The Switch I Region of Rheb Is Critical for Its Interaction with FKBP38
Copyright policy )The Switch I Region of Rheb Is Critical for Its Interaction with FKBP38
The Ras-like small GTPase Rheb is an upstream activator of the mammalian target of rapamycin (mTOR). It has recently been shown that Rheb activates mTOR by binding to its endogenous inhibitor FKBP38 and preventing it from association with mTOR. The interaction of Rheb with FKBP38 is controlled by its guanine nucleotide binding states, which are responsive to growth factor and amino acid conditions. In this study, we show that Rheb interacts with FKBP38 through a section within its switch I region that is equivalent to the effector domain of other Ras-like small GTPases. We find that the ability for Rheb to interact with FKBP38 correlates with its activity for mTOR activation. Our findings suggest that FKBP38 is a bona fide effector of Rheb and that the ability to interact with FKBP38 is important for Rheb as an activator of mTOR.
- University of Pittsburgh United States
- Southern Medical University China (People's Republic of)
Guanine, TOR Serine-Threonine Kinases, Neuropeptides, Proteins, Mechanistic Target of Rapamycin Complex 1, GTP Phosphohydrolases, Protein Structure, Tertiary, Tacrolimus Binding Proteins, Cytosol, Microscopy, Fluorescence, Multiprotein Complexes, Humans, Ras Homolog Enriched in Brain Protein, Protein Kinases, Gene Deletion, HeLa Cells, Monomeric GTP-Binding Proteins, Plasmids, Protein Binding, Transcription Factors
Guanine, TOR Serine-Threonine Kinases, Neuropeptides, Proteins, Mechanistic Target of Rapamycin Complex 1, GTP Phosphohydrolases, Protein Structure, Tertiary, Tacrolimus Binding Proteins, Cytosol, Microscopy, Fluorescence, Multiprotein Complexes, Humans, Ras Homolog Enriched in Brain Protein, Protein Kinases, Gene Deletion, HeLa Cells, Monomeric GTP-Binding Proteins, Plasmids, Protein Binding, Transcription Factors
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