Mechanotransduction and the regulation of mTORC1 signaling in skeletal muscle

Int J Biochem Cell Biol. 2011 Sep;43(9):1267-76. doi: 10.1016/j.biocel.2011.05.007. Epub 2011 May 19.

Abstract

Mechanical stimuli play a major role in the regulation of skeletal muscle mass, and the maintenance of muscle mass contributes significantly to disease prevention and issues associated with the quality of life. Although the link between mechanical signals and the regulation of muscle mass has been recognized for decades, the mechanisms involved in converting mechanical information into the molecular events that control this process remain poorly defined. Nevertheless, our knowledge of these mechanisms is advancing and recent studies have revealed that signaling through a protein kinase called the mammalian target of rapamycin (mTOR) plays a central role in this event. In this review we will, (1) discuss the evidence which implicates mTOR in the mechanical regulation of skeletal muscle mass, (2) provide an overview of the mechanisms through which signaling by mTOR can be regulated, and (3) summarize our current knowledge of the potential mechanisms involved in the mechanical activation of mTOR signaling.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Amino Acids / metabolism
  • Animals
  • Gene Expression
  • Humans
  • Mechanistic Target of Rapamycin Complex 1
  • Mechanotransduction, Cellular*
  • Multiprotein Complexes
  • Muscle Spindles / metabolism
  • Muscle, Skeletal / enzymology
  • Muscle, Skeletal / metabolism
  • Muscle, Skeletal / physiology*
  • Organ Size
  • Phosphatidic Acids / metabolism
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phospholipase D / metabolism
  • Protein Binding
  • Proteins / genetics
  • Proteins / metabolism*
  • Signal Transduction*
  • TOR Serine-Threonine Kinases

Substances

  • Amino Acids
  • Multiprotein Complexes
  • Phosphatidic Acids
  • Proteins
  • Mechanistic Target of Rapamycin Complex 1
  • TOR Serine-Threonine Kinases
  • Phospholipase D