Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5852
pubmed:dateCreated
2007-11-9
pubmed:abstractText
The mammalian target of rapamycin, mTOR, is a central regulator of cell growth. Its activity is regulated by Rheb, a Ras-like small guanosine triphosphatase (GTPase), in response to growth factor stimulation and nutrient availability. We show that Rheb regulates mTOR through FKBP38, a member of the FK506-binding protein (FKBP) family that is structurally related to FKBP12. FKBP38 binds to mTOR and inhibits its activity in a manner similar to that of the FKBP12-rapamycin complex. Rheb interacts directly with FKBP38 and prevents its association with mTOR in a guanosine 5'-triphosphate (GTP)-dependent manner. Our findings suggest that FKBP38 is an endogenous inhibitor of mTOR, whose inhibitory activity is antagonized by Rheb in response to growth factor stimulation and nutrient availability.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids, http://linkedlifedata.com/resource/pubmed/chemical/Culture Media, http://linkedlifedata.com/resource/pubmed/chemical/FKBP8 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Insulin, http://linkedlifedata.com/resource/pubmed/chemical/Intercellular Signaling Peptides..., http://linkedlifedata.com/resource/pubmed/chemical/MTOR protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Monomeric GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Mutant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides, http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RHEB protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sirolimus, http://linkedlifedata.com/resource/pubmed/chemical/TOR Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Tacrolimus Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/mTORC1 complex, human
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1095-9203
pubmed:author
pubmed:issnType
Electronic
pubmed:day
9
pubmed:volume
318
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
977-80
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:17991864-Amino Acids, pubmed-meshheading:17991864-Cell Line, pubmed-meshheading:17991864-Culture Media, pubmed-meshheading:17991864-Guanosine Triphosphate, pubmed-meshheading:17991864-Humans, pubmed-meshheading:17991864-Insulin, pubmed-meshheading:17991864-Intercellular Signaling Peptides and Proteins, pubmed-meshheading:17991864-Monomeric GTP-Binding Proteins, pubmed-meshheading:17991864-Mutant Proteins, pubmed-meshheading:17991864-Neuropeptides, pubmed-meshheading:17991864-Phosphorylation, pubmed-meshheading:17991864-Protein Binding, pubmed-meshheading:17991864-Protein Kinases, pubmed-meshheading:17991864-Protein Structure, Tertiary, pubmed-meshheading:17991864-Proteins, pubmed-meshheading:17991864-Recombinant Proteins, pubmed-meshheading:17991864-Serum, pubmed-meshheading:17991864-Signal Transduction, pubmed-meshheading:17991864-Sirolimus, pubmed-meshheading:17991864-TOR Serine-Threonine Kinases, pubmed-meshheading:17991864-Tacrolimus Binding Proteins, pubmed-meshheading:17991864-Transcription Factors
pubmed:year
2007
pubmed:articleTitle
Rheb activates mTOR by antagonizing its endogenous inhibitor, FKBP38.
pubmed:affiliation
Department of Pharmacology, University of Pittsburgh School of Medicine, E1357 Biomedical Science Tower, 200 Lothrop Street, Pittsburgh, PA 15213, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural