mTOR-dependent control of skeletal muscle protein synthesis

Int J Sport Nutr Exerc Metab. 2001 Dec:11 Suppl:S177-85. doi: 10.1123/ijsnem.11.s1.s177.

Abstract

Muscle mass is influenced by many factors including genetically programmed changes, hormonal state, level of activity, and disease processes. Ultimately, whether or not a muscle hypertrophies or atrophies is determined by a simple relationship between the rates of protein synthesis and degradation. When synthesis exceeds degradation, the muscle hypertrophies, and vice versa. In contrast to this simple relationship, the processes that control muscle protein synthesis and degradation are complex. Recently, significant progress has been made in understanding the biochemical mechanisms that control the rate of translation initiation, which is generally the limiting phase in protein synthesis.

Publication types

  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins / metabolism*
  • Cell Cycle Proteins
  • Humans
  • Insulin / physiology
  • Insulin-Like Growth Factor I / physiology
  • Muscle Proteins / biosynthesis*
  • Muscle, Skeletal / metabolism*
  • Phosphoproteins / metabolism*
  • Phosphorylation
  • Protein Biosynthesis
  • Protein Kinases / physiology*
  • RNA, Messenger / metabolism
  • TOR Serine-Threonine Kinases
  • Transcription, Genetic

Substances

  • Adaptor Proteins, Signal Transducing
  • Carrier Proteins
  • Cell Cycle Proteins
  • EIF4EBP1 protein, human
  • Insulin
  • Muscle Proteins
  • Phosphoproteins
  • RNA, Messenger
  • Insulin-Like Growth Factor I
  • Protein Kinases
  • MTOR protein, human
  • TOR Serine-Threonine Kinases