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DC Field | Value | Language |
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dc.contributor.author | Codina, Marta | - |
dc.contributor.author | Gutiérrez Fruitós, Joaquín | - |
dc.contributor.author | Kao, Joseph P. Y. | - |
dc.contributor.author | Du, Shao Jun | - |
dc.contributor.author | Li, Junling | - |
dc.date.accessioned | 2018-10-01T17:53:59Z | - |
dc.date.available | 2018-10-01T17:53:59Z | - |
dc.date.issued | 2010-01-01 | - |
dc.identifier.issn | 1932-6203 | - |
dc.identifier.uri | http://hdl.handle.net/2445/124984 | - |
dc.description.abstract | Background Myofibrillogenesis requires the correct folding and assembly of sarcomeric proteins into highly organized sarcomeres. Heat shock protein 90α1 (Hsp90α1) has been implicated as a myosin chaperone that plays a key role in myofibrillogenesis. Knockdown or mutation of hsp90α1 resulted in complete disorganization of thick and thin filaments and M- and Z-line structures. It is not clear whether the disorganization of these sarcomeric structures is due to a direct effect from loss of Hsp90α1 function or indirectly through the disorganization of myosin thick filaments. Methodology/Principal Findings In this study, we carried out a loss-of-function analysis of myosin thick filaments via gene-specific knockdown or using a myosin ATPase inhibitor BTS (N-benzyl-p-toluene sulphonamide) in zebrafish embryos. We demonstrated that knockdown of myosin heavy chain 1 (myhc1) resulted in sarcomeric defects in the thick and thin filaments and defective alignment of Z-lines. Similarly, treating zebrafish embryos with BTS disrupted thick and thin filament organization, with little effect on the M- and Z-lines. In contrast, loss of Hsp90α1 function completely disrupted all sarcomeric structures including both thick and thin filaments as well as the M- and Z-lines. Conclusion/Significance Together, these studies indicate that the hsp90α1 mutant phenotype is not simply due to disruption of myosin folding and assembly, suggesting that Hsp90α1 may play a role in the assembly and organization of other sarcomeric structures. | - |
dc.format.extent | 9 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Public Library of Science (PLoS) | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1371/journal.pone.0008416 | - |
dc.relation.ispartof | PLoS One, 2010, vol. 5, num. 1, p. 1-9 | - |
dc.relation.uri | https://doi.org/10.1371/journal.pone.0008416 | - |
dc.rights | cc-by (c) Codina, M. et al., 2010 | - |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es | - |
dc.source | Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia) | - |
dc.subject.classification | Peix zebra | - |
dc.subject.classification | Contracció muscular | - |
dc.subject.classification | Proteïnes | - |
dc.subject.other | Zebra danio | - |
dc.subject.other | Muscle contraction | - |
dc.subject.other | Proteins | - |
dc.title | Loss of Symhc1 or Hsp90, function results in different effects on myofibril organization in skeletal muscles of zebrafish embryos | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 573098 | - |
dc.date.updated | 2018-10-01T17:53:59Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
Appears in Collections: | Articles publicats en revistes (Biologia Cel·lular, Fisiologia i Immunologia) |
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573098.pdf | 1.11 MB | Adobe PDF | View/Open |
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