P38-γ–dependent gene silencing restricts entry into the myogenic differentiation program
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The mitogen-activated protein kinase p38-gamma is highly expressed in skeletal muscle and is associated with the dystrophin glycoprotein complex; however, its function remains unclear. After induced damage, muscle in mice lacking p38-gamma generated significantly fewer myofibers than wild-type muscle. Notably, p38-gamma-deficient muscle contained 50% fewer satellite cells that exhibited premature Myogenin expression and markedly reduced proliferation. We determined that p38-gamma directly phosphorylated MyoD on Ser199 and Ser200, which results in enhanced occupancy of MyoD on the promoter of myogenin together with markedly decreased transcriptional activity. This repression is associated with extensive methylation of histone H3K9 together with recruitment of the KMT1A methyltransferase to the myogenin promoter. Notably, a MyoD S199A/S200A mutant exhibits markedly reduced binding to KMT1A. Therefore, p38-gamma signaling directly induces the assembly of a repressive MyoD transcriptional complex. Together, these results establish a hitherto unappreciated and essential role for p38-gamma signaling in positively regulating the expansion of transient amplifying myogenic precursor cells during muscle growth and regeneration.
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The γ isoform of p38 can modulate myogenesis by repressing transcriptional activity of MyoD, promoting proliferation.
“The γ isoform of p38 can also modulate myogenesis by repressing the transcriptional activity of MyoD promoting proliferation [136] although it is unknown whether EPA and DHA alter the activation of p38 MAPK in the context of myogenesis.”
From Potential Roles of n-3 PUFAs during Skeletal Muscle Growth and Regeneration (2018) · cites this paper as [136]
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Satellite Cells and the Muscle Stem Cell Niche
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“We found that the isoform of p38 kinase (p38 ) phosphorylates MyoD, which negates the transcriptional activation potential of MyoD and leads to a repressive MyoD complex occupying the Myogenin promoter (191).”
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Segalés, J., Perdiguero, E., & Muñoz‐Cánoves, P. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00091 · Cited by 209 · see citing works
“By contrast, activation of p38γ in satellite cells suppresses MyoD transcriptional activity by direct phosphorylation, via association with the H3K9 methyltransferase KMT1A, thus also affecting this myogenic decision (Gillespie et al., 2009).”
BackgroundSoleimani, V. D., Punch, V. G., Kawabe, Y.-I., Jones, A., Palidwor, G., Porter, C. J., Cross, J. W., Carvajal, J. J., Kockx, C. E. M., van IJcken, W. F. J., et al. (2012) · Developmental Cell · doi:10.1016/j.devcel.2012.03.014 · Cited by 192 · see citing works
“Reverse cross-linking and phenol/chloroform extraction of chromatin were done as described previously (Gillespie et al., 2009).”
MethodSoleimani, V. D., Yin, H., Jahani-Asl, A., Ming, H., Kockx, C. E. M., van Ijcken, W. F. J., Grosveld, F., & Rudnicki, M. A. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.046 · Cited by 200 · see citing works
“, 1997), and posttranscriptional modifications of MyoD (Gillespie et al., 2009; Song et al., 1998) and its heterodimerization partners (Butler et al.”
BackgroundMethodp38 MAPK Pathway in the Heart: New Insights in Health and Disease
Romero-Becerra, R., Santamans, A. M., Folgueira, C., & Sabio, G. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197412 · Cited by 171 · see citing works
The myogenic kinome: protein kinases critical to mammalian skeletal myogenesis
Knight, J. D. R., & Kothary, R. (2011) · Skeletal Muscle · doi:10.1186/2044-5040-1-29 · Cited by 159 · see citing works
Chang, N. C., Sincennes, M., Chevalier, F. P., Brun, C. E., Lacaria, M., Segalés, J., Muñoz‐Cánoves, P., Ming, H., & Rudnicki, M. A. (2018) · Cell stem cell · doi:10.1016/j.stem.2018.03.022 · Cited by 154 · see citing works
“In order to prevent the effects of precocious differentiation mediated by loss of p38γ and the consequent downregulation of Myf5 transcription (Gillespie et al., 2009), we cultured cells in the presence of the eIF2α phosphatase inhibitor, Sal003 (Zismanov et al., 2016).”
BackgroundInfluentialSatellite Cells and Skeletal Muscle Regeneration
Dumont, N. A., Bentzinger, C., Sincennes, M.-C., & Rudnicki, M. (2015) · Comprehensive Physiology · doi:10.1002/j.2040-4603.2015.tb00646.x · Cited by 682 · see citing works
C/EBPβ mediates tumour‐induced ubiquitin ligase atrogin1/MAFbx upregulation and muscle wasting
Zhang, G., Jin, B., & Li, Y. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.292 · Cited by 136 · see citing works
Risco, A., del Fresno, C., Mambol, A., Alsina‐Beauchamp, D., MacKenzie, K. F., Yang, H., Barber, D. F., Morcelle, C., Arthur, J. S. C., Ley, S. C., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1207290109 · Cited by 123 · see citing works
“Moreover, studies in mice suggest that p38γ blocks premature differentiation of satellite cells, a skeletal muscle stem-cell population that participates in adult muscle regeneration (13).”
BackgroundConcise Review: Epigenetic Regulation of Myogenesis in Health and Disease
Sincennes, M., Brun, C. E., & Rudnicki, M. A. (2016) · Stem Cells Translational Medicine · doi:10.5966/sctm.2015-0266 · Cited by 114 · see citing works
ERK5 Regulates Muscle Cell Fusion through Klf Transcription Factors
Sunadome, K., Yamamoto, T., Ebisuya, M., Kondoh, K., Sehara‐Fujisawa, A., & Nishida, E. (2011) · Developmental Cell · doi:10.1016/j.devcel.2010.12.005 · Cited by 107 · see citing works
Potential Roles of n-3 PUFAs during Skeletal Muscle Growth and Regeneration
Tachtsis, B., Camera, D., & Lacham-Kaplan, O. (2018) · Nutrients · doi:10.3390/nu10030309 · Cited by 104 · see citing works
“The γ isoform of p38 can also modulate myogenesis by repressing the transcriptional activity of MyoD promoting proliferation [136] although it is unknown whether EPA and DHA alter the activation of p38 MAPK in the context of myogenesis.”
BackgroundDirect Reprogramming of Mouse Fibroblasts into Functional Skeletal Muscle Progenitors
Bar‐Nur, O., Gerli, M., Stefano, B. D., Almada, A. E., Galvin, A., Coffey, A., Huebner, A. J., Feige, P., Verheul, C., Cheung, P., et al. (2018) · Stem Cell Reports · doi:10.1016/j.stemcr.2018.04.009 · Cited by 98 · see citing works
“The previous finding that MyoD promotes proliferation and suppresses differentiation ofmyoblasts in certain in vitro (Gillespie et al., 2009) and in vivo (Tedesco et al.”
BackgroundResultBrennan, C. M., Emerson, C. P., Owens, J. M., & Christoforou, N. (2021) · JCI Insight · doi:10.1172/jci.insight.149915 · Cited by 92 · see citing works
“The MyoD-KMT1A repressive complex is recruited to the myogenin promoter, preventing expression and thereby blocking induction of the differentiation gene program (44).”
Epigenetic regulation of satellite cell fate during skeletal muscle regeneration
Massenet, J., Gardner, E., Chazaud, B., & Dilworth, F. J. (2021) · Skeletal Muscle · doi:10.1186/s13395-020-00259-w · Cited by 94 · see citing works
“Another study revealed the function of P38γ MAPK into the phosphorylation of the Ser199 and 200 of MYOD1 to allow the recruitment SUV39h1/KMT1a to the Myog promoter, reducing its expression during proliferation [59].”
BackgroundFaralli, H., & Dilworth, F. J. (2012) · Comparative and Functional Genomics · doi:10.1155/2012/836374 · Cited by 87 · see citing works
“Among the different signaling pathways that are activated during induction of myogenic differentiation the best characterized is that of the p38 MAPK signaling pathway.”
BackgroundInfluentialActivin A induces skeletal muscle catabolism via p38β mitogen‐activated protein kinase
Ding, H. J., Zhang, G., Sin, K. W. T., Liu, Z., Lin, R., Li, M., & Li, Y. (2016) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12145 · Cited by 83 · see citing works
Liu, Q., Zha, X., Faralli, H., Yin, H., Louis‐Jeune, C., Perdiguero, E., Pranckevičienė, E., Muñoz‐Cánoves, P., Rudnicki, M. A., Brand, M., et al. (2012) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjs045 · Cited by 81 · see citing works
“Early in myogenesis, p38 signaling is important in proliferating myoblasts where it prevents premature differentiation (Gillespie et al., 2009).”
BackgroundYates, D. T., Clarke, D. S., Macko, A. R., Anderson, M. J., Shelton, L. A., Nearing, M., Allen, R. E., Rhoads, R. P., & Limesand, S. W. (2014) · The Journal of Physiology · doi:10.1113/jphysiol.2014.272591 · Cited by 80 · see citing works
“During expansion, proliferating myoblasts also express the myogenic regulatory factor, myoD (Gillespie et al. 2009).”
Backgroundp38γ and p38δ Mitogen Activated Protein Kinases (MAPKs), New Stars in the MAPK Galaxy
Escós, A., Risco, A., Alsina‐Beauchamp, D., & Cuenda, A. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00031 · Cited by 77 · see citing works
Verrier, L., Escaffit, F., Chailleux, C., Trouche, D., & Vandromme, M. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1001390 · Cited by 71 · see citing works
“The histone methyltransferase Suv39h1 is responsible for the establishment of this repressive epigenetic mark in myoblasts, and is targeted to the Myog promoter by interacting with MyoD [22,23].”
New Insights into the p38 γ and p38 δ MAPK Pathways
Risco, A., & Cuenda, A. (2011) · Journal of Signal Transduction · doi:10.1155/2012/520289 · Cited by 70 · see citing works
“p38γ substrates that do not require PDZ domain-binding interactions are the mitochondrial protein Sab [37] and the transcription factor MyoD, whose phosphorylation by p38γ results in a decrease in its transcriptional activity [38].”
Blanc, R. S., Kallenbach, J. G., Bachman, J. F., Mitchell, A., Paris, N. D., & Chakkalakal, J. V. (2020) · Nature Communications · doi:10.1038/s41467-020-17620-8 · Cited by 68 · see citing works
Differentiation and large scale spatial organization of the genome
Joffe, B. I., Leonhardt, H., & Solovei, I. V. (2010) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2010.05.009 · Cited by 68 · see citing works
“Binding of MyoD to a promoter indeed was shown to affect its H3K9 methylation level [33].”
BackgroundRegulation of myogenic gene expression
Vicente‐García, C., Hernández‐Camacho, J. D., & Carvajal, J. J. (2022) · Experimental Cell Research · doi:10.1016/j.yexcr.2022.113299 · Cited by 65 · see citing works
“After p38 ɣ -mediated phosphorylation [87], MyoD recruits KMT1A/Suv39h1, which deposits H3K9me2/3 marks at the promoter assisting in gene repression [88].”
BackgroundMethodThe role of MyoD1 and histone modifications in the activation of muscle enhancers
Blum, R., & Dynlacht, B. D. (2013) · Epigenetics · doi:10.4161/epi.25441 · Cited by 63 · see citing works
Polycomb proteins in mammalian cell differentiation and plasticity
Prezioso, C., & Orlando, V. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.04.062 · Cited by 65 · see citing works
“In contrast to the activating role of p38-alpha in muscle gene activation, p38-gamma represses MyoD transcriptional activity by direct phosphorylation, via association with H3K9 methyltransferase KMT1A [109].”
BackgroundEpigenetic regulation of skeletal myogenesis
Saccone, V., & Puri, P. (2010) · Organogenesis · doi:10.4161/org.6.1.11293 · Cited by 63 · see citing works
Brien, P., Pugazhendhi, D., Woodhouse, S., Oxley, D., & Pell, J. M. (2013) · Stem Cells · doi:10.1002/stem.1399 · Cited by 58 · see citing works
Jin, W., Peng, J., & Jiang, S. (2016) · Biochemistry and Biophysics Reports · doi:10.1016/j.bbrep.2016.04.009 · Cited by 57 · see citing works
Heme Oxygenase-1 Controls an HDAC4-miR-206 Pathway of Oxidative Stress in Rhabdomyosarcoma
Cieśla, M., Marona, P., Kozakowska, M., Jeż, M., Seczyńska, M., Łoboda, A., Bukowska-Straková, K., Szade, A., Walawender, M., Kusior, M. E., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-1883 · Cited by 55 · see citing works
Epigenetic modifications in muscle regeneration and progression of Duchenne muscular dystrophy
Rugowska, A., Starosta, A., & Konieczny, P. (2021) · Clinical Epigenetics · doi:10.1186/s13148-021-01001-z · Cited by 58 · see citing works
“However, its exact mechanistic involvement in the temporal patterning of gene expression remains unknown in these processes [207].”
BackgroundP38β MAPK Upregulates Atrogin1/MAFbx by Specific Phosphorylation of C/EBPβ
Zhang, G., & Li, Y.-P. (2012) · Skeletal Muscle · doi:10.1186/2044-5040-2-20 · Cited by 53 · see citing works
“On the other hand, p38γ MAPK appears to regulate the expansion of myogenic precursor cells [14], endurance exercise-induced mitochondrial biogenesis and angiogenesis [15], as well as glucose uptake [16].”
BackgroundStress-Activated Protein Kinases in Spinal Cord Injury: Focus on Roles of p38
Kasuya, Y., Umezawa, H., & Hatano, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030867 · Cited by 54 · see citing works
“responsible for skeletal muscle growth and regeneration [25].”
BackgroundP38 kinase in gastrointestinal cancers
Phan, T. X., Zhang, X. H., Rosen, S. T., & Melstrom, L. G. (2023) · Cancer Gene Therapy · doi:10.1038/s41417-023-00622-1 · Cited by 51 · see citing works
Coda, D. M., Lingua, M. F., Morena, D., Foglizzo, V., Bersani, F., Ala, U., Ponzetto, C., & Taulli, R. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1005993 · Cited by 51 · see citing works
Girven, M., Dugdale, H. F., Owens, D. J., Hughes, D. C., Stewart, C. E., & Sharples, A. P. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25380 · Cited by 48 · see citing works
“It has also been demonstrated that a different p38 MAPK family member, p38-g, also plays a crucial role in regulating skeletal muscle differentiation (Gillespie et al., 2009; Lassar, 2009).”
STAT3-iNOS Signaling Mediates EGFRvIII-Induced Glial Proliferation and Transformation
Puram, S. V., Yeung, C., Jahani‐Asl, A., Lin, C., de la Iglesia, N., Konopka, G., Jackson‐Grusby, L., & Bonni, A. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.3243-11.2012 · Cited by 47 · see citing works
“Antibody–protein–DNA complexes were collected, washed, and eluted, and crosslinks were reversed according to the instructions of the manufacturer (Millipore) as described previously (Gillespie et al., 2009).”
Methodp38β MAPK mediates ULK1-dependent induction of autophagy in skeletal muscle of tumor-bearing mice
Liu, Z., Sin, K. W. T., Ding, H. J., Doan, H. A., Gao, S., Miao, H., Wei, Y., Wang, Y., Zhang, G., & Li, Y. (2018) · Cell Stress · doi:10.15698/cst2018.11.163 · Cited by 47 · see citing works
“…for most of the known roles of p38 MAPK including mediating inflammation [44, 45] and promoting myogenesis [46, 47]. p38 γ MAPK regulates the expansion of myogenic precursor cells [48], endurance exercise-induced mitochondrial biogenesis and angiogenesis [30], as well as glucose uptake [49].”
Epigenetic Regulation of Adult Myogenesis
Robinson, D. C. L., & Dilworth, F. J. (2017) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2017.08.002 · Cited by 43 · see citing works
“In part, the p38γMAPK signaling cascade helps modulate MyoD activity by specifically phosphorylating Ser199 and Ser200 of MyoD to mediate active repression of myogenic genes such as myogenin (Gillespie et al., 2009).”
Backgroundp38γ MAPK is required for inflammation-associated colon tumorigenesis
Yin, N. B., Qi, X., Tsai, S., Lu, Y., Basir, Z., Oshima, K., Thomas, J. P., Myers, C. R., Stoner, G. D., & Chen, G. (2015) · Oncogene · doi:10.1038/onc.2015.158 · Cited by 45 · see citing works
Segalés, J., Islam, A. B. M. M. K., Kumar, R., Liu, Q.-C., Sousa‐Victor, P., Dilworth, F. J., Ballestar, E., Perdiguero, E., & Muñoz‐Cánoves, P. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0074-x · Cited by 42 · see citing works
Endo, T. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.09.048 · Cited by 42 · see citing works
Histone deacetylase inhibitors: a potential epigenetic treatment for Duchenne muscular dystrophy.
Consalvi, S., Saccone, V., & Mozzetta, C. (2014) · Epigenomics · doi:10.2217/epi.14.36 · Cited by 36 · see citing works
Gene loss, thermogenesis, and the origin of birds
Newman, S. A., Mezentseva, N. V., & Badyaev, A. V. (2013) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.12090 · Cited by 36 · see citing works
New insights into the epigenetic control of satellite cells
Moresi, V. (2015) · World Journal of Stem Cells · doi:10.4252/wjsc.v7.i6.945 · Cited by 31 · see citing works
“Consistently, in p38-gamma MAPK-null SCs, KMT1A cannot associate with the myogenin promoter; therefore, myogenin is expressed earlier, resulting in decreased SC proliferation and defective differentiation [66] .”
Prmt7 promotes myoblast differentiation via methylation of p38MAPK on arginine residue 70
Jeong, H., Lee, S.-J., Lee, H., Kim, H., Vuong, T. A., Cho, H., Bae, G., & Kang, J. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0373-y · Cited by 34 · see citing works
“Previously, the opposing roles of p38α and p38γ have been proposed in MyoD-mediated myoblast differentiation [32].”
BackgroundRegulation of muscle stem cell fate
Fu, X., Zhuang, C., & Hu, P. (2022) · Cell Regeneration · doi:10.1186/s13619-022-00142-7 · Cited by 30 · see citing works
Sculpting Chromatin Beyond the Double Helix
Sartorelli, V., & Juan, A. H. (2011) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/b978-0-12-385940-2.00003-6 · Cited by 28 · see citing works
Belozerov, V. E., Lin, Z., Gingras, A., McDermott, J. C., & Siu, K. W. M. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00232-12 · Cited by 27 · see citing works
The p38 MAPK family, a pushmi-pullyu of skeletal muscle differentiation
Lassar, A. B. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200911123 · Cited by 25 · see citing works
“Gillespie et al. (2009) demonstrate that p38- MAPK phosphorylates the carboxy terminus of MyoD on serines 199 and 200, leading to increased interaction of MyoD with KMT1A.”
BackgroundResultInfluentialEssential Role for p38α MAPK But Not p38γ MAPK in Igf2 Expression and Myoblast Differentiation
Lovett, F. A., Cosgrove, R. A., Gonzalez, I., & Pell, J. M. (2010) · Endocrinology · doi:10.1210/en.2010-0209 · Cited by 25 · see citing works
Signaling pathways of adipose stem cell-derived exosomes promoting muscle regeneration
Zhu, A., Liu, N., Shang, Y., Zhen, Y., & An, Y. (2022) · Chinese Medical Journal · doi:10.1097/cm9.0000000000002404 · Cited by 24 · see citing works
“As for p38g, it helps assemble MyoD/ histone lysine methyltransferase 1A (KMT1A) inhibitory transcription complex to prevent MyoG expression, restricting myoblasts from prematurely entering further differentiation and promoting proliferation relatively.([76]) Additionally, p38a plays an essential role in forming multi…”
BackgroundMolecular regulation of satellite cells via intercellular signaling
Yeh, C.-J., Sattler, K. M., & Lepper, C. (2023) · Gene · doi:10.1016/j.gene.2023.147172 · Cited by 21 · see citing works
Chromatin signaling in muscle stem cells: interpreting the regenerative microenvironment
Brancaccio, A., & Palacios, D. (2015) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2015.00036 · Cited by 23 · see citing works
“The first lysine methyltransferase identified was Suv39h1 (KMT1A) that targets H3K9.”
BackgroundBrault, J. J., Pizzimenti, N. M., Dentel, J. N., & Wiseman, R. W. (2013) · Journal of Cellular Biochemistry · doi:10.1002/jcb.24486 · Cited by 23 · see citing works
Loonat, A. A., Martin, E. D., Sarafraz, N., Tilgner, K., Hertz, N. T., Levin, R. S., Shokat, K. M., Burlingame, A. L., Golforoush, P. A., Uddin, S., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201701545r · Cited by 22 · see citing works
p38α MAPK disables KMT1A-mediated repression of myogenic differentiation program
Chatterjee, B., Wolff, D. W., Jothi, M., Mal, M., & Mal, A. K. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0100-z · Cited by 21 · see citing works
“By contrast, p38γ MAPK represses myogenic differentiation by facilitating the association of MyoD with KMT1A in growing myoblasts [33].”
BackgroundInfluentialSin, T. K., Zhang, G., Zhang, Z., Gao, S., Li, M., & Li, Y. (2019) · Cancers · doi:10.3390/cancers11091272 · Cited by 22 · see citing works
“The p38 MAPK family is comprised of four isoforms, three of which (α, β, and γ) are expressed in skeletal muscle with distinct functions: p38α promotes myogenesis [68,69], whereas p38γ promotes satellite cell self-renewal [70] and other muscle activities [71,72].”
BackgroundQin, L.-L., Li, X.-K., Xu, J., Mo, D., Tong, X., Pan, Z., Li, J., Chen, Y., Zhang, Z., Wang, C., et al. (2012) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-012-1413-9 · Cited by 21 · see citing works
“However, a recent finding revealed that phosphorylation of MyoD on Ser199 and Ser200 by the mitogen-activated protein kinase p38gamma (p38-c) enhances MyoD’s occupancy on the Myogenin gene promoter with markedly decreased transcriptional activity [43].”
BackgroundSatellite cell count, VO 2max, and p 38 MAPK in inactive to moderately active young men
Macaluso, F., Brooks, N. E., van de Vyver, M., van Tubbergh, K., Niesler, C. U., & Myburgh, K. H. (2011) · Scandinavian Journal of Medicine and Science in Sports · doi:10.1111/j.1600-0838.2011.01389.x · Cited by 21 · see citing works
“Of the four isoforms (a, b, g, and d), p38a and p38g have been identified as key myogenic regulatory members (Cuenda & Rousseau, 2007; Hui et al., 2007; Gillespie et al., 2009).”
Backgroundp38γ MAPK Inflammatory and Metabolic Signaling in Physiology and Disease
Qi, X.-M., & Chen, G. (2023) · Cells · doi:10.3390/cells12131674 · Cited by 20 · see citing works
Gardner, S., Gross, S. M., David, L. L., Klimek, J. E., & Rotwein, P. S. (2015) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00184.2015 · Cited by 19 · see citing works
“By contrast, p38 has been found to block satellite cell differentiation (15, 25), indicating that individual p38s may mediate opposite biological effects in muscle.”
BackgroundSkeletal Muscle Stem Cells in the Spotlight: The Satellite Cell
Yablonka‐Reuveni, Z., & Day, K. R. (2011) · Humana Press eBooks · doi:10.1007/978-1-61779-021-8_11 · Cited by 19 · see citing works
“MyoD serves as the master transcription factor required to upregulate genes associated with myogenic differentiation [150, 151] and most studies on the role of MyoD during proliferation addressed mechanisms that suppress MyoD function to avoid premature differentiation [152].”
BackgroundHou, S., Lepp, A., & Chen, G. (2010) · AfCS-Nature Molecule Pages · doi:10.1038/mp.a001720.01 · Cited by 18 · see citing works
The multifaceted role of MyoD in adult skeletal muscle: homeostasis, regeneration, and diseases
Tsuji, R., Hayashi, T., Takahashi, S., Asakura, A., & Fujita, R. (2025) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00334.2025 · Cited by 18 · see citing works
Laminin differentially regulates the stemness of type I and type II pericytes
Gautam, J., Nirwane, A. M., & Yao, Y. (2017) · Stem Cell Research & Therapy · doi:10.1186/s13287-017-0479-4 · Cited by 16 · see citing works
Roles of p38 MAPK signaling in the skeletal muscle formation, regeneration, and pathology
Tomida, T., & Adachi‐Akahane, S. (2020) · Folia Pharmacologica Japonica · doi:10.1254/fpj20030 · Cited by 16 · see citing works
Chen, Y., Zhu, H., McCauley, S. R., Zhao, L., Johnson, S., Rhoads, R. P., & El‐Kadi, S. W. (2017) · Physiological Reports · doi:10.14814/phy2.13075 · Cited by 15 · see citing works
“Proliferation and differentiation of SCs, is primarily controlled by a group of muscle-specific transcription factors, known as myogenic regulatory factors (MRFs), including Myf5, MyoD, and myogenin (Holterman and Rudnicki 2005).”
BackgroundInfluentialGonadotropin-inhibiting hormone promotes apoptosis of bovine ovary granulosa cells
Li, X., Xu, G., Li, Z., Liu, H., Ma, X., Yang, L., Zhang, P., Zhao, J., Wang, J., & Lu, W. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119063 · Cited by 14 · see citing works
Liu, S.-Y., Chen, L.-K., Jhong, Y., Chen, C., Hsiao, L.-E., Ku, H.-H., Lee, P.-H., Hwang, G.-S., & Juan, C. (2024) · Clinical Science · doi:10.1042/cs20240341 · Cited by 14 · see citing works
Epigenetic control of muscle stem cells: time for a new dimension
Bianconi, V., & Mozzetta, C. (2022) · Trends in Genetics · doi:10.1016/j.tig.2022.01.001 · Cited by 13 · see citing works
p38γ MAPK delays myelination and remyelination and is abundant in multiple sclerosis lesions
Marziali, L. N., Hwang, Y., Palmisano, M., Cuenda, A., Sim, F. J., Gonzalez, A., Volsko, C. M., Dutta, R., Trapp, B. D., Wrabetz, L. G., et al. (2023) · Brain · doi:10.1093/brain/awad421 · Cited by 12 · see citing works
“35,36 We performed studies in vitro and in vivo demonstrating a key role of the γ isoform of p38 in the differentiation of OPCs, with implications in developmental myelination and remyelination.”
BackgroundMAPK family genes' influences on myogenesis in cattle: Genome-wide analysis and identification
Li, B., Wang, J., Raza, S. H. A., Wang, S., Liang, C., Zhang, W., Yu, S., Shah, M. A., Abdulmonem, W. A., Alharbi, Y. M., et al. (2023) · Research in Veterinary Science · doi:10.1016/j.rvsc.2023.04.024 · Cited by 11 · see citing works
Forcales, S. V., & Puri, P. (2010) · AfCS-Nature Molecule Pages · doi:10.1038/mp.a001510.01 · Cited by 11 · see citing works
Key Age-Imposed Signaling Changes That Are Responsible for the Decline of Stem Cell Function
Mehdipour, M., Liu, Y., Liu, C., Kumar, B., Kim, D., Gathwala, R., & Conboy, I. M. (2018) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-981-13-2835-0_5 · Cited by 8 · see citing works
Padilla‐Benavides, T., Reyes‐Gutierrez, P., & Imbalzano, A. N. (2020) · Biology · doi:10.3390/biology9070152 · Cited by 8 · see citing works
Muscle cell-derived Ccl8 is a negative regulator of skeletal muscle regeneration
Boss-Kennedy, A., Kim, D., Barai, P., Maldonado, C., Reyes-Ordoñez, A., & Chen, J. (2024) · The FASEB Journal · doi:10.1096/fj.202400184r · Cited by 5 · see citing works
Shi, H., & Gil-Antón, M. (2012) · InTech eBooks · doi:10.5772/30307 · Cited by 6 · see citing works
“A recent study using p38け-deficient mice revealed that muscles lacking this isoform of p38 MAPK contain 50% less satellite cells, and these cells exhibit reduced proliferation (Gillespie et al., 2009) implying that this p38 MAPK isoform may also be an important regulator of satellite cell deposition and proliferation.”
Chapter 63 – Immunological Responses to Muscle Injury
Tidball, J., & Rinaldi, C. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-381510-1.00063-6 · Cited by 4 · see citing works
Regulatory Landscapes of Muscle Satellite Cells: From Mechanism to Application
Lee, J., Yoon, S. H., Shim, K. S., & Tae, J. (2025) · International Journal of Stem Cells · doi:10.15283/ijsc25037 · Cited by 5 · see citing works
“MyoD also fosters SC proliferation (40).”
Mooshayef, N., Gilad, N., Mohanam, M. P., & Engelberg, D. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108281 · Cited by 3 · see citing works
“Of note, the expression levels of MyoD were slightly lower and the level of phosphorylated p38 a is slightly higher in the C2p38 b / g − / − cells than those in parental C2C12 cells.”
InfluentialRegulation of Muscle Stem Cell Quiescent and Undifferentiated State: Roles of Hesr1 and Hesr3 Genes
Yamaguchi, M., & Fukada, S. (2013) · Springer eBooks · doi:10.1007/978-94-007-5958-9_9 · Cited by 3 · see citing works
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Epigenetic Regulation of Muscle Stem Cells During Skeletal Muscle Regeneration and Disease
Biferali, B., & Mozzetta, C. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814879-2.00013-3 · Cited by 2 · see citing works
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3D organization of enhancers in MuSCs
He, L., Sun, H., & Wang, H. (2024) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2024.01.011 · Cited by 1 · see citing works
The SUV39 Family of H3K9 Methyltransferases in Skeletal Muscle Stem Cells
Garcia, P., Ait‐Si‐Ali, S., & Grand, F. L. (2025) · FASEB BioAdvances · doi:10.1096/fba.2024-00102 · Cited by 1 · see citing works
“Moreover, SUV39H1 has been found down-stream of p38γ, participating in the assembly of a repressive MYOD1 transcriptional complex and allowing for myogenic progression [140].”
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The Yin and Yang of Polycomb Repression in Regenerating Muscle
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“In contrast, phosphorylation of MyoD by p38g results in formation of a repressive MyoD complex and extensive methylation at H3K9 (Gillespie et al., 2009).”
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- Authors
- Gillespie, M. A., Le Grand, F., Scimè, A., Kuang, S., von Maltzahn, J., Seale, V., Cuenda, A., Ranish, J. A., & Rudnicki, M. A.
- Affiliations
- University of Ottawa (CA)
- The Sprott Centre for Stem Cell Research, Regenerative Medicine Program, Ottawa Health Research Institute, Ottawa, Ontario K1H 8L6, Canada 1
- Consejo Superior de Investigaciones Científicas (ES)
- Institute for Systems Biology (US)
- Corresponding author
- Rudnicki, Michael A.
- ORCID
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2009-12-21
- Volume
- 187
- Issue
- 7
- Pages
- 991-1005
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2806273
- OpenAlex
- W2136285175
- Cited by
- 131
- References
- 80
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 5 · 2023: 8 · 2022: 7 · 2021: 5 · 2020: 7 · 2019: 4 · 2018: 9 · 2017: 10 · 2016: 11 · 2015: 7 · 2014: 5 · 2013: 6 · 2012: 14
- FWCI
- 5.23
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research (MOP12080)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Congenital heart defects research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- myogenesis, gene silencing, histone H3 lysine 9 methylation, satellite cells, muscle regeneration, muscle growth, myogenic precursor cells, dystrophin-glycoprotein complex, skeletal muscle
- MeSH terms
- Animals, Cell Differentiation, Cell Line, Gene Expression Regulation, Histones, Mice, Inbred C57BL, Phosphorylation, Promoter Regions, Genetic, Regeneration, Transcription, Genetic, Signal Transduction, MyoD Protein, Myogenin, Muscle, Skeletal, Gene Silencing, Muscle Development, Epigenesis, Genetic, Mitogen-Activated Protein Kinase 12, Cell Proliferation, Mice
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