{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTRIM63, which encodes the muscle‐specific E3 ubiquitin ligase MuRF1, plays a central role in maintaining myofibrillar protein homeostasis in skeletal and cardiac muscle. Under atrophy‐inducing conditions such as disuse, glucocorticoid exposure, and disease‐related stress, TRIM63 transcription is upregulated and contributes to the degradation of key sarcomeric proteins (e.g. troponin I, titin) via the ubiquitin–proteasome system. Its expression is tightly regulated by various transcription factors—including members of the FOXO family, the glucocorticoid receptor, and SMAD proteins—to coordinate muscle protein turnover during remodeling, atrophy, and adaptation to exercise."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in protein degradation, extensive studies have elucidated the molecular and structural properties of TRIM63. In muscle, TRIM63 not only marks sarcomeric proteins for ubiquitination but also interacts directly with structural proteins such as titin, influencing the integrity of the M-line and overall sarcomere assembly. Moreover, TRIM63 activity is implicated in the regulation of metabolic processes—including glycolysis and insulin secretion—thereby linking contractile protein turnover with energy metabolism. Post-translational modifications and coordinated interactions with signaling molecules (for example, through its conserved RING, B-box, and COS domains) further refine its activity in response to stresses such as oxidative damage and exercise-induced remodeling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinical and translational studies have further implicated TRIM63 in a broad spectrum of muscle-related pathologies. Genetic variants and altered expression of TRIM63 have been associated with conditions such as cancer cachexia, chronic obstructive pulmonary disease, and cardiac remodeling in hypertrophic cardiomyopathy and post–myocardial infarction hypertrophy. In these contexts, aberrant TRIM63 activity influences both muscle atrophy and compensatory hypertrophic responses. Furthermore, modulation of TRIM63—whether by natural regulators (e.g. vitamin D, or deubiquitinating enzymes like USP19) or by emerging small-molecule inhibitors—offers a promising therapeutic target for preserving muscle mass and function. Recent structural insights into its domain organization and diagnostic applications such as RNA in situ hybridization as a biomarker highlight the growing potential of TRIM63 as both a central mechanistic mediator and a clinical tool in muscle disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "37"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Sue C Bodine, Leslie M Baehr "}, {"type": "b", "children": [{"type": "t", "text": "Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Endocrinol Metab (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpendo.00204.2014"}], "href": "https://doi.org/10.1152/ajpendo.00204.2014"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25096180"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25096180"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Vishram Kedar, Holly McDonough, Ranjana Arya, et al. 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