Talk:Musculoskeletal System - Muscle Development: Difference between revisions
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==Phenotypes induced by NM causing α-skeletal muscle actin mutants in fibroblasts, Sol 8 myoblasts and myotubes== | ==Phenotypes induced by NM causing α-skeletal muscle actin mutants in fibroblasts, Sol 8 myoblasts and myotubes== | ||
http://www.biomedcentral.com/1756-0500/2/40/ | http://www.biomedcentral.com/1756-0500/2/40/ | ||
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1904199 | |||
==Kindlin-2 is required for myocyte elongation and is essential for myogenesis== | |||
http://www.biomedcentral.com/1471-2121/9/36 | |||
Integrins are required for normal muscle differentiation and disruptions in integrin signaling result in human muscle disease. The intracellular components that regulate integrin function during myogenesis are poorly understood. Unc-112 is an integrin-associated protein required for muscle development in C. elegans. To better understand the intracellular effectors of integrin signaling in muscle, we examined the mammalian homolog of Unc-112, kindlin-2. | |||
Schematic of kindlin-2 function during early myogenesis. A. Undifferentiated C2C12 cells with typical fibroblast-like morphology B. Upon change to differentiation media, control cells withdraw from the cell cycle and elongate. In cells with reduced levels of kindlin-2, cells fail to elongate, and instead maintain a "pro-migratory" phenotype. C. By differentiation day 4, elongated control cells fuse into multinucleated myotubes. Reduced levels of kindlin-2 result in failure of myotube formation, likely as a result of decreased elongation, inadequate cell adhesion and impaired myoblast fusion. One mechanism underlying these alterations is a failure of redistribution of ILK containing focal adhesions. | |||
==PITX2 gain-of-function induced defects in mouse forelimb development== | |||
http://www.biomedcentral.com/1471-213X/8/25 | |||
Revision as of 07:54, 28 September 2010
centrosome proteins - muscle cell differentiation
- Centrosome proteins form an insoluble perinuclear matrix during muscle cell differentiation. Srsen V, Fant X, Heald R, Rabouille C, Merdes A. BMC Cell Biol. 2009 Apr 21;10:28. PMID: 19383121 | BMC Cell Biol.
- Nuclei of non-muscle cells bind centrosome proteins upon fusion with differentiating myoblasts. Fant X, Srsen V, Espigat-Georger A, Merdes A. PLoS One. 2009 Dec 14;4(12):e8303. PMID: 20011525
- Reorganization of microtubule nucleation during muscle differentiation. Bugnard E, Zaal KJ, Ralston E. Cell Motil Cytoskeleton. 2005 Jan;60(1):1-13.PMID: 15532031
Skeletal Dysplasias Associated with Mild Myopathy—A Clinical and Molecular Review
Good figures for bone
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2875749/?tool=pubmed
Phenotypes induced by NM causing α-skeletal muscle actin mutants in fibroblasts, Sol 8 myoblasts and myotubes
http://www.biomedcentral.com/1756-0500/2/40/
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1904199
Kindlin-2 is required for myocyte elongation and is essential for myogenesis
http://www.biomedcentral.com/1471-2121/9/36
Integrins are required for normal muscle differentiation and disruptions in integrin signaling result in human muscle disease. The intracellular components that regulate integrin function during myogenesis are poorly understood. Unc-112 is an integrin-associated protein required for muscle development in C. elegans. To better understand the intracellular effectors of integrin signaling in muscle, we examined the mammalian homolog of Unc-112, kindlin-2.
Schematic of kindlin-2 function during early myogenesis. A. Undifferentiated C2C12 cells with typical fibroblast-like morphology B. Upon change to differentiation media, control cells withdraw from the cell cycle and elongate. In cells with reduced levels of kindlin-2, cells fail to elongate, and instead maintain a "pro-migratory" phenotype. C. By differentiation day 4, elongated control cells fuse into multinucleated myotubes. Reduced levels of kindlin-2 result in failure of myotube formation, likely as a result of decreased elongation, inadequate cell adhesion and impaired myoblast fusion. One mechanism underlying these alterations is a failure of redistribution of ILK containing focal adhesions.
