Feb 14. <a href="https://doi.org/10.1073/pnas.1715247115">Link to article on publisher's site</a></p>
dc.identifier.issn0027-8424 (Linking)
dc.identifier.doi10.1073/pnas.1715247115
dc.identifier.pmid29444861
dc.identifier.urihttp://hdl.handle.net/20.500.14038/48265
dc.description.abstractElectron 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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=29444861&dopt=Abstract">Link to Article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1073/pnas.1715247115
dc.rights© 2018. Published under the PNAS license, http://www.pnas.org/page/authors/licenses.
dc.subjectevolution
dc.subjectinteracting-heads motif
dc.subjectmuscle
dc.subjectmyosin II
dc.subjectmyosin regulation
dc.subjectBiochemistry
dc.subjectCell Biology
dc.subjectCellular and Molecular Physiology
dc.titleInteracting-heads motif has been conserved as a mechanism of myosin II inhibition since before the origin of animals
dc.typeJournal Article
dc.source.journaltitleProceedings of the National Academy of Sciences of the United States of America
dc.source.volume115
dc.source.issue9
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1389&amp;context=radiology_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/radiology_pubs/379
dc.legacy.embargo2018-08-27T00:00:00-07:00
dc.identifier.contextkey11721036
refterms.dateFOA2022-08-23T17:20:16Z
html.description.abstract<p>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.</p>
dc.identifier.submissionpathradiology_pubs/379
dc.contributor.departmentCraig Lab
dc.contributor.departmentDepartment of Radiology
dc.contributor.departmentDepartment of Cell and Developmental Biology
dc.source.pagesE1991-E2000


Files in this item

Thumbnail
Name:
E1991.full.pdf
Size:
2.215Mb
Format:
PDF

This item appears in the following Collection(s)

Show simple item record