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Peer-reviewedCC BY-NC 4.0Zoological Research

Comprehensive multi-post-translational modifications profiling reveals age-associated remodeling in skeletal muscle

  • Jian Li1
  • Xin-Qiang Lan2
  • Cai-Fen Guo3
  • Xiang Wang2
  • Chun-Ping Huang2
  • Dong-Qin Zhang4
  • Lin Zeng5
  • Xiao-Li Tian6
  • Yang Xiang2
  • Qi-Quan Wang2
6 affiliations
  1. 1Department of Sports Medicine, The Beijing Jishuitan Hospital Guizhou Hospital, Guiyang, Guizhou 550014, China
  2. 2Metabolic Control and Aging, Human Aging Research Institute and School of Life Science, Nanchang University, and Jiangxi Key Laboratory of Human Aging, Nanchang, Jiangxi 330031, China
  3. 3Department of Urology, The Affiliated Hospital of Guizhou Medical University, Guiyang, Guizhou 550001, China
  4. 4HeartSeek Biotechnology, Kunming, Yunnan 650000, China
  5. 5Institutional Center for Shared Technologies and Facilities of the Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan 650201, China
  6. 6Aging and Vascular Diseases, Human Aging Research Institute and School of Life Science, Nanchang University, and Jiangxi Key Laboratory of Aging and Diseases, Nanchang, Jiangxi 330031, China
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Abstract

Sarcopenia, characterized by the progressive loss of skeletal muscle mass and function, is a major hallmark of aging. Post-translational modifications (PTMs) play essential roles in regulating protein activity and cellular homeostasis; however, how multiple PTMs are remodeled during skeletal muscle aging remains incompletely characterized. Here, we performed comprehensive multi-layered proteomic profiling of skeletal muscle from young (3-month-old) and aged (24-month-old) mice, systematically quantifying the global proteome together with five major PTMs: acetylation, phosphorylation, N-glycosylation, O-glycosylation, and ubiquitination. In total, we identified 5337 proteins and mapped thousands of PTM sites, generating an integrated atlas of age-associated proteomic and PTM remodeling in skeletal muscle. Pathway enrichment analyses revealed distinct modification-specific patterns: acetylation and phosphorylation were predominantly associated with metabolic and mitochondrial-related pathways; N-glycosylation was enriched in immune- and secretory pathway-related processes; O-glycosylation was associated with muscle contraction-related pathways; and ubiquitination was preferentially linked to cytoskeletal organization in muscle cells. Correlation analyses further uncovered diverse association patterns among different PTMs across protein- and modification-level datasets. Phosphorylation and ubiquitination exhibited consistent positive associations, whereas acetylation and ubiquitination showed both inverse and concordant co-variation patterns across subsets of proteins. Phosphorylation and O-glycosylation displayed heterogeneous association patterns across different proteins, and acetylation and phosphorylation demonstrated positive correlations with distinct age-associated directional changes across protein subsets. Together, these results provide a comprehensive, multi-dimensional view of age-associated remodeling of the skeletal muscle proteome and multiple PTM layers, offering a valuable resource for understanding molecular alterations accompanying muscle aging and sarcopenia.

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Cite

BibTeXRIS
BibTeX
@article{li2026comprehensive,
  title = {{Comprehensive multi-post-translational modifications profiling reveals age-associated remodeling in skeletal muscle}},
  author = {Jian Li and Xin-Qiang Lan and Cai-Fen Guo and Xiang Wang and Chun-Ping Huang and Dong-Qin Zhang and Lin Zeng and Xiao-Li Tian and Yang Xiang and Qi-Quan Wang},
  journal = {Zoological Research},
  year = {2026},
  month = sep,
  doi = {10.24272/j.issn.2095-8137.2025.460},
  url = {https://doi.org/10.24272/j.issn.2095-8137.2025.460},
  note = {CC BY-NC 4.0},
}
RIS
TY  - JOUR
TI  - Comprehensive multi-post-translational modifications profiling reveals age-associated remodeling in skeletal muscle
AU  - Jian Li
AU  - Xin-Qiang Lan
AU  - Cai-Fen Guo
AU  - Xiang Wang
AU  - Chun-Ping Huang
AU  - Dong-Qin Zhang
AU  - Lin Zeng
AU  - Xiao-Li Tian
AU  - Yang Xiang
AU  - Qi-Quan Wang
PY  - 2026
DA  - 2026/09/18
JO  - Zoological Research
DO  - 10.24272/j.issn.2095-8137.2025.460
UR  - https://doi.org/10.24272/j.issn.2095-8137.2025.460
AB  - Sarcopenia, characterized by the progressive loss of skeletal muscle mass and function, is a major hallmark of aging. Post-translational modifications (PTMs) play essential roles in regulating protein activity and cellular homeostasis; however, how multiple PTMs are remodeled during skeletal muscle aging remains incompletely characterized. Here, we performed comprehensive multi-layered proteomic profiling of skeletal muscle from young (3-month-old) and aged (24-month-old) mice, systematically quantifying the global proteome together with five major PTMs: acetylation, phosphorylation, N-glycosylation, O-glycosylation, and ubiquitination. In total, we identified 5337 proteins and mapped thousands of PTM sites, generating an integrated atlas of age-associated proteomic and PTM remodeling in skeletal muscle. Pathway enrichment analyses revealed distinct modification-specific patterns: acetylation and phosphorylation were predominantly associated with metabolic and mitochondrial-related pathways; N-glycosylation was enriched in immune- and secretory pathway-related processes; O-glycosylation was associated with muscle contraction-related pathways; and ubiquitination was preferentially linked to cytoskeletal organization in muscle cells. Correlation analyses further uncovered diverse association patterns among different PTMs across protein- and modification-level datasets. Phosphorylation and ubiquitination exhibited consistent positive associations, whereas acetylation and ubiquitination showed both inverse and concordant co-variation patterns across subsets of proteins. Phosphorylation and O-glycosylation displayed heterogeneous association patterns across different proteins, and acetylation and phosphorylation demonstrated positive correlations with distinct age-associated directional changes across protein subsets. Together, these results provide a comprehensive, multi-dimensional view of age-associated remodeling of the skeletal muscle proteome and multiple PTM layers, offering a valuable resource for understanding molecular alterations accompanying muscle aging and sarcopenia.
SN  - 2095-8137
ER  -