Mammalian target of rapamycin (mTOR): Structure, signaling pathways and biological effects

Chen, H; Morris, MJ

Mammalian target of rapamycin (mTOR): Structure, signaling pathways and biological effects

Chen, H

Morris, MJ

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Publisher:: Nova Science Publishers
Publication Type:: Chapter
Citation:: Advances in Medicine and Biology Volume 68, 2013, 1, pp. 145 - 158
Issue Date:: 2013-01

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Field	Value	Language
dc.contributor.author	Chen, H https://orcid.org/0000-0001-6883-3752	en_US
dc.contributor.author	Morris, MJ	en_US
dc.contributor.editor	Berhardt, LV	en_US
dc.date.issued	2013-01	en_US
dc.identifier.citation	Advances in Medicine and Biology Volume 68, 2013, 1, pp. 145 - 158	en_US
dc.identifier.isbn	978-1-62618-806-8	en_US
dc.identifier.uri	http://hdl.handle.net/10453/27617
dc.description.abstract	The mammalian target of rapamycin (mTOR) is a highly conserved member of the phosphoinositide 3-kinase (PI3K) related kinase protien family and functions as a cellular sensor of changes in ambient glucose and amino acid levels; critical for cellular proliferation and differentiation. There are two multiprotein complexes of mTOR signalling components, as mTOR complex 1 (mTORC1) and mTORC2. Only mTORC1 appears to be nutrient dependent. In response to low intracellular energy availability, mTORC1 stabilizes and reduces the activity of mTOR. On the other hand, conditions of nutrient abundance promote its activity. However, such mechanisms have only been reported in either cell line models or lean animals; and hence their application to human states is yet to be determined.	en_US
dc.publisher	Nova Science Publishers	en_US
dc.relation.ispartof	Advances in Medicine and Biology Volume 68	en_US
dc.title	Mammalian target of rapamycin (mTOR): Structure, signaling pathways and biological effects	en_US
dc.type	Chapter
utslib.location	New York	en_US
utslib.for	100401 Gene and Molecular Therapy	en_US
utslib.for	111103 Nutritional Physiology	en_US
utslib.citation.edition	1	en_US
dc.location.activity	St Paul, MN
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
pubs.organisational-group	/University of Technology Sydney/Strength - CHT - Health Technologies
utslib.copyright.status	open_access
pubs.consider-herdc	true	en_US
pubs.edition	1	en_US
pubs.place-of-publication	New York	en_US

Abstract:

The mammalian target of rapamycin (mTOR) is a highly conserved member of the phosphoinositide 3-kinase (PI3K) related kinase protien family and functions as a cellular sensor of changes in ambient glucose and amino acid levels; critical for cellular proliferation and differentiation. There are two multiprotein complexes of mTOR signalling components, as mTOR complex 1 (mTORC1) and mTORC2. Only mTORC1 appears to be nutrient dependent. In response to low intracellular energy availability, mTORC1 stabilizes and reduces the activity of mTOR. On the other hand, conditions of nutrient abundance promote its activity. However, such mechanisms have only been reported in either cell line models or lean animals; and hence their application to human states is yet to be determined.

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http://hdl.handle.net/10453/27617