dc.contributor.author |
Figueiredo, VC |
en |
dc.contributor.author |
Markworth, JF |
en |
dc.contributor.author |
Cameron-Smith, David |
en |
dc.date.accessioned |
2017-10-16T23:50:03Z |
en |
dc.date.issued |
2017-07 |
en |
dc.identifier.citation |
Cellular and Molecular Life Sciences 74(14):2537-2545 Jul 2017 |
en |
dc.identifier.issn |
1420-682X |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/36110 |
en |
dc.description.abstract |
The mammalian target of rapamycin (mTOR) complex exerts a pivotal role in protein anabolism and cell growth. Despite its importance, few studies adequately address the complexity of phosphorylation of the mTOR protein itself to enable conclusions to be drawn on the extent of kinase activation following this event. In particular, a large number of studies in the skeletal muscle biology field have measured Serine 2448 (Ser2448) phosphorylation as a proxy of mTOR kinase activity. However, the evidence to be described is that Ser2448 is not a measure of mTOR kinase activity nor is a target of AKT activity and instead has inhibitory effects on the kinase that is targeted by the downstream effector p70S6K in a negative feedback loop mechanism, which is evident when revisiting muscle research studies. It is proposed that this residue modification acts as a fine-tuning mechanism that has been gained during vertebrate evolution. In conclusion, it is recommended that Ser2448 is an inadequate measure and that preferential analysis of mTORC1 activation should focus on the downstream and effector proteins, including p70S6K and 4E-BP1, along mTOR protein partners that bind to mTOR protein to form the active complexes 1 and 2. |
en |
dc.format.medium |
Print-Electronic |
en |
dc.language |
eng |
en |
dc.publisher |
Springer Verlag |
en |
dc.relation.ispartofseries |
Cellular and Molecular Life Sciences |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.subject |
Muscles |
en |
dc.subject |
Animals |
en |
dc.subject |
Humans |
en |
dc.subject |
Serine |
en |
dc.subject |
Exercise |
en |
dc.subject |
Phosphorylation |
en |
dc.subject |
TOR Serine-Threonine Kinases |
en |
dc.subject |
Biomarkers |
en |
dc.title |
Considerations on mTOR regulation at serine 2448: Implications for muscle metabolism studies |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1007/s00018-017-2481-5 |
en |
pubs.issue |
14 |
en |
pubs.begin-page |
2537 |
en |
pubs.volume |
74 |
en |
dc.rights.holder |
Copyright: Springer Verlag |
en |
dc.identifier.pmid |
28220207 |
en |
pubs.end-page |
2545 |
en |
pubs.publication-status |
Published |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Review |
en |
pubs.elements-id |
615758 |
en |
dc.identifier.eissn |
1420-9071 |
en |
pubs.record-created-at-source-date |
2017-10-17 |
en |
pubs.dimensions-id |
28220207 |
en |