Methyltransferase-like 21c methylates and stabilizes the heat shock protein Hspa8 in type I myofibers in mice
Open accessAbstract
Protein methyltransferases mediate posttranslational modifications of both histone and nonhistone proteins. Whereas histone methylation is well-known to regulate gene expression, the biological significance of nonhistone methylation is poorly understood. Methyltransferase-like 21c (Mettl21c) is a newly classified nonhistone lysine methyltransferase whose in vivo function has remained elusive. Using a Mettl21c LacZ knockin mouse model, we show here that Mettl21c expression is absent during myogenesis and restricted to mature type I (slow) myofibers in the muscle. Using co-immunoprecipitation, MS, and methylation assays, we demonstrate that Mettl21c trimethylates heat shock protein 8 (Hspa8) at Lys-561 to enhance its stability. As such, Mettl21c knockout reduced Hspa8 trimethylation and protein levels in slow muscles, and Mettl21c overexpression in myoblasts increased Hspa8 trimethylation and protein levels. We further show that Mettl21c-mediated stabilization of Hspa8 enhances its function in chaperone-mediated autophagy, leading to degradation of client proteins such as the transcription factors myocyte enhancer factor 2A (Mef2A) and Mef2D. In contrast, Mettl21c knockout increased Mef2 protein levels in slow muscles. These results identify Hspa8 as a Mettl21c substrate and reveal that nonhistone methylation has a physiological function in protein stabilization.
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Mettl21e negatively regulates 26S proteasome activity, while Mettl21c is crucial for autophagy regulation.
“While Mettl21e negatively regulates 26S proteasome activity, Mettl21c seems to be crucial for autophagy regulation.”
From Mechanisms of muscle atrophy and hypertrophy: implications in health and disease (2021) · cites this paper as [61]
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Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
Sarbassov, D. D., Guertin, D. A., Ali, S. M., & Sabatini, D. M. (2005) · Science · doi:10.1126/science.1106148 · Cited by 6,216 · see citing works
Fiber Types in Mammalian Skeletal Muscles
Schiaffino, S., & Reggiani, C. (2011) · Physiological Reviews · doi:10.1152/physrev.00031.2010 · Cited by 3,022 · see citing works
Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact
Black, J. C., Rechem, C. V., & Whetstine, J. R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.006 · Cited by 1,318 · see citing works
Signal-dependent nuclear export of a histone deacetylase regulates muscle differentiation
McKinsey, T. A., Zhang, C., Lu, J., & Olson, E. N. (2000) · Nature · doi:10.1038/35040593 · Cited by 1,051 · see citing works
Chaperone-mediated autophagy: roles in disease and aging
Cuervo, A. M., & Wong, E. S. P. (2013) · Cell Research · doi:10.1038/cr.2013.153 · Cited by 850 · see citing works
Autophagy: A lysosomal degradation pathway with a central role in health and disease
Eskelinen, E., & Säftig, P. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.07.014 · Cited by 699 · see citing works
Chang, S., McKinsey, T. A., Zhang, C. L., Richardson, J. A., Hill, J. A., & Olson, E. N. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.19.8467-8476.2004 · Cited by 612 · see citing works
Chaperone-Assisted Selective Autophagy Is Essential for Muscle Maintenance
Arndt, V., Dick, N., Tawo, R., Dreiseidler, M., Wenzel, D., Hesse, M., Fürst, D. O., Säftig, P., Saint, R. B., Fleischmann, B. K., et al. (2010) · Current Biology · doi:10.1016/j.cub.2009.11.022 · Cited by 572 · see citing works
Consequences of the selective blockage of chaperone-mediated autophagy
Massey, A. C., Kaushik, S., Sovak, G., Kiffin, R., & Cuervo, A. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507436103 · Cited by 529 · see citing works
Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3
Gamerdinger, M., Hajieva, P., Kaya, A. M., Wolfrum, U., Hartl, F. U., & Behl, C. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.29 · Cited by 522 · cited 1× · see citing works
“For example, Hspa8 cooperates with BAG3, which mediates macro-autophagy and maintains mitochondria homeostasis (31, 32).”
BackgroundCaM kinase signaling induces cardiac hypertrophy and activates the MEF2 transcription factor in vivo
Passier, R., Zeng, H., Frey, N., Naya, F. J., Nicol, R. L., McKinsey, T. A., Overbeek, P. A., Richardson, J. A., Grant, S. R., & Olson, E. N. (2000) · Journal of Clinical Investigation · doi:10.1172/jci8551 · Cited by 521 · see citing works
Valosin-containing protein (VCP) is required for autophagy and is disrupted in VCP disease
Ju, J.-S., Fuentealba, R. A., Miller, S. E., Jackson, E., Piwnica-Worms, D., Baloh, R. H., & Weihl, C. C. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200908115 · Cited by 494 · see citing works
Non-histone protein methylation as a regulator of cellular signalling and function
Biggar, K. K., & Li, S. S.-C. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3915 · Cited by 479 · see citing works
A Small Molecule Inhibitor of Inducible Heat Shock Protein 70
Leu, J. I.-J., Pimkina, J. S., Frank, A. K., Murphy, M. E., & George, D. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.023 · Cited by 442 · see citing works
Stricher, F., Macri, C., Ruff, M., & Muller, S. (2013) · Autophagy · doi:10.4161/auto.26448 · Cited by 420 · see citing works
Histone deacetylase degradation andMEF2 activation promote the formation of slow-twitch myofibers
Potthoff, M. J., Wu, H., Arnold, M., Shelton, J. M., Backs, J., McAnally, J., Richardson, J. A., Bassel‐Duby, R., & Olson, E. N. (2007) · Journal of Clinical Investigation · doi:10.1172/jci31960 · Cited by 416 · see citing works
Critical roles of non-histone protein lysine methylation in human tumorigenesis
Hamamoto, R., Saloura, V., & Nakamura, Y. (2015) · Nature Reviews Cancer · doi:10.1038/nrc3884 · Cited by 376 · see citing works
Activation of MEF2 by muscle activity is mediated through a calcineurin‐dependent pathway
Wu, H., Rothermel, B., Kanatous, S., Rosenberg, P. B., Naya, F. J., Shelton, J. M., Hutcheson, K. A., DiMaio, J. M., Olson, E. N., Bassel‐Duby, R., et al. (2001) · The EMBO Journal · doi:10.1093/emboj/20.22.6414 · Cited by 366 · see citing works
Regulation of Neuronal Survival Factor MEF2D by Chaperone-Mediated Autophagy
Yang, Q., She, H., Gearing, M., Colla, E., Lee, M. K., Shacka, J. J., & Mao, Z. (2009) · Science · doi:10.1126/science.1166088 · Cited by 302 · see citing works
The functional diversity of protein lysine methylation
Lanouette, S., Mongeon, V., Figeys, D., & Couture, J. (2014) · Molecular Systems Biology · doi:10.1002/msb.134974 · Cited by 274 · see citing works
Requirement of MEF2A, C, and D for skeletal muscle regeneration
Liu, N., Nelson, B. R., Bezprozvannaya, S., Shelton, J. M., Richardson, J. A., Bassel‐Duby, R., & Olson, E. N. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401732111 · Cited by 227 · see citing works
Regulation of Skeletal Muscle Sarcomere Integrity and Postnatal Muscle Function by Mef2c
Potthoff, M. J., Arnold, M., McAnally, J., Richardson, J. A., Bassel‐Duby, R., & Olson, E. N. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01187-07 · Cited by 218 · see citing works
Interaction of myocyte enhancer factor 2 (MEF2) with a mitogen-activated protein kinase, ERK5/BMK1
Yang, C.-H., Ornatsky, O., McDermott, J. C., Cruz, T. F., & Prody, C. A. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.20.4771 · Cited by 161 · see citing works
Cloutier, P., Lavallée‐Adam, M., Faubert, D., Blanchette, M., & Coulombe, B. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003210 · Cited by 156 · see citing works
Wang, C., Yue, F., & Kuang, S. (2017) · BIO-PROTOCOL · doi:10.21769/bioprotoc.2279 · Cited by 134 · see citing works
Self-citationPagé, N., Gros, F., Schall, N., Décossas, M., Bagnard, D., Briand, J., & Muller, S. (2010) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2010.139832 · Cited by 125 · see citing works
Wüst, S., Dröse, S., Heidler, J., Wittig, I., Klockner, I., Frankó, A., Bonke, E., Günther, S., Gärtner, U., Boettger, T., et al. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.02.022 · Cited by 123 · see citing works
Cho, H., Shimazu, T., Toyokawa, G., Daigo, Y., Maehara, Y., Hayami, S., Ito, A., Masuda, K., Ikawa, N., Field, H. I., et al. (2012) · Nature Communications · doi:10.1038/ncomms2074 · Cited by 119 · see citing works
Post-translational control of the MEF2A transcriptional regulatory protein
Ornatsky, O., Cox, D. M., Tangirala, P., Andreucci, J. J., Quinn, Z. A., Wrana, J. L., Prywes, R., Yu, Y.-T., & McDermott, J. C. (1999) · Nucleic Acids Research · doi:10.1093/nar/27.13.2646 · Cited by 107 · see citing works
Jakobsson, M. E., Moen, A. R., Bousset, L., Egge-Jacobsen, W. M., Kernstock, S., Melki, R., & Falnes, P. Ø. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.483248 · Cited by 106 · see citing works
Protein lysine methylation by seven-β-strand methyltransferases
Falnes, P. Ø., Jakobsson, M. E., Davydova, E., Ho, A. Y. Y., & Małecki, J. (2016) · Biochemical Journal · doi:10.1042/bcj20160117 · Cited by 100 · see citing works
Huang, J. M., Hsu, Y., Mo, C., de Abreu, E. L., Kiel, D. P., Bonewald, L. F., Brotto, M., & Karasik, D. (2014) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.2200 · Cited by 99 · see citing works
Zhang, H., Amick, J., Chakravarti, R., Santarriaga, S., Schlanger, S., McGlone, C., Dare, M., Nix, J. C., Scaglione, K. M., Stuehr, D. J., et al. (2015) · Structure · doi:10.1016/j.str.2015.01.003 · Cited by 98 · see citing works
Evidence for the Role of BAG3 in Mitochondrial Quality Control in Cardiomyocytes
Tahrir, F. G., Knezevic, T., Gupta, M., Gordon, J., Cheung, J. Y., Feldman, A. M., & Khalili, K. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25476 · Cited by 75 · see citing works
Zhang, L., Sun, Y., Fei, M., Tan, C., Wu, J., Zheng, J., Tang, J., Sun, W., Lv, Z., Bao, J., et al. (2014) · Autophagy · doi:10.4161/auto.28477 · Cited by 61 · see citing works
Hypoxia Inhibits Myogenic Differentiation through p53 Protein-dependent Induction of Bhlhe40 Protein
Wang, C., Liu, W., Liu, Z., Chen, L., Liu, X., & Kuang, S. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.688671 · Cited by 59 · see citing works
Self-citationWiederstein, J. L., Nolte, H., Günther, S., Piller, T., Baraldo, M., Kostin, S., Bloch, W., Schindler, N., Sandri, M., Blaauw, B., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.136 · Cited by 52 · see citing works
Activation of the MEF2 transcription factor in skeletal muscles from myotonic mice
Wu, H., & Olson, E. N. (2002) · Journal of Clinical Investigation · doi:10.1172/jci15417 · Cited by 50 · see citing works
Activation of the MEF2 transcription factor in skeletal muscles from myotonic mice
Wu, H., & Olson, E. N. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0215417 · Cited by 44 · see citing works
Wang, C., Wang, M., Arrington, J. V., Shan, T., Yue, F., Nie, Y., Tao, W. A., & Kuang, S. (2016) · Development · doi:10.1242/dev.138099 · Cited by 22 · see citing works
Self-citationWang, C., Zhang, B., Ratliff, A. C., Arlington, J., Chen, J., Xiong, Y., Yue, F., Nie, Y., Hu, K., Jin, W. L., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201900582r · Cited by 16 · see citing works
Self-citation
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2 of the 43 references couldn’t be matched to a known paper.
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Vainshtein, A., & Sandri, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21134759 · Cited by 214 · see citing works
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Nitika, N., Porter, C. M., Truman, A. W., & Truttmann, M. C. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.011666 · Cited by 174 · see citing works
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Tooley, J. G., Catlin, J. P., & Tooley, C. E. S. (2022) · Stem Cell Reviews and Reports · doi:10.1007/s12015-022-10444-7 · Cited by 55 · see citing works
Kong, L., Yue, Y., Li, J., Yang, B., Chen, B., Liu, J., & Lu, Z. (2023) · Food Research International · doi:10.1016/j.foodres.2023.113240 · Cited by 47 · see citing works
Impact of Chaperone-Mediated Autophagy in Brain Aging: Neurodegenerative Diseases and Glioblastoma
Auzmendi-Iriarte, J., & Matheu, A. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.630743 · Cited by 45 · see citing works
Yao, L., Yin, H., Hong, M., Wang, Y., Yu, T., Teng, Y., Li, T., & Wu, Q. (2021) · Leukemia · doi:10.1038/s41375-021-01225-1 · Cited by 31 · see citing works
Falnes, P. Ø., Małecki, J., Herrera, M. C., Bengtsen, M. B., & Davydova, E. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104661 · Cited by 27 · see citing works
Lysine Methyltransferases Signaling: Histones are Just the Tip of the Iceberg
Lukinović, V., Casanova, A. G., Roth, G. S., Chuffart, F., & Reynoird, N. (2020) · Current Protein and Peptide Science · doi:10.2174/1871527319666200102101608 · Cited by 22 · see citing works
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Zoabi, M., Zhang, L., Li, T., Elias, J. E., Carlson, S. M., & Gozani, O. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014505 · Cited by 22 · see citing works
Chaperone-mediated autophagy in neurodegenerative diseases: mechanisms and therapy
Liu, Y., Tan, M., & Tan, M. (2023) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04640-9 · Cited by 18 · see citing works
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Wang, S., Zhao, J., Wang, L., Zhang, T., Zeng, W., & Lu, H. (2022) · British Poultry Science · doi:10.1080/00071668.2022.2121639 · Cited by 12 · see citing works
Steinert, N. D., Jorgenson, K. W., Lin, K., Hermanson, J. B., Lemens, J. L., & Hornberger, T. A. (2023) · iScience · doi:10.1016/j.isci.2023.106526 · Cited by 12 · see citing works
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Olsen, T., Lee, S., Vinknes, K., Norheim, F., Hjorth, M., Turner, C., Refsum, H., Jensen, J., Birkeland, K., & Drevon, C. (2021) · Research Square · doi:10.21203/rs.3.rs-143201/v1 · Cited by 1 · see citing works
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Costa, T. C. (2022) · doi:10.47328/ufvbbt.2022.488 · Cited by 1 · see citing works
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Khrystoforova, I., Liu, C., & Karasik, D. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-820088-9.00010-x
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- Authors
- Wang, C., Arrington, J., Ratliff, A. C., Chen, J., Horton, H. E., Nie, Y., Yue, F., Hrycyna, C. A., Tao, W. A., & Kuang, S.
- Affiliations
- Purdue University West Lafayette (US)
- Corresponding author
- Wang, Chao
- Kuang, Shihuan
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2019-09
- Volume
- 294
- Issue
- 37
- Pages
- 13718-13728
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC6746458
- OpenAlex
- W2964263751
- Cited by
- 33
- References
- 43
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 2 · 2023: 10 · 2022: 5 · 2021: 6 · 2020: 5
- FWCI
- 1.32
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- HHS | NIH | National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIAMS) (R01AR071649)
- USDA | National Institute of Food and Agriculture (NIFA) (NC-1184)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- Hsc70, lysine methyltransferase, protein stabilization, trimethylation, slow muscle fibers, myogenesis, chaperone-mediated autophagy, MEF2A, MEF2D, protein degradation
- MeSH terms
- Animals, Autophagy, Female, Heat-Shock Proteins, Humans, Male, Methylation, Methyltransferases, Muscles, Myofibrils, Protein Processing, Post-Translational, Muscle Development, Myoblasts, HSC70 Heat-Shock Proteins, Mice, Gene Knock-In Techniques, HEK293 Cells, MEF2 Transcription Factors
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