Article

mVps34 is activated by an acute bout of resistance exercise

Details

Citation

MacKenzie MG, Hamilton DL, Murray JT & Baar K (2007) mVps34 is activated by an acute bout of resistance exercise. Biochemical Society Transactions, 35 (5), pp. 1314-1316. http://www-scopus-com.ezproxy.stir.ac.uk/record/display.url?eid=2-s2.0-36749001754&origin=resultslist&sort=plf-f&src=s&st1=mVps34+is+activated+by+an+acute+bout+of+resistance+exercise&sid=FCB07B7C2BC67441229E6CBD3A543A8B.WeLimyRvBMk2ky9SFKc8Q%3a1150&sot=b&s; https://doi.org/10.1042/BST0351314

Abstract
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.

Keywords
hypertrophy; mammalian target of rapamycin (mTOR); protein degradation; protein synthesis; resistance exercise; vacuolar protein sorting mutant 34 (Vp534)

Journal
Biochemical Society Transactions: Volume 35, Issue 5

StatusPublished
Publication date30/11/2007
PublisherPortland Press for the Biochemical Society
Publisher URLhttp://www-scopus-com.ezproxy.stir.ac.uk/…Q%3a1150&sot=b&s
ISSN0300-5127