Journal
BIOCHEMICAL JOURNAL
Volume 405, Issue -, Pages 513-522Publisher
PORTLAND PRESS LTD
DOI: 10.1042/BJ20070540
Keywords
cancer; mammalian target of rapamycin (mTOR); mTOR complex-2 (mTORC2); proline-rich repeat protein-5 (PRR-5); protein kinase; rapamycin-insensitive companion of mTOR (Rictor); protein observed with Rictor-1 (Protor)
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Funding
- MRC [MC_U127015387] Funding Source: UKRI
- Medical Research Council [MC_U127015387] Funding Source: researchfish
- Medical Research Council [MC_U127015387] Funding Source: Medline
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The mTOR (mammalian target of rapamycin) protein kinase is an important regulator of cell growth. Two complexes of mTOR have been identified: complex 1, consisting of mTOR-Raptor (regulatory associated protein of mTOR)-mLST8 (termed mT- ORC1), and complex 2, comprising mTOR-Rictor (rapamycinin-sensitive companion of mTOR)-mLST8-Sin1 (termed mTORC2). mTORC1 phosphorylates the p70 ribosomal S6K (S6 kinase) at its hydrophobic motif (Thr(389)), whereas mTORC2 phosphorylates PKB (protein kinase B) at its hydrophobic motif (Ser(473)). In the present study, we report that widely expressed isoforms of unstudied proteins termed Protor-1 (protein observed with Rictor-1) and Protor-2 interact with Rictor and are components of mTORC2. We demonstrate that immunoprecipitation of Protor-1 or Protor-2 results in the co-immunoprecipitation of other mTORC2 subunits, but not Raptor, a specific component of mTORC1. We show that detergents such as Triton X-100 or n-octylglucoside dissociate mTOR and mLST8 from a complex of Protor-1, Sin] and Rictor. We also provide evidence that Rictor regulates the expression of Protor-1, and that Protor-1 is not required for the assembly of other mTORC2 subunits into a complex. Protor-1 is a novel Rictor-binding subunit of mTORC2, but further work is required to establish its role.
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