Ehler, E. & Gautel, M. The sarcomere and sarcomerogenesis. Adv. Exp. Med. Biol.642, 1–14 (2008). CASPubMed Google Scholar
Lange, S., Ehler, E. & Gautel, M. From A to Z and back? Multicompartment proteins in the sarcomere. Trends Cell Biol.16, 11–18 (2006). CASPubMed Google Scholar
Pette, D. & Staron, R. S. Myosin isoforms, muscle fiber types, and transitions. Microsc. Res. Tech.50, 500–509 (2000). CASPubMed Google Scholar
Schiaffino, S. Fibre types in skeletal muscle: a personal account. Acta. Physiol. (Oxf.)199, 451–463 (2010). An authoritative review of skeletal muscle phenotypes and the molecular mechanisms controlling muscle fibre types. CAS Google Scholar
Zammit, P. S. All muscle satellite cells are equal, but are some more equal than others? J. Cell Sci.121, 2975–2982 (2008). CASPubMed Google Scholar
Ten Broek, R. W., Grefte, S. & Von den Hoff, J. W. Regulatory factors and cell populations involved in skeletal muscle regeneration. J. Cell. Physiol.224, 7–16 (2010). CASPubMed Google Scholar
Tedesco, F. S., Dellavalle, A., Diaz-Manera, J., Messina, G. & Cossu, G. Repairing skeletal muscle: regenerative potential of skeletal muscle stem cells. J. Clin. Invest.120, 11–19 (2010). A timely review on the role of satellite cells in muscle damage repair. CASPubMedPubMed Central Google Scholar
Bryson-Richardson, R. J. & Currie, P. D. The genetics of vertebrate myogenesis. Nature Rev. Genet.9, 632–646 (2008). A comprehensive review of the embryological processes leading to the formation of skeletal muscles. CASPubMed Google Scholar
Buckingham, M. Making muscle in mammals. Trends Genet.8, 144–149 (1992). CASPubMed Google Scholar
Berkes, C. A. & Tapscott, S. J. MyoD and the transcriptional control of myogenesis. Semin. Cell Dev. Biol.16, 585–595 (2005). CASPubMed Google Scholar
Kassar-Duchossoy, L. et al. Mrf4 determines skeletal muscle identity in Myf5:MyoD double-mutant mice. Nature431, 466–471 (2004). CASPubMed Google Scholar
Sato, T., Rocancourt, D., Marques, L., Thorsteinsdottir, S. & Buckingham, M. A Pax3/Dmrt2/Myf5 regulatory cascade functions at the onset of myogenesis. PLoS Genet.6, e1000897 (2010). PubMedPubMed Central Google Scholar
Tajbakhsh, S., Rocancourt, D., Cossu, G. & Buckingham, M. Redefining the genetic hierarchies controlling skeletal myogenesis: Pax-3 and Myf-5 act upstream of MyoD. Cell89, 127–138 (1997). CASPubMed Google Scholar
Brunelli, S., Relaix, F., Baesso, S., Buckingham, M. & Cossu, G. β-catenin-independent activation of MyoD in presomitic mesoderm requires PKC and depends on Pax3 transcriptional activity. Dev. Biol.304, 604–614 (2007). CASPubMed Google Scholar
Maroto, M. et al. Ectopic Pax-3 activates MyoD and Myf-5 expression in embryonic mesoderm and neural tissue. Cell89, 139–148 (1997). CASPubMed Google Scholar
Mennerich, D. & Braun, T. Activation of myogenesis by the homeobox gene Lbx1 requires cell proliferation. EMBO J.20, 7174–7183 (2001). CASPubMedPubMed Central Google Scholar
Mansouri, A., Stoykova, A., Torres, M. & Gruss, P. Dysgenesis of cephalic neural crest derivatives in _Pax_7-/- mutant mice. Development122, 831–838 (1996). CASPubMed Google Scholar
Relaix, F., Rocancourt, D., Mansouri, A. & Buckingham, M. A Pax3/Pax7-dependent population of skeletal muscle progenitor cells. Nature435, 948–953 (2005). This work defines the major populations of progenitor cells in muscle development. CASPubMed Google Scholar
Lagha, M. et al. Pax3 regulation of FGF signaling affects the progression of embryonic progenitor cells into the myogenic program. Genes Dev.22, 1828–1837 (2008). The role of PAX3 in the lineage commitment of myogenic progenitor cells in concert with other myogenic factors is described. CASPubMedPubMed Central Google Scholar
McKinnell, I. W. et al. Pax7 activates myogenic genes by recruitment of a histone methyltransferase complex. Nature Cell Biol.10, 77–84 (2008). CASPubMed Google Scholar
Daston, G., Lamar, E., Olivier, M. & Goulding, M. Pax-3 is necessary for migration but not differentiation of limb muscle precursors in the mouse. Development122, 1017–1027 (1996). CASPubMed Google Scholar
Bajard, L. et al. A novel genetic hierarchy functions during hypaxial myogenesis: Pax3 directly activates Myf5 in muscle progenitor cells in the limb. Genes Dev.20, 2450–2464 (2006). The direct activation ofMyf5by PAX3 in limb muscle cells is described. CASPubMedPubMed Central Google Scholar
Buchberger, A., Freitag, D. & Arnold, H. H. A homeo-paired domain-binding motif directs Myf5 expression in progenitor cells of limb muscle. Development134, 1171–1180 (2007). CASPubMed Google Scholar
Giordani, J. et al. Six proteins regulate the activation of Myf5 expression in embryonic mouse limbs. Proc. Natl Acad. Sci. USA104, 11310–11315 (2007). CASPubMedPubMed Central Google Scholar
Grifone, R. et al. Six1 and Eya1 expression can reprogram adult muscle from the slow-twitch phenotype into the fast-twitch phenotype. Mol. Cell. Biol.24, 6253–6267 (2004). CASPubMedPubMed Central Google Scholar
Laclef, C. et al. Altered myogenesis in _Six1_-deficient mice. Development130, 2239–2252 (2003). CASPubMed Google Scholar
Grifone, R. et al. Six1 and Six4 homeoproteins are required for Pax3 and Mrf expression during myogenesis in the mouse embryo. Development132, 2235–2249 (2005). CASPubMed Google Scholar
Grifone, R. et al. Eya1 and Eya2 proteins are required for hypaxial somitic myogenesis in the mouse embryo. Dev. Biol.302, 602–616 (2007). CASPubMed Google Scholar
Penn, B. H., Bergstrom, D. A., Dilworth, F. J., Bengal, E. & Tapscott, S. J. A MyoD-generated feed-forward circuit temporally patterns gene expression during skeletal muscle differentiation. Genes Dev.18, 2348–2353 (2004). CASPubMedPubMed Central Google Scholar
Molkentin, J. D., Black, B. L., Martin, J. F. & Olson, E. N. Cooperative activation of muscle gene expression by MEF2 and myogenic bHLH proteins. Cell83, 1125–1136 (1995). CASPubMed Google Scholar
Lu, J. R. et al. Control of facial muscle development by MyoR and capsulin. Science298, 2378–2381 (2002). One of the first papers to delineate the transcriptional network that drives head muscle development. CASPubMed Google Scholar
Dong, F. et al. Pitx2 promotes development of splanchnic mesoderm-derived branchiomeric muscle. Development133, 4891–4899 (2006). CASPubMed Google Scholar
Gage, P. J., Suh, H. & Camper, S. A. Dosage requirement of Pitx2 for development of multiple organs. Development126, 4643–4651 (1999). CASPubMed Google Scholar
Jerome, L. A. & Papaioannou, V. E. DiGeorge syndrome phenotype in mice mutant for the T-box gene, Tbx1. Nature Genet.27, 286–291 (2001). CASPubMed Google Scholar
Kelly, R. G., Jerome-Majewska, L. A. & Papaioannou, V. E. The del22q11.2 candidate gene Tbx1 regulates branchiomeric myogenesis. Hum. Mol. Genet.13, 2829–2840 (2004). CASPubMed Google Scholar
Sambasivan, R. et al. Distinct regulatory cascades govern extraocular and pharyngeal arch muscle progenitor cell fates. Dev. Cell16, 810–821 (2009). This paper addresses the distinct regulatory circuits that determine head muscle fates. CASPubMed Google Scholar
Ying, S. Y., Chang, D. C. & Lin, S. L. The microRNA (miRNA): overview of the RNA genes that modulate gene function. Mol. Biotechnol.38, 257–268 (2008). CASPubMed Google Scholar
Bushati, N. & Cohen, S. M. microRNA functions. Annu. Rev. Cell Dev. Biol.23, 175–205 (2007). CASPubMed Google Scholar
Chen, J. F. et al. The role of microRNA-1 and microRNA-133 in skeletal muscle proliferation and differentiation. Nature Genet.38, 228–233 (2006). CASPubMed Google Scholar
Rao, P. K., Kumar, R. M., Farkhondeh, M., Baskerville, S. & Lodish, H. F. Myogenic factors that regulate expression of muscle-specific microRNAs. Proc. Natl Acad. Sci. USA103, 8721–8726 (2006). CASPubMedPubMed Central Google Scholar
Sokol, N. S. & Ambros, V. Mesodermally expressed Drosophila microRNA-1 is regulated by Twist and is required in muscles during larval growth. Genes Dev.19, 2343–2354 (2005). CASPubMedPubMed Central Google Scholar
Zhao, Y., Samal, E. & Srivastava, D. Serum response factor regulates a muscle-specific microRNA that targets Hand2 during cardiogenesis. Nature436, 214–220 (2005). The identification of upstream regulators and downstream targets of muscle-specific miRNAs. CASPubMed Google Scholar
Liu, N. et al. An intragenic MEF2-dependent enhancer directs muscle-specific expression of microRNAs 1 and 133. Proc. Natl Acad. Sci. USA104, 20844–20849 (2007). CASPubMedPubMed Central Google Scholar
Sweetman, D. et al. Specific requirements of MRFs for the expression of muscle specific microRNAs, miR-1, miR-206 and miR-133. Dev. Biol.321, 491–499 (2009). Google Scholar
van Rooij, E. et al. Control of stress-dependent cardiac growth and gene expression by a microRNA. Science316, 575–579 (2007). CASPubMed Google Scholar
Boutz, P. L., Chawla, G., Stoilov, P. & Black, D. L. MicroRNAs regulate the expression of the alternative splicing factor nPTB during muscle development. Genes Dev.21, 71–84 (2007). The regulation of alternative splicing by miRNAs through control of a differential splicing factor. CASPubMedPubMed Central Google Scholar
Taulli, R. et al. The muscle-specific microRNA miR-206 blocks human rhabdomyosarcoma growth in xenotransplanted mice by promoting myogenic differentiation. J. Clin. Invest.119, 2366–2378 (2009). CASPubMedPubMed Central Google Scholar
Williams, A. H. et al. MicroRNA-206 delays ALS progression and promotes regeneration of neuromuscular synapses in mice. Science326, 1549–1554 (2009). CASPubMedPubMed Central Google Scholar
Crist, C. G. et al. Muscle stem cell behavior is modified by microRNA-27 regulation of Pax3 expression. Proc. Natl Acad. Sci. USA106, 13383–13387 (2009). CASPubMedPubMed Central Google Scholar
Hirai, H. et al. MyoD regulates apoptosis of myoblasts through microRNA-mediated down-regulation of Pax3. J. Cell Biol.191, 347–365 (2010). CASPubMedPubMed Central Google Scholar
Chen, J. F. et al. microRNA-1 and microRNA-206 regulate skeletal muscle satellite cell proliferation and differentiation by repressing Pax7. J. Cell Biol.190, 867–879 (2010). The discovery of the role of muscle-specific miRNAs in the control of satellite cells. CASPubMedPubMed Central Google Scholar
Dey, B. K., Gagan, J. & Dutta, A. miR-206 and -486 induce myoblast differentiation by downregulating Pax7. Mol. Cell. Biol.31, 203–214 (2011). CASPubMed Google Scholar
Zhao, Y. et al. Dysregulation of cardiogenesis, cardiac conduction, and cell cycle in mice lacking miRNA-1-2. Cell129, 303–317 (2007). CASPubMed Google Scholar
Lim, L. P. et al. Microarray analysis shows that some microRNAs downregulate large numbers of target mRNAs. Nature433, 769–773 (2005). A seminal paper demonstrating the regulation of multiple targets by miRNAs. CASPubMed Google Scholar
Kleinman, M. E. et al. Sequence- and target-independent angiogenesis suppression by siRNA via TLR3. Nature452, 591–597 (2008). CASPubMedPubMed Central Google Scholar
Krutzfeldt, J. et al. Specificity, duplex degradation and subcellular localization of antagomirs. Nucleic Acids Res.35, 2885–2892 (2007). CASPubMedPubMed Central Google Scholar
Bassel-Duby, R. & Olson, E. N. Signaling pathways in skeletal muscle remodeling. Annu. Rev. Biochem.75, 19–37 (2006). CASPubMed Google Scholar
Schiaffino, S., Sandri, M. & Murgia, M. Activity-dependent signaling pathways controlling muscle diversity and plasticity. Physiology (Bethesda)22, 269–278 (2007). CAS Google Scholar
Potthoff, M. J. et al. Histone deacetylase degradation and MEF2 activation promote the formation of slow-twitch myofibers. J. Clin. Invest.117, 2459–2467 (2007). The identification of regulatory circuits that are involved in slow-twitch muscle fibre formation. CASPubMedPubMed Central Google Scholar
Li, S. et al. Requirement for serum response factor for skeletal muscle growth and maturation revealed by tissue-specific gene deletion in mice. Proc. Natl Acad. Sci. USA102, 1082–1087 (2005). CASPubMedPubMed Central Google Scholar
Parlakian, A. et al. Targeted inactivation of serum response factor in the developing heart results in myocardial defects and embryonic lethality. Mol. Cell. Biol.24, 5281–5289 (2004). These two papers identify the essential role of SRF for postnatal muscle growth. CASPubMedPubMed Central Google Scholar
Raffaello, A. et al. JunB transcription factor maintains skeletal muscle mass and promotes hypertrophy. J. Cell Biol.191, 101–113 (2010). JUNB directly represses the activity of FOXO proteins and thus augments anti-atrophic transcriptional pathways. CASPubMedPubMed Central Google Scholar
Moresi, V. et al. Myogenin and class II HDACs control neurogenic muscle atrophy by inducing E3 ubiquitin ligases. Cell143, 35–45 (2010). Myogenin is redeployed in postnatal muscle under hierarchical control by HDACs to drive the expression of atrogenes. CASPubMedPubMed Central Google Scholar
Molkentin, J. D. Dichotomy of Ca2+ in the heart: contraction versus intracellular signaling. J. Clin. Invest.116, 623–626 (2006). CASPubMedPubMed Central Google Scholar
Niro, C. et al. Six1 and Six4 gene expression is necessary to activate the fast-type muscle gene program in the mouse primary myotome. Dev. Biol.338, 168–182 (2010). CASPubMed Google Scholar
Baxendale, S. et al. The B-cell maturation factor Blimp-1 specifies vertebrate slow-twitch muscle fiber identity in response to Hedgehog signaling. Nature Genet.36, 88–93 (2004). References 66 and 67 identify the major developmental programmes determining future slow- or fast-twitch muscle types. CASPubMed Google Scholar
Hagiwara, N., Yeh, M. & Liu, A. Sox6 is required for normal fiber type differentiation of fetal skeletal muscle in mice. Dev. Dyn.236, 2062–2076 (2007). CASPubMed Google Scholar
von Hofsten, J. et al. Prdm1- and Sox6-mediated transcriptional repression specifies muscle fibre type in the zebrafish embryo. EMBO Rep.9, 683–689 (2008). CASPubMedPubMed Central Google Scholar
Hinits, Y., Osborn, D. P. & Hughes, S. M. Differential requirements for myogenic regulatory factors distinguish medial and lateral somitic, cranial and fin muscle fibre populations. Development136, 403–414 (2009). CASPubMedPubMed Central Google Scholar
Kalhovde, J. M. et al. 'Fast' and 'slow' muscle fibres in hindlimb muscles of adult rats regenerate from intrinsically different satellite cells. J. Physiol.562, 847–857 (2005). CASPubMed Google Scholar
Perez-Ruiz, A., Gnocchi, V. F. & Zammit, P. S. Control of Myf5 activation in adult skeletal myonuclei requires ERK signalling. Cell Signal.19, 1671–1680 (2007). CASPubMed Google Scholar
Calabria, E. et al. NFAT isoforms control activity-dependent muscle fiber type specification. Proc. Natl Acad. Sci. USA106, 13335–13340 (2009). CASPubMedPubMed Central Google Scholar
Tothova, J. et al. NFATc1 nucleocytoplasmic shuttling is controlled by nerve activity in skeletal muscle. J. Cell Sci.119, 1604–1611 (2006). Distinct neuronal activity patterns modulate cytoplasmic Ca2+levels, and thus the activity of the transcription factor NFATC1 by modulating the activity of its activator, calcineurin. CASPubMed Google Scholar
Frey, N. et al. Mice lacking calsarcin-1 are sensitized to calcineurin signaling and show accelerated cardiomyopathy in response to pathological biomechanical stress. Nature Med.10, 1336–1343 (2004). CASPubMed Google Scholar
Hoshijima, M. Mechanical stress-strain sensors embedded in cardiac cytoskeleton: Z disk, titin, and associated structures. Am. J. Physiol. Heart Circ. Physiol.290, H1313–H1325 (2006). CASPubMed Google Scholar
Zammit, P. S., Partridge, T. A. & Yablonka-Reuveni, Z. The skeletal muscle satellite cell: the stem cell that came in from the cold. J. Histochem. Cytochem.54, 1177–1191 (2006). CASPubMed Google Scholar
Sacco, A., Doyonnas, R., Kraft, P., Vitorovic, S. & Blau, H. M. Self-renewal and expansion of single transplanted muscle stem cells. Nature456, 502–506 (2008). CASPubMedPubMed Central Google Scholar
Blaauw, B. et al. Inducible activation of Akt increases skeletal muscle mass and force without satellite cell activation. FASEB J.23, 3896–3905 (2009). CASPubMed Google Scholar
Sandri, M. et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell117, 399–412 (2004). CASPubMedPubMed Central Google Scholar
Stitt, T. N. et al. The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol. Cell.14, 395–403 (2004). FOXO proteins are identified as the major transcription factors regulating the expression of MURF atrogenes in atrophy. CASPubMed Google Scholar
Sandri, M. Signaling in muscle atrophy and hypertrophy. Physiology (Bethesda)23, 160–170 (2008). A comprehensive review of the mechanisms regulating muscle protein turnover and metabolism. CAS Google Scholar
Willis, M. S., Schisler, J. C., Portbury, A. L. & Patterson, C. Build it up – tear it down: protein quality control in the cardiac sarcomere. Cardiovasc. Res.81, 439–448 (2009). CASPubMed Google Scholar
Mammucari, C. et al. FoxO3 controls autophagy in skeletal muscle in vivo. Cell Metab.6, 458–471 (2007). CASPubMed Google Scholar
Zhao, J. et al. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab.6, 472–483 (2007). References 84 and 85 identify a crucial pathway that controls muscle mass and homeostatic regulation through the transcription of autophagy and lysosomal proteins under the control of FOXO proteins. CASPubMed Google Scholar
Li, H. H. et al. Atrogin-1/muscle atrophy F-box inhibits calcineurin-dependent cardiac hypertrophy by participating in an SCF ubiquitin ligase complex. J. Clin. Invest.114, 1058–1071 (2004). CASPubMedPubMed Central Google Scholar
Li, H. H. et al. Atrogin-1 inhibits Akt-dependent cardiac hypertrophy in mice via ubiquitin-dependent coactivation of forkhead proteins. J. Clin. Invest.117, 3211–3223 (2007). CASPubMedPubMed Central Google Scholar
Masiero, E. et al. Autophagy is required to maintain muscle mass. Cell Metab.10, 507–515 (2009). Autophagy is required for the homeostasis of muscle mass and is not per se detrimental, as its inhibition is shown here to lead to a paradoxical loss of muscle mass. CASPubMed Google Scholar
Mourkioti, F. & Rosenthal, N. NF-κB signaling in skeletal muscle: prospects for intervention in muscle diseases. J. Mol. Med.86, 747–759 (2008). CASPubMed Google Scholar
Mourkioti, F. et al. Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration. J. Clin. Invest.116, 2945–2954 (2006). Transcription of MURF atrogenes is controlled by NF-κB activity. CASPubMedPubMed Central Google Scholar
Macpherson, P. C., Wang, X. & Goldman, D. Myogenin regulates denervation-dependent muscle atrophy in mouse soleus muscle. J. Cell. Biochem. 4 Apr 2011 (10.1002/jcb.23136).
Small, E. M. et al. Regulation of PI3-kinase/Akt signaling by muscle-enriched microRNA-486. Proc. Natl Acad. Sci. USA107, 4218–4223 (2010). miR-486 is transcriptionally controlled by SRF and negatively regulates FOXO protein expression, providing an amplifying feedback loop in hypertrophying muscle. CASPubMedPubMed Central Google Scholar
Elia, L. et al. Reciprocal regulation of microRNA-1 and insulin-like growth factor-1 signal transduction cascade in cardiac and skeletal muscle in physiological and pathological conditions. Circulation120, 2377–2385 (2009). CASPubMedPubMed Central Google Scholar
Gautel, M. The sarcomeric cytoskeleton: who picks up the strain? Curr. Opin. Cell Biol.23, 39–46 (2011). CASPubMed Google Scholar
Kruger, M. & Linke, W. A. The giant protein titin: a regulatory node that integrates myocyte signaling pathways. J. Biol. Chem. 21 Jan 2011 (10.1074/jbc.R110.173260).
Boateng, S. Y., Senyo, S. E., Qi, L., Goldspink, P. H. & Russell, B. Myocyte remodelling in response to hypertrophic stimuli requires nucleocytoplasmic shuttling of muscle LIM protein. J. Mol. Cell. Cardiol.47, 426–435 (2009). CASPubMedPubMed Central Google Scholar
Geier, C. et al. Beyond the sarcomere: CSRP3 mutations cause hypertrophic cardiomyopathy. Hum. Mol. Genet.17, 2753–2765 (2008). CASPubMed Google Scholar
Knoll, R. et al. The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy. Cell111, 943–955 (2002). CASPubMed Google Scholar
Qi, L. & Boateng, S. Y. The circadian protein Clock localizes to the sarcomeric Z-disk and is a sensor of myofilament cross-bridge activity in cardiac myocytes. Biochem. Biophys. Res. Commun.351, 1054–1059 (2006). CASPubMedPubMed Central Google Scholar
Andrews, J. L. et al. CLOCK and BMAL1 regulate MyoD and are necessary for maintenance of skeletal muscle phenotype and function. Proc. Natl Acad. Sci. USA107, 19090–19095 (2010). Circadian rhythm, mechanical activity and myogenic transcription regulation are linked in references 99 and 100. CASPubMedPubMed Central Google Scholar
Meder, B. et al. JunB-CBFβ signaling is essential to maintain sarcomeric Z-disc structure and when defective leads to heart failure. J. Cell Sci.123, 2613–2620 (2010). CASPubMed Google Scholar
Hayashi, C. et al. Multiple molecular interactions implicate the connectin/titin N2A region as a modulating scaffold for p94/calpain 3 activity in skeletal muscle. J. Biol. Chem.283, 14801–14814 (2008). CASPubMed Google Scholar
Tsukamoto, Y. et al. Arpp/Ankrd2, a member of the muscle ankyrin repeat proteins (MARPs), translocates from the I-band to the nucleus after muscle injury. Histochem. Cell Biol.129, 55–64 (2008). CASPubMed Google Scholar
Kojic, S. et al. The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle. J. Mol. Biol.339, 313–325 (2004). CASPubMed Google Scholar
Lange, S. et al. The kinase domain of titin controls muscle gene expression and protein turnover. Science308, 1599–1603 (2005). A mechanically modulated pathway acting through the giant protein kinase titin regulates the activity of the atrogenes MURF, SQSTM1 and NBR1, with MURF2 acting as a repressor of SRF activity. Disruption of this titin link leads to human myopathy. CASPubMed Google Scholar
Ochala, J. et al. Preferential skeletal muscle myosin loss in response to mechanical silencing in a novel rat intensive care unit model: underlying mechanisms. J. Physiol.589, 2007–2026 (2011). CASPubMedPubMed Central Google Scholar
Willis, M. S. et al. Muscle ring finger 1, but not muscle ring finger 2, regulates cardiac hypertrophy in vivo. Circ. Res.100, 456–459 (2007). CASPubMedPubMed Central Google Scholar
Spencer, J. A., Eliazer, S., Ilaria, R. L. Jr, Richardson, J. A. & Olson, E. N. Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein. J. Cell Biol.150, 771–784 (2000). Identification of the E3 ubiquitin ligase MURF3 and its dual roles in muscle development and protein degradation, and linkage of these roles to the transcriptional control of SRF. CASPubMedPubMed Central Google Scholar
Gautel, M. The sarcomere and the nucleus: functional links to hypertrophy, atrophy and sarcopenia. Adv. Med. Biol. Exp.642, 176–191 (2008). CAS Google Scholar
Komatsu, M. et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell131, 1149–1163 (2007). CASPubMed Google Scholar
Pankiv, S. et al. p62/SQSTM1 binds directly to atg8/lc3 to facilitate degradation of ubiquitinated protein aggregates by autophagy. J. Biol. Chem.282, 24131–24145 (2007). CASPubMed Google Scholar
Waters, S., Marchbank, K., Solomon, E., Whitehouse, C. & Gautel, M. Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic protein turnover. FEBS Lett.583, 1846–1852 (2009). CASPubMed Google Scholar
Kirkin, V. et al. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol. Cell33, 505–516 (2009). CASPubMed Google Scholar
Moscat, J., Diaz-Meco, M. T. & Wooten, M. W. Signal integration and diversification through the p62 scaffold protein. Trends Biochem. Sci.32, 95–100 (2007). CASPubMed Google Scholar
Gautel, M. Cytoskeletal protein kinases: titin and its relations in strain sensing. Pflugers Arch. 18 Mar 2011 (10.1007/s00424-011-0946–0941).
Adams, V. et al. Induction of MuRF1 is essential for TNF-α-induced loss of muscle function in mice. J. Mol. Biol.384, 48–59 (2008). CASPubMed Google Scholar
Tisdale, M. J. Mechanisms of cancer cachexia. Physiol. Rev.89, 381–410 (2009). CASPubMed Google Scholar
Goldspink, G. Changes in muscle mass and phenotype and the expression of autocrine and systemic growth factors by muscle in response to stretch and overload. J. Anat.194, 323–334 (1999). CASPubMedPubMed Central Google Scholar
Vinciguerra, M., Musaro, A. & Rosenthal, N. Regulation of muscle atrophy in aging and disease. Adv. Exp. Med. Biol.694, 211–233 (2010). CASPubMed Google Scholar
Matsakas, A. & Patel, K. Intracellular signalling pathways regulating the adaptation of skeletal muscle to exercise and nutritional changes. Histol. Histopathol.24, 209–222 (2009). CASPubMed Google Scholar
Trendelenburg, A. U. et al. Myostatin reduces AKT/TORC1/p70S6K signaling, inhibiting myoblast differentiation and myotube size. Am. J. Physiol. Cell Physiol.296, C1258–C1270 (2009). CASPubMed Google Scholar
Sartori, R. et al. Smad2 and 3 transcription factors control muscle mass in adulthood. Am. J. Physiol. Cell Physiol.296, C1248–C1257 (2009). CASPubMed Google Scholar
Morissette, M. R., Cook, S. A., Buranasombati, C., Rosenberg, M. A. & Rosenzweig, A. Myostatin inhibits IGF-I-induced myotube hypertrophy through Akt. Am. J. Physiol. Cell Physiol.297, C1124–C1132 (2009). CASPubMed Google Scholar
George, I. et al. Myostatin activation in patients with advanced heart failure and after mechanical unloading. Eur. J. Heart Fail.12, 444–453 (2010). CASPubMedPubMed Central Google Scholar
Heineke, J. et al. Genetic deletion of myostatin from the heart prevents skeletal muscle atrophy in heart failure. Circulation121, 419–425 (2010). The secretion of myostatin by failing hearts is a major factor in heart failure-associated muscle loss. CASPubMedPubMed Central Google Scholar
Sainz, N. et al. Leptin administration favors muscle mass accretion by decreasing FoxO3a and increasing PGC-1α in ob/ob mice. PLoS ONE4, e6808 (2009). PubMedPubMed Central Google Scholar
Chambon, C. et al. Myocytic androgen receptor controls the strength but not the mass of limb muscles. Proc. Natl Acad. Sci. USA107, 14327–14332 (2010). CASPubMedPubMed Central Google Scholar
Shimizu, N. et al. Crosstalk between glucocorticoid receptor and nutritional sensor mTOR in skeletal muscle. Cell Metab.13, 170–182 (2011). AR, a well-known hypertrophic factor, augments in feedback loops the anabolic signals of the IGF1–AKT pathway. CASPubMed Google Scholar
Eddins, M. J. et al. Targeting the ubiquitin E3 ligase MuRF1 to inhibit muscle atrophy. Cell Biochem. Biophys. 30 Mar 2011 (10.1007/s12013-011-9175–9177). Small-molecule inhibitors of the atrogene MURF1 ubiquitin ligase are active in cells and suggest that atrogene inhibition might be a viable route to therapies for muscle loss.
Perera, S., Holt, M. R., Mankoo, B. S. & Gautel, M. Developmental regulation of MURF ubiquitin ligases and autophagy proteins nbr1, p62/SQSTM1 and LC3 during cardiac myofibril assembly and turnover. Dev. Biol.351, 46–61 (2011). The atrogenes MURF1, MURF2 and MURF3 show tight developmental regulation and are expressed in developing muscle, suggesting that their main function is not simply control of muscle mass loss. CASPubMedPubMed Central Google Scholar
Chen, S. N. et al. TRIM63, encoding MuRF1, is a novel gene for familial hypertrophic cardiomyopathy. Circulation122 (Suppl.), A21194 (2010). Google Scholar
Kalcheim, C. & Ben-Yair, R. Cell rearrangements during development of the somite and its derivatives. Curr. Opin. Genet. Dev.15, 371–380 (2005). CASPubMed Google Scholar
Gros, J., Scaal, M. & Marcelle, C. A two-step mechanism for myotome formation in chick. Dev. Cell6, 875–882 (2004). CASPubMed Google Scholar
Tzahor, E. Heart and craniofacial muscle development: a new developmental theme of distinct myogenic fields. Dev. Biol.327, 273–279 (2009). CASPubMed Google Scholar
Noden, D. M. The role of the neural crest in patterning of avian cranial skeletal, connective, and muscle tissues. Dev. Biol.96, 144–165 (1983). CASPubMed Google Scholar
Rinon, A. et al. Cranial neural crest cells regulate head muscle patterning and differentiation during vertebrate embryogenesis. Development134, 3065–3075 (2007). CASPubMed Google Scholar
Grenier, J., Teillet, M. A., Grifone, R., Kelly, R. G. & Duprez, D. Relationship between neural crest cells and cranial mesoderm during head muscle development. PLoS ONE4, e4381 (2009). PubMedPubMed Central Google Scholar
Borycki, A. G. & Emerson, C. P., Jr. Multiple tissue interactions and signal transduction pathways control somite myogenesis. Curr. Top. Dev. Biol.48, 165–224 (2000). CASPubMed Google Scholar
Reshef, R., Maroto, M. & Lassar, A. B. Regulation of dorsal somitic cell fates: BMPs and Noggin control the timing and pattern of myogenic regulator expression. Genes Dev.12, 290–303 (1998). CASPubMedPubMed Central Google Scholar
Borello, U. et al. The Wnt/β-catenin pathway regulates Gli-mediated Myf5 expression during somitogenesis. Development133, 3723–3732 (2006). CASPubMed Google Scholar
Chen, A. E., Ginty, D. D. & Fan, C. M. Protein kinase A signalling via CREB controls myogenesis induced by Wnt proteins. Nature433, 317–322 (2005). CASPubMed Google Scholar
Sanger, J. W., Wang, J., Fan, Y., White, J. & Sanger, J. M. Assembly and dynamics of myofibrils. J. Biomed. Biotechnol.2010, 858606 (2010). PubMedPubMed Central Google Scholar
Linke, W. A. & Kruger, M. The giant protein titin as an integrator of myocyte signaling pathways. Physiology (Bethesda)25, 186–198 (2010). CAS Google Scholar
Kontrogianni-Konstantopoulos, A., Ackermann, M. A., Bowman, A. L., Yap, S. V. & Bloch, R. J. Muscle giants: molecular scaffolds in sarcomerogenesis. Physiol. Rev.89, 1217–1267 (2009). CASPubMed Google Scholar
Hinits, Y. & Hughes, S. M. Mef2s are required for thick filament formation in nascent muscle fibres. Development134, 2511–2519 (2007). CASPubMed Google Scholar
Potthoff, M. J. et al. Regulation of skeletal muscle sarcomere integrity and postnatal muscle function by Mef2c. Mol. Cell Biol.27, 8143–8151 (2007). References 146 and 147 identify MEF2C as the main transcription factor that directs the formation of mature sarcomeres by driving the expression of myosin and myomesin. CASPubMedPubMed Central Google Scholar
Niu, Z. et al. Serum response factor orchestrates nascent sarcomerogenesis and silences the biomineralization gene program in the heart. Proc. Natl Acad. Sci. USA105, 17824–17829 (2008). CASPubMedPubMed Central Google Scholar
Niu, Z., Li, A., Zhang, S. X. & Schwartz, R. J. Serum response factor micromanaging cardiogenesis. Curr. Opin. Cell Biol.19, 618–627 (2007). CASPubMedPubMed Central Google Scholar
Rios, A. C., & Marcelle C. Head muscles: aliens who came in from the cold? Dev. Cell16, 779–780 (2009). CASPubMed Google Scholar