TOR Target of Rapamycin
TOR, the Target of Rapamycin was discovered a little over ten years ago in a genetic screen in S. cerevisiae in search of mutants resistant to the cytostatic effects of the anti-mycotic, rapamycin. Since that time orthologues have been identified i
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Editors R.W. Compans, Atlanta/Georgia M.D. Cooper, Birmingham/Alabama H. Koprowski, Philadelphia/Pennsylvania F. Melchers, Basel • M.B.A. Oldstone, La Jolla/California S. Olsnes, Oslo - M. Potter, Bethesda/Maryland P.K. Vogt, La Iolla/Calitornia- H. Wagner, Munich
Springer Berlin Heidelberg New York Hong Kong London Milan Paris Tokyo
G. Thomas
D.M. Sabatini
M.N. Hall (Eds.)
TOR Target of Rapamycin With 49 Figures and 7 Tables
Springer
Georg e Thomas Friedrich-Miescher-In stitut e, Maulbe erstrasse 66, 4058 Basel, Switzerland e-mail: g th om as@fm i.ch
David M. Sabatin i, MD, PhD Whitehead Institute, 9 Camb rid ge Center, Cambridge, MA 02142, USA e-ma il: saba t in i@w i.m it.ed u
Michael N. Hall Biozentrum, University of Basel, Klingelbergstrasse 70, 4056 Basel, Switzerland e- m a il: M [email protected] Cover Illustration by Sonja Dam es: Structure of the terna ry complex consisting of FKBP12 (blue ribbon), rapamycin (red space fi lling representat ion), and the FRB doma in of human TOR (yellow ribbon). The figure is based on the crystal structure published by]. Choi, ]. Chen, S.L. Schreiber, and l- Clardy (1996, Science 273 : 239 -242, 'Structure of the FKBP12-Rapamy cin Complex Interacting w ith the Binding Doma in ofHuman FRAP'; PDB fi le: 1FAP).
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Preface
As the role of TOR continues to unfold, it is clear that this atypical protein kinase occupies a central role in eukaryotic biology as an energy and nutrient effector. It is also clear that with the advent of metazoans, the ancient signal transduction pathway in which TOR resides has been inte
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