ArticleBiochemical and biophysical research communications2017
Tribbles 3 regulates protein turnover in mouse skeletal muscle.
Article in Biochemical and biophysical research communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Tribbles 3 blunts exercise-induced skeletal muscle adaptation.bioRxiv : the preprint server for biology · 2025Article
- Effects of PGC-1α overexpression on the myogenic response during skeletal muscle regeneration.Sports medicine and health science · 2022Article
- Enrichment of Newly Synthesized Proteins following treatment of C2C12 Myotubes with Endotoxin and Interferon-γ.Inflammation · 2022Article
- Obesity-induced TRB3 negatively regulates Brown adipose tissue function in mice.Biochemical and biophysical research communications · 2021Article
- Animal models of sarcopenia.Aging cell · 2020Review
- Sarcopenia is attenuated by TRB3 knockout in aging mice via the alleviation of atrophy and fibrosis of skeletal muscles.Journal of cachexia, sarcopenia and muscle · 2020Article
- TRB3 regulates skeletal muscle mass in food deprivation-induced atrophy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Change in Ubiquitin Proteasome System of Grass CarpFrontiers in physiology · 2018Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Skeletal muscle atrophy is associated with a disruption in protein turnover involving increased protein degradation and suppressed protein synthesis. Although it has been well studied that the IGF-1/PI3K/Akt pathway plays an essential role in the regulation of the protein turnover, molecule(s) that triggers the change in protein turnover still remains to be elucidated. TRB3 has been shown to inhibit Akt through direct binding. In this study, we hypothesized that TRB3 in mouse skeletal muscle negatively regulates protein turnover via the disruption of Akt and its downstream molecules. Muscle-specific TRB3 transgenic (TRB3TG) mice had decreased muscle mass and fiber size, resulting in impaired muscle function. We also found that protein synthesis rate and signaling molecules, mTOR and S6K1, were significantly reduced in TRB3TG mice, whereas the protein breakdown pathway was significantly activated. In contrast, TRB3 knockout mice showed increased muscle mass and had an increase in protein synthesis rate, but decreases in FoxOs, atrogin-1, and MuRF-1. These findings indicate that TRB3 regulates protein synthesis and breakdown via the Akt/mTOR/FoxO pathways.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.