PUBLICATION

Loss of Smyhc1 or Hsp90alpha1 function results in different effects on myofibril organization in skeletal muscles of zebrafish embryos

Authors
Codina, M., Li, J., Gutiérrez, J., Kao, J.P., and Du, S.J.
ID
ZDB-PUB-100112-16
Date
2010
Source
PLoS One   5(1): e8416 (Journal)
Registered Authors
Du, Shao Jun (Jim)
Keywords
none
MeSH Terms
  • Animals
  • Gene Knockdown Techniques
  • Myosin Heavy Chains/genetics
  • Myosin Heavy Chains/physiology*
  • Zebrafish/embryology*
  • HSP90 Heat-Shock Proteins/genetics
  • HSP90 Heat-Shock Proteins/physiology*
  • Muscle, Skeletal/embryology*
  • Muscle, Skeletal/metabolism
(all 9)
PubMed
20049323 Full text @ PLoS One
Abstract
BACKGROUND: Myofibrillogenesis requires the correct folding and assembly of sarcomeric proteins into highly organized sarcomeres. Heat shock protein 90alpha1 (Hsp90alpha1) has been implicated as a myosin chaperone that plays a key role in myofibrillogenesis. Knockdown or mutation of hsp90alpha1 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 Hsp90alpha1 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 Hsp90alpha1 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 hsp90alpha1 mutant phenotype is not simply due to disruption of myosin folding and assembly, suggesting that Hsp90alpha1 may play a role in the assembly and organization of other sarcomeric structures.
Genes / Markers
Figures
Figure Gallery (8 images)
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Expression
Phenotype
Mutations / Transgenics
Allele Construct Type Affected Genomic Region
tu44c
    		Point Mutation
    1 - 1 of 1
    Show
    Human Disease / Model
    No data available
    Sequence Targeting Reagents
    Target Reagent Reagent Type
    smyhc1MO1-smyhc1MRPHLNO
    1 - 1 of 1
    Show
    Fish
    Fish
    hsp90aa1.1tu44c/tu44c
    WT
    WT + MO1-smyhc1
    1 - 3 of 3
    Show
    Antibodies
    Orthology
    No data available
    Engineered Foreign Genes
    No data available
    Mapping
    No data available
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    Citation
    Codina, M., Li, J., Gutiérrez, J., Kao, J.P., and Du, S.J. (2010) Loss of Smyhc1 or Hsp90alpha1 function results in different effects on myofibril organization in skeletal muscles of zebrafish embryos. PLoS One. 5(1):e8416.