The nebulin SH3 domain is dispensable for normal skeletal muscle structure but is required for effective active load bearing in mouse. (Articolo in rivista)

Type
Label
  • The nebulin SH3 domain is dispensable for normal skeletal muscle structure but is required for effective active load bearing in mouse. (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1242 (literal)
Alternative label
  • Daniel L. Yamamoto1,*, Carmen Vitiello2,*, Jianlin Zhang3, David S. Gokhin4, Alessandra Castaldi5,6, Gerald Coulis2, Fabio Piaser5,6, Maria Carmela Filomena6,7, Peter J. Eggenhuizen1, Paolo Kunderfranco5,6, Serena Camerini8, Kazunori Takano9, Takeshi Endo9, Marco Crescenzi8, Pradeep K. L. Luther10, Richard L. Lieber4, Ju Chen3,A? and Marie-Louise Bang5,6,A (2013)
    The nebulin SH3 domain is dispensable for normal skeletal muscle structure but is required for effective active load bearing in mouse.
    in Journal of cell science
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Daniel L. Yamamoto1,*, Carmen Vitiello2,*, Jianlin Zhang3, David S. Gokhin4, Alessandra Castaldi5,6, Gerald Coulis2, Fabio Piaser5,6, Maria Carmela Filomena6,7, Peter J. Eggenhuizen1, Paolo Kunderfranco5,6, Serena Camerini8, Kazunori Takano9, Takeshi Endo9, Marco Crescenzi8, Pradeep K. L. Luther10, Richard L. Lieber4, Ju Chen3,A? and Marie-Louise Bang5,6,A (literal)
Pagina inizio
  • 5477 (literal)
Pagina fine
  • 5489 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://www.ncbi.nlm.nih.gov/pubmed/24046450 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 126 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 12 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 23 (literal)
Note
  • PubMed (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • 1Institute of Biomedical Technologies, National Research Council, 20090 Milan, Italy 2IRCCS MultiMedica, 20138 Milan, Italy 3University of California San Diego, School of Medicine, La Jolla, CA 92093, USA 4Department of Bioengineering, University of California San Diego, La Jolla, CA 92093, USA 5Milan Unit, Institute of Genetic and Biomedical Research, National Research Council, 20089 Milan, Italy 6Humanitas Clinical and Research Center, Rozzano, 20089 Milan, Italy 7Department of Translational Medicine, University of Milan, 20089 Milan, Italy 8Department of Cell Biology and Neurosciences, National Institute of Health, Rome 00161, Italy 9Department of Biology, Graduate School of Science, Chiba University, Chiba 263-8522, Japan 10Faculty of Medicine, National Heart and Lung Institute, Imperial College London, London SW7 2AZ, UK *These authors contributed equally to this work A?Authors for correspondence (juchen@ucsd.edu; marie-louise.bang@cnr.it) (literal)
Titolo
  • The nebulin SH3 domain is dispensable for normal skeletal muscle structure but is required for effective active load bearing in mouse. (literal)
Abstract
  • Nemaline myopathy (NM) is a congenital myopathy with an estimated incidence of 150,000 live births. It is caused by mutations in thin filament components, including nebulin, which accounts for about 50% of the cases. The identification of NM cases with nonsense mutations resulting in loss of the extreme C-terminal SH3 domain of nebulin suggests an important role of the nebulin SH3 domain, which is further supported by the recent demonstration of its role in IGF-1-induced sarcomeric actin filament formation through targeting of N-WASP to the Z-line. To provide further insights into the functional significance of the nebulin SH3 domain in the Z-disk and to understand the mechanisms by which truncations of nebulin lead to NM, we took two approaches: (1) an affinity-based proteomic screening to identify novel interaction partners of the nebulin SH3 domain; and (2) generation and characterization of a novel knockin mouse model with a premature stop codon in the nebulin gene, eliminating its C-terminal SH3 domain (Neb?SH3 mouse). Surprisingly, detailed analyses of Neb?SH3 mice revealed no structural or histological skeletal muscle abnormalities and no changes in gene expression or localization of interaction partners of the nebulin SH3 domain, including myopalladin, palladin, zyxin and N-WASP. Also, no significant effect on peak isometric stress production, passive tensile stress or Young's modulus was found. However, Neb?SH3 muscle displayed a slightly altered force-frequency relationship and was significantly more susceptible to eccentric contraction-induced injury, suggesting that the nebulin SH3 domain protects against eccentric contraction-induced injury and possibly plays a role in fine-tuning the excitation-contraction coupling mechanism. KEYWORDS: (literal)
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Insieme di parole chiave di
data.CNR.it