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DC Field | Value | Language |
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dc.contributor.author | Pernigo, S | - |
dc.contributor.author | Fukuzawa, A | - |
dc.contributor.author | Beedle, AEM | - |
dc.contributor.author | Holt, M | - |
dc.contributor.author | Round, A | - |
dc.contributor.author | Pandini, A | - |
dc.contributor.author | Garcia-Manyes, S | - |
dc.contributor.author | Gautel, M | - |
dc.contributor.author | Steiner, RA | - |
dc.date.accessioned | 2016-12-19T11:57:54Z | - |
dc.date.available | 2016-12-19T11:57:54Z | - |
dc.date.issued | 2016-12-15 | - |
dc.identifier | ORCiD: Alessandro Pandini https://orcid.org/0000-0002-4158-233X | - |
dc.identifier.citation | Pernigo, S. et al. (2017) 'Binding of myomesin to obscurin-like-1 to the muscle M-band provides a strategy for isoform-specific mechanical protection', Structure, 25 (1): pp. 107 - 120. doi: 10.1016/j.str.2016.11.015. | en_US |
dc.identifier.issn | 0969-2126 | - |
dc.identifier.uri | https://bura.brunel.ac.uk/handle/2438/13690 | - |
dc.description | Supplemental Information is available online at: https://www.sciencedirect.com/science/article/pii/S0969212616303574#app3 | - |
dc.description.abstract | The sarcomeric cytoskeleton is a network of modular proteins that integrate mechanical and signaling roles. Obscurin, or its homolog obscurin-like-1, bridges the giant ruler titin and the myosin crosslinker myomesin at the M-band. Yet, the molecular mechanisms underlying the physical obscurin(-like-1):myomesin connection, important for mechanical integrity of the M-band, remained elusive. Here, using a combination of structural, cellular, and single-molecule force spectroscopy techniques, we decode the architectural and functional determinants defining the obscurin(-like-1):myomesin complex. The crystal structure reveals a trans-complementation mechanism whereby an incomplete immunoglobulin-like domain assimilates an isoform-specific myomesin interdomain sequence. Crucially, this unconventional architecture provides mechanical stability up to forces of ∼135 pN. A cellular competition assay in neonatal rat cardiomyocytes validates the complex and provides the rationale for the isoform specificity of the interaction. Altogether, our results reveal a novel binding strategy in sarcomere assembly, which might have implications on muscle nanomechanics and overall M-band organization. | en_US |
dc.description.sponsorship | This work was supported by a British Heart Foundation grant (PG/10/67/28527) awarded to R.A.S. and M.G. as well as MRC grant MR/J010456/1 to M.G. and a British Heart Foundation grant (PG/13/50/30426) and EPSRC Fellowship (K00641X/1) to S.G.-M. | en_US |
dc.format.extent | 107 - 120 | - |
dc.format.medium | Print-Electronic | - |
dc.language.iso | en | en_US |
dc.publisher | Elsevier | en_US |
dc.rights | Copyright © 2016 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY license (https://creativecommons.org/licenses/by/4.0/). | - |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | - |
dc.subject | muscle | en_US |
dc.subject | M-band | en_US |
dc.subject | myomesin | en_US |
dc.subject | obscurin | en_US |
dc.subject | obscurin-like-1 | en_US |
dc.subject | protein complexes | en_US |
dc.subject | x-ray crystallography | en_US |
dc.subject | SAXS | en_US |
dc.subject | atomic force microscopy | en_US |
dc.subject | immunoglobulin domain | en_US |
dc.title | Binding of myomesin to obscurin-like-1 to the muscle M-band provides a strategy for isoform-specific mechanical protection | en_US |
dc.type | Article | en_US |
dc.identifier.doi | https://doi.org/10.1016/j.str.2016.11.015 | - |
dc.relation.isPartOf | Structure | - |
pubs.issue | 1 | - |
pubs.publication-status | Published | - |
pubs.volume | 25 | - |
dc.identifier.eissn | 1878-4186 | - |
dc.rights.license | https://creativecommons.org/licenses/by/4.0/legalcode.en | - |
dc.rights.holder | The Author(s) | - |
Appears in Collections: | Dept of Computer Science Research Papers |
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FullText.pdf | Copyright © 2016 The Author(s). Published by Elsevier Ltd. This is an open access article under the CC BY license (https://creativecommons.org/licenses/by/4.0/). | 13.45 MB | Adobe PDF | View/Open |
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