Cited by 121Muscle metabolism and nutritionPI3K/AKT/mTOR signaling in cancerMetabolism, Diabetes, and Cancer

Regulation of mTORC1 by growth factors, energy status, amino acids and mechanical stimuli at a glance

Open access
Bond, Peter·2016·Journal of the International Society of Sports Nutrition

Abstract

The mechanistic/mammalian target of rapamycin complex 1 (mTORC1) plays a pivotal role in the regulation of skeletal muscle protein synthesis. Activation of the complex leads to phosphorylation of two important sets of substrates, namely eIF4E binding proteins and ribosomal S6 kinases. Phosphorylation of these substrates then leads to an increase in protein synthesis, mainly by enhancing translation initiation. mTORC1 activity is regulated by several inputs, such as growth factors, energy status, amino acids and mechanical stimuli. Research in this field is rapidly evolving and unraveling how these inputs regulate the complex. Therefore this review attempts to provide a brief and up-to-date narrative on the regulation of this marvelous protein complex. Additionally, some sports supplements which have been shown to regulate mTORC1 activity are discussed.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1186/s12970-016-0118-y

Cites

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Muscle protein synthesis response to amino acids is impaired, in part via suppression of insulin signalling, which is required to drive mTORC1 signalling for protein synthesis.

    “Besides the direct inflammation‐induced mechanisms explained in earlier section, the muscle protein synthesis response to amino acids is also impaired, in part via the suppression of insulin signalling, which is required to drive mTORC1 signalling for protein synthesis.[ 84 ]”

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

The citation lists haven’t been fetched yet

References 104 · Cited by 121

Authors
Bond, P.
Affiliations
PeterBond.nl Waterhoenlaan 25 Zeist Netherlands
Corresponding author
Bond, Peter
Venue
Journal of the International Society of Sports Nutrition
Published
2016-01-05
Volume
13
Issue
1
Pages
8-8
ISSN
1550-2783 (ISSN-L)
OpenAlex
W2288940883
Cited by
121
References
104
Citations by year
2026: 14 · 2025: 10 · 2024: 7 · 2023: 9 · 2022: 14 · 2021: 16 · 2020: 15 · 2019: 6 · 2018: 15 · 2017: 12 · 2016: 3
FWCI
1.30
Type
journal article
Language
en
Open access
Locations
  • Journal of the International Society of Sports Nutrition (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Muscle metabolism and nutrition
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords
mTORC1, skeletal muscle protein synthesis, growth factors, energy status, amino acids, mechanical stimuli, eIF4E-binding protein, RSK, translation initiation, sports supplements
MeSH terms
Mechanistic Target of Rapamycin Complex 1, Amino Acids, Animals, Humans, Muscle Proteins, Phosphorylation, Protein Binding, Growth Hormone, Protein Biosynthesis, Signal Transduction, Muscle, Skeletal, Dietary Supplements, Active Transport, Cell Nucleus, Multiprotein Complexes, Intracellular Signaling Peptides and Proteins, AMP-Activated Protein Kinases, TOR Serine-Threonine Kinases

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review