PMID- 21138990
OWN - NLM
STAT- MEDLINE
DCOM- 20111202
LR  - 20211203
IS  - 1759-4685 (Electronic)
IS  - 1759-4685 (Linking)
VI  - 3
IP  - 4
DP  - 2011 Aug
TI  - mTORC1 signaling: what we still don't know.
PG  - 206-20
LID - 10.1093/jmcb/mjq038 [doi]
AB  - The mammalian target of rapamycin (mTOR) is a protein kinase that plays key roles 
      in cellular regulation. It forms complexes with additional proteins. The 
      best-understood one is mTOR complex 1 (mTORC1). The regulation and cellular 
      functions of mTORC1 have been the subjects of intense study; despite this, many 
      questions remain to be answered. They include questions about the actual 
      mechanisms by which mTORC1 signaling is stimulated by hormones and growth 
      factors, which involves the small GTPase Rheb, and by amino acids, which involves 
      other GTPase proteins. The control of Rheb and the mechanism by which it 
      activates mTORC1 remain incompletely understood. Although it has been known for 
      many years that rapamycin interferes with some functions of mTORC1, it is not 
      known how it does this, or why only some functions of mTORC1 are affected. mTORC1 
      regulates diverse cellular functions. Several mTORC1 substrates are now known, 
      although in several cases their physiological roles are poorly or incompletely 
      understood. In the case of several processes, although it is clear that they are 
      regulated by mTORC1, it is not known how mTORC1 does this. Lastly, mTORC1 is 
      implicated in ageing, but again it is unclear what mechanisms account for this. 
      Given the importance of mTORC1 signaling both for cellular functions and in human 
      disease, it is a high priority to gain further insights into the control of 
      mTORC1 signaling and the mechanisms by which it controls cellular functions and 
      animal physiology.
FAU - Wang, Xuemin
AU  - Wang X
AD  - School of Biological Sciences, Life Sciences Building, University of Southampton, 
      UK.
FAU - Proud, Christopher G
AU  - Proud CG
LA  - eng
GR  - Biotechnology and Biological Sciences Research Council/United Kingdom
GR  - Wellcome Trust/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20101207
PL  - United States
TA  - J Mol Cell Biol
JT  - Journal of molecular cell biology
JID - 101503669
RN  - 0 (Multiprotein Complexes)
RN  - 0 (Neuropeptides)
RN  - 0 (Proteins)
RN  - 0 (RHEB protein, human)
RN  - 0 (Ras Homolog Enriched in Brain Protein)
RN  - 0 (Tuberous Sclerosis Complex 1 Protein)
RN  - 0 (Tumor Suppressor Proteins)
RN  - EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1)
RN  - EC 2.7.11.1 (TOR Serine-Threonine Kinases)
RN  - EC 2.7.11.25 (MAP Kinase Kinase Kinases)
RN  - EC 3.6.5.2 (Monomeric GTP-Binding Proteins)
SB  - IM
MH  - Autophagy
MH  - Humans
MH  - MAP Kinase Kinase Kinases/metabolism
MH  - Mechanistic Target of Rapamycin Complex 1
MH  - Monomeric GTP-Binding Proteins/metabolism
MH  - Multiprotein Complexes
MH  - Neuropeptides/metabolism
MH  - Proteins/*metabolism
MH  - Ras Homolog Enriched in Brain Protein
MH  - *Signal Transduction
MH  - TOR Serine-Threonine Kinases
MH  - Tuberous Sclerosis Complex 1 Protein
MH  - Tumor Suppressor Proteins/metabolism
EDAT- 2010/12/09 06:00
MHDA- 2011/12/13 00:00
CRDT- 2010/12/09 06:00
PHST- 2010/12/09 06:00 [entrez]
PHST- 2010/12/09 06:00 [pubmed]
PHST- 2011/12/13 00:00 [medline]
AID - mjq038 [pii]
AID - 10.1093/jmcb/mjq038 [doi]
PST - ppublish
SO  - J Mol Cell Biol. 2011 Aug;3(4):206-20. doi: 10.1093/jmcb/mjq038. Epub 2010 Dec 7.