P38β MAPK Upregulates Atrogin1/MAFbx by Specific Phosphorylation of C/EBPβ
Open accessAbstract
BACKGROUND: The p38 mitogen-activated protein kinases (MAPK) family plays pivotal roles in skeletal muscle metabolism. Recent evidence revealed that p38α and p38β exert paradoxical effects on muscle protein homeostasis. However, it is unknown why p38β, but not p38α, is capable of mediating muscle catabolism via selective activation of the C/EBPβ that upregulates atrogin1/MAFbx. METHODS: Tryptic phosphopeptide mapping was carried out to identify p38α- and p38β-mediated phosphorylation sites in C/EBPβ. Chromosome immunoprecipitation (ChIP) assay was used to evaluate p38α and p38β effect on C/EBPβ binding to the atrogin1/MAFbx promoter. Overexpression or siRNA-mediated gene knockdown of p38α and p38β, and site-directed mutagenesis or knockout of C/EBPβ, were used to analyze the roles of these kinases in muscle catabolism in C2C12 myotubes and mice. RESULTS: Cellular expression of constitutively active p38α or p38β resulted in phosphorylation of C/EBPβ at multiple serine and threonine residues; however, only p38β phosphorylated Thr-188, which had been known to be critical to the DNA-binding activity of C/EBPβ. Only p38β, but not p38α, activated C/EBPβ-binding to the atrogin1/MAFbx promoter. A C/EBPβ mutant in which Thr-188 was replaced by alanine acted as a dominant-negative inhibitor of atrogin1/MAFbx upregulation induced by either p38β or Lewis lung carcinoma (LLC) cell-conditioned medium (LCM). In addition, knockdown of p38β specifically inhibited C/EBPβ activation and atrogin1/MAFbx upregulation induced by LCM. Finally, expression of active p38β in mouse tibialis anterior specifically induced C/EBPβ phosphorylation at Thr-188, atrogin1/MAFbx upregulation and muscle mass loss, which were blocked in C/EBPβ-null mice. CONCLUSIONS: The α and β isoforms of p38 MAPK are capable of recognizing distinct phosphorylation sites in a substrate. The unique capacity of p38β in mediating muscle catabolism is due to its capability in phosphorylating Thr-188 of C/EBPβ.
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p38-MAPK upregulation could directly lead to increased proteasome-related catabolism, as shown in mice.
“Ultimately, p38-MAPK upregulation could directly lead to increased proteasome-related catabolism, as shown in mice [173].”
From Main Pathogenic Mechanisms and Recent Advances in COPD Peripheral Skeletal Muscle Wasting (2023) · cites this paper as [173]
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Sandri, M., Sandri, C., Gilbert, A., Skurk, C., Calabria, E., Picard, A., Walsh, K., Schiaffino, S., Lecker, S. H., & Goldberg, A. L. (2004) · Cell · doi:10.1016/s0092-8674(04)00400-3 · Cited by 3,012 · see citing works
Evans, W., Morley, J., Argilés, J., Bales, C., Baracos, V., Guttridge, D., Jatoi, A., Kalantar-zadeh, K., Lochs, H., Mantovani, G., et al. (2008) · Clinical Nutrition · doi:10.1016/j.clnu.2008.06.013 · Cited by 2,341 · see citing works
Stitt, T. N., Drujan, D., Clarke, B. A., Panaro, F., Timofeyva, Y., Kline, W. O., Gonzalez, M., Yancopoulos, G. D., & Glass, D. J. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00211-4 · Cited by 1,964 · see citing works
CCAAT/enhancer-binding proteins: structure, function and regulation
Ramji, D. P., & Foka, P. (2002) · Biochemical Journal · doi:10.1042/bj20020508 · Cited by 1,401 · see citing works
IKKβ/NF-κB Activation Causes Severe Muscle Wasting in Mice
Cai, D., Frantz, J. D., Tawa, N. E., Melendez, P. A., Oh, B.-C., Lidov, H. G. W., Hasselgren, P.-O., Frontera, W. R., Lee, J., Glass, D. J., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.027 · Cited by 1,367 · see citing works
Protein degradation by the ubiquitin-proteasome pathway in normal and disease states
Lecker, S. H., Goldberg, A. L., & Mitch, W. E. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010083 · Cited by 1,234 · see citing works
Tisdale, M. J. (2009) · Physiological Reviews · doi:10.1152/physrev.00016.2008 · Cited by 1,192 · see citing works
Characterization of the Structure and Function of a New Mitogen-activated Protein Kinase (p38β)
Jiang, Y., Chen, C., Li, Z., Guo, W., Gegner, J. A., Lin, S., & Han, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.17920 · Cited by 746 · see citing works
p38MAPK: stress responses from molecular mechanisms to therapeutics
Coulthard, L. R., White, D. E., Jones, D. L., McDermott, M. F., & Burchill, S. A. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.06.005 · Cited by 691 · see citing works
Li, Y.-P., Chen, Y., John, J., Moylan, J. S., Jin, B., Mann, D. L., & Reid, M. B. (2005) · The FASEB Journal · doi:10.1096/fj.04-2364com · Cited by 601 · see citing works
Self-citationSacheck, J. M., Hyatt, J. K., Raffaello, A., Thomas Jagoe, R., Roy, R. R., Reggie Edgerton, V., Lecker, S. H., & Goldberg, A. L. (2007) · The FASEB Journal · doi:10.1096/fj.06-6604com · Cited by 585 · see citing works
Enslen, H., Raingeaud, J., & Davis, R. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.3.1741 · Cited by 534 · see citing works
Phosphorylation by p38 MAPK as an Alternative Pathway for GSK3β Inactivation
Thornton, T. M., Pedraza-Alva, G., Deng, B., Wood, C. D., Aronshtam, A., Clements, J. L., Sabio, G., Davis, R. J., Matthews, D. E., Doble, B., et al. (2008) · Science · doi:10.1126/science.1156037 · Cited by 484 · see citing works
de Álvaro, C., Teruel, T., Hernández, R., & Lorenzo, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312021200 · Cited by 430 · see citing works
C/EBPβ Controls Exercise-Induced Cardiac Growth and Protects against Pathological Cardiac Remodeling
Boström, P., Mann, N., Wu, J., Quintero, P. A., Plovie, E. R., Panáková, D., Gupta, R. K., Xiao, C., MacRae, C. A., Rosenzweig, A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.11.036 · Cited by 411 · see citing works
Palacios, D., Mozzetta, C., Consalvi, S., Caretti, G., Saccone, V., Proserpio, V., Marquez, V. E., Valente, S., Mai, A., Forcales, S. V., et al. (2010) · Cell Stem Cell · doi:10.1016/j.stem.2010.08.013 · Cited by 392 · see citing works
An essential role for C/EBPβ in female reproductionPreprint
Sterneck, E., Tessarollo, L., & Johnson, P. F. (1997) · Genes & Development · doi:10.1101/gad.11.17.2153 · Cited by 389 · see citing works
Thomas, M., Lu, J. J.-Q., Ge, Q., Zhang, C. C., Chen, J., & Klibanov, A. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502067102 · Cited by 366 · see citing works
Specific Inhibitors of p38 Mitogen-activated Protein Kinase Block 3T3-L1 Adipogenesis
Engelman, J. A., Lisanti, M. P., & Scherer, P. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.48.32111 · Cited by 360 · see citing works
Tang, Q.-Q., Grønborg, M., Huang, H., Kim, J. W., Otto, T. C., Pandey, A., & Lane, M. D. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503891102 · Cited by 333 · see citing works
Regulation of skeletal muscle gene expression by p38 MAP kinases
Lluı́s, F., Perdiguero, E., Nebreda, Á. R., & Muñoz‐Cánoves, P. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.11.002 · Cited by 279 · see citing works
P38 MAPK Links Oxidative Stress to Autophagy-Related Gene Expression in Cachectic Muscle Wasting
McClung, J. M., Judge, A. R., Powers, S. K., & Yan, Z. (2010) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00192.2009 · Cited by 277 · see citing works
The p38α/β MAPK functions as a molecular switch to activate the quiescent satellite cell
Jones, N. C., Tyner, K. J., Nibarger, L., Stanley, H. M., Cornelison, D., Fedorov, Y. V., & Olwin, B. B. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200408066 · Cited by 272 · see citing works
Doyle, A., Zhang, G., Fattah, E. A. A., Eissa, N. T., & Li, Y. (2011) · The FASEB Journal · doi:10.1096/fj.10-164152 · Cited by 256 · see citing works
Self-citationPerdiguero, E., Ruiz‐Bonilla, V., Gresh, L., Hui, L., Ballestar, E., Sousa‐Victor, P., Baeza-Raja, B., Jardı́, M., Bosch-Comas, A., Esteller, M., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601587 · Cited by 253 · see citing works
Williams, S. C., Baer, M., Dillner, A., & Johnson, P. F. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07319.x · Cited by 222 · see citing works
Pogozelski, A. R., Geng, T., Li, P., Yin, X., Lira, V. A., Zhang, M., Chi, J.-T., & Yan, Z. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007934 · Cited by 164 · see citing works
Differential activation of p38MAPK isoforms by MKK6 and MKK3
Rémy, G., Risco, A. M., Iñesta-Vaquera, F., González‐Terán, B., Sabio, G., Davis, R. J., & Cuenda, A. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.11.020 · Cited by 155 · 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
Self-citationP38-γ–dependent gene silencing restricts entry into the myogenic differentiation program
Gillespie, M. A., Le Grand, F., Scimè, A., Kuang, S., von Maltzahn, J., Seale, V., Cuenda, A., Ranish, J. A., & Rudnicki, M. A. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200907037 · Cited by 131 · cited 1× · 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].”
BackgroundThe p38 MAPK stress pathway as a tumor suppressor or more?
Loesch, M. (2008) · Frontiers in bioscience · doi:10.2741/2951 · Cited by 115 · see citing works
Muscle atrophy in experimental cancer cachexia: Is the IGF‐1 signaling pathway involved?
Penna, F., Bonetto, A., Muscaritoli, M., Costamagna, D., Minero, V. G., Bonelli, G., Fanelli, F., Baccino, F., & Costelli, P. (2010) · International Journal of Cancer · doi:10.1002/ijc.25146 · Cited by 111 · see citing works
Role of cdk2 in the sequential phosphorylation/activation of C/EBPβ during adipocyte differentiation
Li, X., Kim, J. W., Grønborg, M., Urlaub, H., Lane, M. D., & Tang, Q. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703771104 · Cited by 109 · see citing works
Ho, R. C., Alcazar, O., FUJII, N. L., Hirshman, M. F., & Goodyear, L. J. (2004) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00563.2003 · Cited by 96 · see citing works
Kim, J. W., Tang, Q.-Q., Li, X., & Lane, M. D. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611137104 · Cited by 87 · see citing works
Chemical Genetics Define the Roles of p38α and p38β in Acute and Chronic Inflammation
O’Keefe, S. J., Mudgett, J. S., Cupo, S. H., Parsons, J. N., Chartrain, N. A., Fitzgerald, C. E., Chen, S.-L., Lowitz, K., Rasa, C. G., Visco, D. M., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704236200 · Cited by 81 · see citing works
Insulin Suppresses Transactivation by CAAT/Enhancer-binding Proteins β (C/EBPβ)
Guo, S., Cichy, S. B., He, X., Yang, Q., Ragland, M., Ghosh, A. K., Johnson, P. F., & Unterman, T. G. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008542200 · Cited by 81 · see citing works
Exercise-induced mitogen-activated protein kinase signalling in skeletal muscle
Long, Y. C., Widegren, U., & Zierath, J. R. (2004) · Proceedings of The Nutrition Society · doi:10.1079/pns2004346 · Cited by 75 · see citing works
Regulation of GLUT4 traffic and function by insulin and contraction in skeletal muscle
Marette, A. (2003) · Frontiers in bioscience · doi:10.2741/1137 · Cited by 65 · see citing works
p38α Is Active in Vitro and in Vivo When Monophosphorylated at Threonine 180
Askari, N., Beenstock, J., Livnah, O., & Engelberg, D. (2009) · Biochemistry · doi:10.1021/bi900024v · Cited by 47 · see citing works
Lee, S., Miller, M., Shuman, J. D., & Johnson, P. F. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.128413 · Cited by 37 · see citing works
Sicard, P., Clark, J., Jacquet, S., Mohammadi, S., Arthur, J. S. C., O’Keefe, S. J., & Marber, M. S. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2010.02.013 · Cited by 35 · see citing works
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Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1
Bodine, S. C., & Baehr, L. M. (2014) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00204.2014 · Cited by 1,117 · see citing works
Interleukin‐6 myokine signaling in skeletal muscle: a double‐edged sword?
Muñoz‐Cánoves, P., Scheele, C., Pedersen, B. K., & Serrano, A. L. (2013) · The FEBS Journal · doi:10.1111/febs.12338 · Cited by 774 · see citing works
Sarcopenia – Molecular mechanisms and open questions
Wiedmer, P., Jung, T., Castro, J. P., Pomatto, L. C. D., Sun, P. Y., Davies, K. J. A., & Grune, T. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101200 · Cited by 476 · see citing works
Tumor induces muscle wasting in mice through releasing extracellular Hsp70 and Hsp90
Zhang, G., Liu, Z., Ding, H., Zhou, Y., Doan, H. A., Sin, K. W. T., Zhu, Z. J., Flores, R., Wen, Y., Gong, X., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-00726-x · Cited by 248 · see citing works
Self-citationQuercetin Protects against Obesity-Induced Skeletal Muscle Inflammation and Atrophy
Le, N. H., Kim, C.-S., Park, T., Park, J. H. Y., Sung, M.-K., Lee, D. G., Hong, S.-M., Choe, S.-Y., Goto, T., Kawada, T., et al. (2014) · Mediators of Inflammation · doi:10.1155/2014/834294 · Cited by 167 · see citing works
Skeletal muscle glycoprotein 130's role in Lewis lung carcinoma–induced cachexia
Puppa, M. J., Gao, S., Narsale, A. A., & Carson, J. A. (2014) · The FASEB Journal · doi:10.1096/fj.13-240580 · Cited by 143 · see citing works
Biological basis and treatment of frailty and sarcopenia
Sato, R., Vatic, M., da Fonseca, G. W. P., Anker, S. D., & von Haehling, S. (2024) · Cardiovascular Research · doi:10.1093/cvr/cvae073 · Cited by 128 · see citing works
Carson, J. A., Hardee, J. P., & VanderVeen, B. N. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.11.005 · Cited by 104 · see citing works
Mediators and Patterns of Muscle Loss in Chronic Systemic Inflammation
Pérez-Baos, S., Prieto‐Potín, I., Roman‐Blas, J. A., Sánchez‐Pernaute, O., Largo, R., & Herrero‐Beaumont, G. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00409 · Cited by 99 · see citing works
p38 MAPK in Glucose Metabolism of Skeletal Muscle: Beneficial or Harmful?
Bengal, E., Aviram, S., & Hayek, T. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186480 · Cited by 98 · see citing works
Impact of Conventional and Atypical MAPKs on the Development of Metabolic Diseases
Kassouf, T., & Sumara, G. (2020) · Biomolecules · doi:10.3390/biom10091256 · Cited by 93 · see citing works
Zhang, G., Liu, Z., Ding, H. J., Miao, H., Garcia, J. M., & Li, Y. (2017) · Scientific Reports · doi:10.1038/s41598-017-02347-2 · Cited by 93 · see citing works
Self-citationSignaling pathways and intervention for therapy of type 2 diabetes mellitus
Cao, R. Y., Tian, H., Zhang, Y., Liu, G., Xu, H., Rao, G., Tian, Y., & Fu, X. (2023) · MedComm · doi:10.1002/mco2.283 · Cited by 92 · see citing works
Main Pathogenic Mechanisms and Recent Advances in COPD Peripheral Skeletal Muscle Wasting
Henrot, P., Dupin, I., Schilfarth, P., Esteves, P., Blervaque, L., Zysman, M., Gouzi, F., Hayot, M., Pomiès, P., & Berger, P. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24076454 · Cited by 85 · see citing works
“Ultimately, p38-MAPK upregulation could directly lead to increased proteasome-related catabolism, as shown in mice [173].”
BackgroundActivin 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
Self-citationWernbom, M., Apró, W., Paulsen, G., Nilsen, T. S., Blomstrand, E., & Raastad, T. (2013) · European Journal of Applied Physiology · doi:10.1007/s00421-013-2733-5 · Cited by 80 · see citing works
Sankaralingam, S., Alrob, O. A., Zhang, L., Jaswal, J. S., Wagg, C. S., Fukushima, A., Padwal, R. S., Johnstone, D. E., Sharma, A. M., & Lopaschuk, G. D. (2014) · Diabetes · doi:10.2337/db14-1050 · Cited by 76 · see citing works
Cachectic skeletal muscle response to a novel bout of low-frequency stimulation
Puppa, M., Murphy, E. A., Fayad, R., Hand, G. A., & Carson, J. A. (2014) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01270.2013 · Cited by 52 · see citing works
Sun, R., Zhang, S., Hu, W., Lü, X. Q., Lou, N., Zhen-de, Y., Chen, S., Zhang, X., & Yang, H. (2016) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00344.2015 · Cited by 49 · see citing works
Signaling mechanism of tumor cell‐induced up‐regulation of E3 ubiquitin ligase UBR2
Zhang, G., Lin, R., Kwon, Y. T., & Li, Y. (2013) · The FASEB Journal · doi:10.1096/fj.12-222711 · Cited by 47 · see citing works
Self-citationp38β 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
Self-citationZhou, X., Zhang, C., Wu, X., Hu, X., Zhang, Y., Wang, X., Zheng, L., Gao, P., Du, J., Zheng, W., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-33631-z · Cited by 47 · see citing works
Bodine, S. C. (2020) · Journal of Applied Physiology · doi:10.1152/japplphysiol.00381.2020 · Cited by 43 · see citing works
Gao, S., & Carson, J. (2016) · American Journal of Physiology - Cell Physiology · doi:10.1152/ajpcell.00052.2015 · Cited by 43 · see citing works
Gao, S., Zhang, G., Zhang, Z., Zhu, J. Z., Li, L., Zhou, Y., Rodney, G. G., Abo‐Zahrah, R., Anderson, L. J., Garcia, J. M., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2200215119 · Cited by 31 · see citing works
Self-citationCancer-Induced Muscle Wasting Requires p38β MAPK Activation of p300
Sin, T. K., Zhang, G., Zhang, Z., Zhu, J. Z., Zuo, Y., Frost, J. A., Li, M., & Li, Y. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-3219 · Cited by 30 · see citing works
Self-citationLautaoja-Kivipelto, J. H., Pekkala, S., Pasternack, A. H., Laitinen, M., Ritvos, O., & Hulmi, J. J. (2020) · Biomolecules · doi:10.3390/biom10050695 · Cited by 28 · see citing works
Sun, R., Zhang, S., Lü, X. Q., Hu, W., Lou, N., Zhao, Y. Q., Zhou, J., Zhang, X., & Yang, H. (2016) · Oncology Reports · doi:10.3892/or.2016.5165 · Cited by 24 · see citing works
Odeh, M., Tamir, Y., Haas, T., & Bengal, E. (2019) · FEBS Journal · doi:10.1111/febs.15070 · Cited by 22 · see citing works
P38α-MAPK Signaling Inhibition Attenuates Soleus Atrophy during Early Stages of Muscle Unloading
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p300 Mediates Muscle Wasting in Lewis Lung Carcinoma
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Self-citationSin, T. K., Zhang, G., Zhang, Z., Gao, S., Li, M., & Li, Y. (2019) · Cancers · doi:10.3390/cancers11091272 · Cited by 22 · see citing works
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Self-citationGuigni, B. A., van der Velden, J. L. J., Kinsey, C. M., Carson, J. A., & Toth, M. J. (2019) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00310.2019 · Cited by 16 · see citing works
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Self-citationHamel-Côté, G., Lapointe, F., Gendron, D., Rola‐Pleszczynski, M., & Staňková, J. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0334-6 · Cited by 12 · see citing works
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Evertsson, K., Fjällström, A.-K., Norrby, M., & Tågerud, S. (2014) · Journal of Molecular Signaling · doi:10.1186/1750-2187-9-2 · Cited by 9 · see citing works
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Lee, S. H., Baek, S., Park, H., Han, K., Lee, K. P., & Ahn, S. H. (2024) · Physical Activity and Nutrition · doi:10.20463/pan.2024.0036 · Cited by 4 · see citing works
GL261 glioblastoma induces delayed body weight gain and stunted skeletal muscle growth in young mice
Huot, J. R., Jamnick, N. A., Pin, F., Livingston, P. D., Callaway, C. S., Morrow, S. K., & Bonetto, A. (2025) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00035.2025 · Cited by 4 · see citing works
Protective effects of irisin in sarcopenia: a promising treatment
Chen, Y., Li, G., Gao, F., Li, R., Yang, M., Ge, Y., & Wu, X. (2026) · Journal of Orthopaedic Translation · doi:10.1016/j.jot.2026.101090 · Cited by 2 · see citing works
Significance of the p38MAPK-CRP2 axis in myofibroblastic phenotypic transition
Hayashi, K., Labios, R. J., Morita, T., Ashimori, A., Aoki, R., Mikuni, M., & Kimura, K. (2023) · Cell Structure and Function · doi:10.1247/csf.23060 · Cited by 2 · see citing works
Yang, J.-M., Han, I., Chen, T.-H., Hsieh, P., Tsai, M., & Chien, H. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176854 · Cited by 2 · see citing works
Liu, Q., Zhou, H., Fu, C., Han, M., Xie, S., Li, M., & Li, C. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142675 · Cited by 2 · see citing works
Hayashi, K., Kobayashi, M., Mori, K., Nakagawa, Y., Watanabe, B., Ashimori, A., Higashijima, F., Yoshimoto, T., Sunada, J., Morita, T., et al. (2024) · Experimental Cell Research · doi:10.1016/j.yexcr.2024.114221 · Cited by 1 · see citing works
You, Y., Su, Z., Wang, H., Liu, S., Wang, J., Qiu, F. X., Jiang, Z., Wang, J., Li, Y., & Zhang, G. (2025) · Journal of Molecular Histology · doi:10.1007/s10735-025-10587-0 · Cited by 1 · see citing works
Self-citationHirano, K., Yamauchi, H., Nakahara, N., Kinoshita, K., Yamaguchi, M., & Takemori, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222312644 · Cited by 1 · see citing works
Thompson, J. M., Doering, T. M., Budiono, B. P., MacKenzie‐Shalders, K. L., Ashton, K. J., Dunn, P. J., & Coffey, V. G. (2026) · Experimental Physiology · doi:10.1113/ep093999
- Authors
- Zhang, G., & Li, Y.-P.
- Affiliations
- The University of Texas Health Science Center at Houston (US)
- ORCID
- Zhang, Guohua
- Venue
- Skeletal Muscle
- Published
- 2012
- Volume
- 2
- Issue
- 1
- Pages
- 20
- ISSN
- 2044-5040 (ISSN-L)
- PMC
- PMC3534568
- OpenAlex
- W2016621017
- Cited by
- 53
- References
- 42
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 6 · 2023: 3 · 2022: 3 · 2021: 2 · 2020: 7 · 2019: 6 · 2018: 2 · 2017: 2 · 2016: 3 · 2015: 2 · 2014: 5 · 2013: 4
- FWCI
- 1.42
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Skeletal Muscle (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Fudan University
- Hebrew University of Jerusalem
- National Cancer Institute
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR052511)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
- Keywords
- p38α MAPK, C/EBPβ, muscle protein degradation, muscle catabolism, selective protein degradation, skeletal muscle atrophy, tibialis anterior
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