The University of Southampton
University of Southampton Institutional Repository

mTORC1 signaling: what we still don't know

mTORC1 signaling: what we still don't know
mTORC1 signaling: what we still don't know
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.
mTORC1, protein synthesis, cell signaling, transcription, cell growth, autophagy, metabolism
1674-2788
206-220
Wang, Xuemin
d6bb4eb2-5687-46ed-b770-cceb22fd792e
Proud, Christopher G.
59dabfc8-4b44-4be8-a17f-578a58550cb3
Wang, Xuemin
d6bb4eb2-5687-46ed-b770-cceb22fd792e
Proud, Christopher G.
59dabfc8-4b44-4be8-a17f-578a58550cb3

Wang, Xuemin and Proud, Christopher G. (2011) mTORC1 signaling: what we still don't know. [in special issue: Collection on Apoptosis] Journal of Molecular Cell Biology, 3 (4), 206-220. (doi:10.1093/jmcb/mjq038). (PMID:21138990)

Record type: Article

Abstract

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.

Full text not available from this repository.

More information

e-pub ahead of print date: 7 December 2010
Published date: August 2011
Keywords: mTORC1, protein synthesis, cell signaling, transcription, cell growth, autophagy, metabolism
Organisations: Centre for Biological Sciences

Identifiers

Local EPrints ID: 350175
URI: http://eprints.soton.ac.uk/id/eprint/350175
ISSN: 1674-2788
PURE UUID: 14acc9ae-01a2-4929-9f3b-272e777a9b47

Catalogue record

Date deposited: 19 Mar 2013 11:15
Last modified: 16 Jul 2019 21:40

Export record

Altmetrics

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×