mTOR Interacts with Raptor to Form a Nutrient-Sensitive Complex that Signals to the Cell Growth Machinery

mTOR/RAFT1/FRAP is the target of the immunosuppressive drug rapamycin and the central component of a nutrient- and hormone-sensitive signaling pathway that regulates cell growth. We report that mTOR forms a stoichiometric complex with raptor, an evolutionarily conserved protein with at least two rol...

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Published in	Cell Vol. 110; no. 2; pp. 163 - 175
Main Authors	Kim, Do-Hyung, Sarbassov, Dos D., Ali, Siraj M., King, Jessie E., Latek, Robert R., Erdjument-Bromage, Hediye, Tempst, Paul, Sabatini, David M.
Format	Journal Article
Language	English
Published	United States Elsevier Inc 26.07.2002
Subjects	Adaptor Proteins, Signal Transducing Amino Acid Sequence Binding Sites Carrier Proteins - metabolism Cell Division Cell Line, Transformed Cell Size Conserved Sequence Culture Media Evolution, Molecular Humans Molecular Sequence Data Phosphoproteins - metabolism Protein Kinases - metabolism Protein Structure, Tertiary Proteins - genetics Proteins - metabolism Regulatory-Associated Protein of mTOR Repetitive Sequences, Amino Acid Ribosomal Protein S6 Kinases - metabolism Signal Transduction Sirolimus - pharmacology TOR Serine-Threonine Kinases
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Abstract	mTOR/RAFT1/FRAP is the target of the immunosuppressive drug rapamycin and the central component of a nutrient- and hormone-sensitive signaling pathway that regulates cell growth. We report that mTOR forms a stoichiometric complex with raptor, an evolutionarily conserved protein with at least two roles in the mTOR pathway. Raptor has a positive role in nutrient-stimulated signaling to the downstream effector S6K1, maintenance of cell size, and mTOR protein expression. The association of raptor with mTOR also negatively regulates the mTOR kinase activity. Conditions that repress the pathway, such as nutrient deprivation and mitochondrial uncoupling, stabilize the mTOR-raptor association and inhibit mTOR kinase activity. We propose that raptor is a missing component of the mTOR pathway that through its association with mTOR regulates cell size in response to nutrient levels.
AbstractList	mTOR/RAFT1/FRAP is the target of the immunosuppressive drug rapamycin and the central component of a nutrient- and hormone-sensitive signaling pathway that regulates cell growth. We report that mTOR forms a stoichiometric complex with raptor, an evolutionarily conserved protein with at least two roles in the mTOR pathway. Raptor has a positive role in nutrient-stimulated signaling to the downstream effector S6K1, maintenance of cell size, and mTOR protein expression. The association of raptor with mTOR also negatively regulates the mTOR kinase activity. Conditions that repress the pathway, such as nutrient deprivation and mitochondrial uncoupling, stabilize the mTOR-raptor association and inhibit mTOR kinase activity. We propose that raptor is a missing component of the mTOR pathway that through its association with mTOR regulates cell size in response to nutrient levels.
Author	Sabatini, David M. Tempst, Paul Kim, Do-Hyung Latek, Robert R. King, Jessie E. Erdjument-Bromage, Hediye Sarbassov, Dos D. Ali, Siraj M.
Author_xml	– sequence: 1 givenname: Do-Hyung surname: Kim fullname: Kim, Do-Hyung organization: Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142 USA – sequence: 2 givenname: Dos D. surname: Sarbassov fullname: Sarbassov, Dos D. organization: Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142 USA – sequence: 3 givenname: Siraj M. surname: Ali fullname: Ali, Siraj M. organization: Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142 USA – sequence: 4 givenname: Jessie E. surname: King fullname: King, Jessie E. organization: Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142 USA – sequence: 5 givenname: Robert R. surname: Latek fullname: Latek, Robert R. organization: Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142 USA – sequence: 6 givenname: Hediye surname: Erdjument-Bromage fullname: Erdjument-Bromage, Hediye organization: Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021 USA – sequence: 7 givenname: Paul surname: Tempst fullname: Tempst, Paul organization: Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, NY 10021 USA – sequence: 8 givenname: David M. surname: Sabatini fullname: Sabatini, David M. email: sabatini@wi.mit.edu organization: Whitehead Institute for Biomedical Research, Nine Cambridge Center, Cambridge, MA 02142 USA
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/12150925$$D View this record in MEDLINE/PubMed
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Snippet	mTOR/RAFT1/FRAP is the target of the immunosuppressive drug rapamycin and the central component of a nutrient- and hormone-sensitive signaling pathway that...
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SubjectTerms	Adaptor Proteins, Signal Transducing Amino Acid Sequence Binding Sites Carrier Proteins - metabolism Cell Division Cell Line, Transformed Cell Size Conserved Sequence Culture Media Evolution, Molecular Humans Molecular Sequence Data Phosphoproteins - metabolism Protein Kinases - metabolism Protein Structure, Tertiary Proteins - genetics Proteins - metabolism Regulatory-Associated Protein of mTOR Repetitive Sequences, Amino Acid Ribosomal Protein S6 Kinases - metabolism Signal Transduction Sirolimus - pharmacology TOR Serine-Threonine Kinases
Title	mTOR Interacts with Raptor to Form a Nutrient-Sensitive Complex that Signals to the Cell Growth Machinery
URI	https://dx.doi.org/10.1016/S0092-8674(02)00808-5 https://www.ncbi.nlm.nih.gov/pubmed/12150925 https://search.proquest.com/docview/71968683
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