mVps34 is activated by an acute bout of resistance exercise.
Resistance-exercise training results in a progressive increase in muscle mass and force production. Following an acute bout of resistance exercise, the rate of protein synthesis increases proportionally with the increase in protein degradation, correlating at 3 h in the starved state. Amino acids taken immediately before or immediately after exercise increase the post-exercise rate of protein synthesis. Therefore a protein that controls protein degradation and amino acid-sensitivity would be a potential candidate for controlling the activation of protein synthesis following resistance exercise. One such candidate is the class III PI3K (phosphoinositide 3-kinase) Vps34 (vacuolar protein sorting mutant 34). Vps34 controls both autophagy and amino acid signalling to mTOR (mammalian target of rapamycin) and its downstream target p70 S6K1 (S6 kinase 1). We have identified a significant increase in mVps34 (mammalian Vps34) activity 3 h after resistance exercise, continuing for at least 6 h, and propose a mechanism whereby mVps34 could act as an internal amino acid sensor to mTOR after resistance exercise.
Mackenzie
M G
MG
James Black Centre, University of Dundee, 28 Dow Street, Dundee DD15EH, U.K. m.g.mackenzie@dundee.ac.uk
Hamilton
D L
DL
Murray
J T
JT
Baar
K
K
D000596:Amino Acids / Q000378:metabolism*; D004789:Enzyme Activation; D006801:Humans; D019869:Phosphatidylinositol 3-Kinases / Q000378:metabolism*; D019893:Ribosomal Protein S6 Kinases / Q000378:metabolism; D014891:Weight Lifting
D000596:Amino Acids; D019869:Phosphatidylinositol 3-Kinases; D019893:Ribosomal Protein S6 Kinases