Pharmacological Characterization Of Purified Recombinant Mtor FRB-Kinase Domain Using Fluorescence-Based Assays  

Oleh:

Reichling, Laurie J. ; Lebakken, Connie S. ; Riddle, Steven M. ; Vedvik, Kevin L. ; Robers, Matthew B. ; Kopp, Leisha M. ; Vogel, Kurt W.

Jenis: Article from Journal - ilmiah internasional
Dalam koleksi: Concurrent Engineering vol. 13 no. 3 (Sep. 2005), page 238-244.
Topik: FRAP1; mTOR; rapamycin; kinase; assay
Fulltext: 238.pdf (179.67KB)

Isi artikel

The mammalian target of rapamycin (mTOR) is a serine/threonine kinase involved in nutrient sensing and cell growth and is a validated target for oncology and immunosuppression. Two modes of direct small-molecule inhibition of mTOR activity are known: targeting of the kinase active site and a unique mode in which the small molecule rapamycin, in complex with FKBP12 (the 12-kDa FK506 binding protein), binds to the FRB (FKBP12/rapamycin binding) domain of mTOR and inhibits kinase activity through a poorly defined mechanism. To facilitate the study of these processes, the authors have expressed and purified a truncated version of mTOR that contains the FRB and kinase domains and have developed homogeneous fluorescence-based assays to study mTOR activity. They demonstrate the utility of these assays in studies of active sitedirected and FRB domain-directed mTOR inhibition. The results suggest that these assays can replace traditional radiometric or Western blot–based assays. (Journal of Biomolecular Screening 2008:238-244)

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