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dc.contributor.authorYang, Shixin
dc.contributor.authorLee, Kyounghwan
dc.contributor.authorWoodhead, John L.
dc.contributor.authorSato, Osamu
dc.contributor.authorIkebe, Mitsuo
dc.contributor.authorCraig, Roger
dc.date2022-08-11T08:10:48.000
dc.date.accessioned2022-08-23T17:20:49Z
dc.date.available2022-08-23T17:20:49Z
dc.date.issued2019-09-02
dc.date.submitted2019-09-25
dc.identifier.citation<p>J Gen Physiol. 2019 Sep 2;151(9):1081-1093. doi: 10.1085/jgp.201912431. Epub 2019 Aug 6. <a href="https://doi.org/10.1085/jgp.201912431">Link to article on publisher's site</a></p>
dc.identifier.issn0022-1295 (Linking)
dc.identifier.doi10.1085/jgp.201912431
dc.identifier.pmid31387899
dc.identifier.urihttp://hdl.handle.net/20.500.14038/48386
dc.description.abstractMyosin II is a motor protein with two heads and an extended tail that plays an essential role in cell motility. Its active form is a polymer (myosin filament) that pulls on actin to generate motion. Its inactive form is a monomer with a compact structure (10S sedimentation coefficient), in which the tail is folded and the two heads interact with each other, inhibiting activity. This conformation is thought to function in cells as an energy-conserving form of the molecule suitable for storage as well as transport to sites of filament assembly. The mechanism of inhibition of the compact molecule is not fully understood. We have performed a 3-D reconstruction of negatively stained 10S myosin from smooth muscle in the inhibited state using single-particle analysis. The reconstruction reveals multiple interactions between the tail and the two heads that appear to trap ATP hydrolysis products, block actin binding, hinder head phosphorylation, and prevent filament formation. Blocking these essential features of myosin function could explain the high degree of inhibition of the folded form of myosin thought to underlie its energy-conserving function in cells. The reconstruction also suggests a mechanism for unfolding when myosin is activated by phosphorylation.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=31387899&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rights© 2019 Yang et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/
dc.subjectMyosin II
dc.subjectmotor proteins
dc.subjectphysiology
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectBiochemistry
dc.subjectCell Biology
dc.subjectCells
dc.subjectCellular and Molecular Physiology
dc.subjectEnzymes and Coenzymes
dc.subjectMolecular Biology
dc.subjectStructural Biology
dc.titleThe central role of the tail in switching off 10S myosin II activity
dc.typeJournal Article
dc.source.journaltitleThe Journal of general physiology
dc.source.volume151
dc.source.issue9
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=1507&amp;context=radiology_pubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/radiology_pubs/497
dc.identifier.contextkey15425130
refterms.dateFOA2022-08-23T17:20:49Z
html.description.abstract<p>Myosin II is a motor protein with two heads and an extended tail that plays an essential role in cell motility. Its active form is a polymer (myosin filament) that pulls on actin to generate motion. Its inactive form is a monomer with a compact structure (10S sedimentation coefficient), in which the tail is folded and the two heads interact with each other, inhibiting activity. This conformation is thought to function in cells as an energy-conserving form of the molecule suitable for storage as well as transport to sites of filament assembly. The mechanism of inhibition of the compact molecule is not fully understood. We have performed a 3-D reconstruction of negatively stained 10S myosin from smooth muscle in the inhibited state using single-particle analysis. The reconstruction reveals multiple interactions between the tail and the two heads that appear to trap ATP hydrolysis products, block actin binding, hinder head phosphorylation, and prevent filament formation. Blocking these essential features of myosin function could explain the high degree of inhibition of the folded form of myosin thought to underlie its energy-conserving function in cells. The reconstruction also suggests a mechanism for unfolding when myosin is activated by phosphorylation.</p>
dc.identifier.submissionpathradiology_pubs/497
dc.contributor.departmentCraig Lab
dc.contributor.departmentDivision of Cell Biology and Imaging, Department of Radiology
dc.source.pages1081-1093


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© 2019 Yang et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
Except where otherwise noted, this item's license is described as © 2019 Yang et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).