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J. Biol. Chem., Vol. 269, Issue 51, 32027-32030, Dec, 1994
R Stan, MM McLaughlin, R Cafferkey, RK Johnson, M Rosenberg and GP Livi
The yeast TOR1 and TOR2 proteins were previously discovered as putative
targets of the immunosuppressive drug rapamycin. Although their cellular
function is unknown, they are predicted to be at least 215 kDa in size and
possess a C-terminal phosphatidylinositol (PI) kinase- related domain. We
previously identified a conserved Ser residue, within the PI kinase-related
domain of both yeast TOR proteins (Ser1972 in TOR1; Ser1975 in TOR2), as
being the site of missense mutations conferring dominant rapamycin
resistance. The Ser1972/1975 residue of yeast TOR is conserved in mammalian
TOR homologs. One possibility is that this residue is critical for a direct
interaction between TOR and the FKBP12-rapamycin complex. There is very
recent biochemical evidence for an interaction between mammalian TOR and
FKBP12-rapamycin (Brown, E. J., Albers, M. W., Shin, T. B., Ichikawa, K.,
Keith, C. T., Lane, W. S., and Schreiber, S. L. (1994) Nature 369, 756-758;
Sabatini, D. M., Erdjument-Bromage, H., Lui, M., Tempst, P., and Snyder, S.
H. (1994) Cell 78, 35-43). Using the yeast two-hybrid system, we now have
obtained genetic proof of a physical interaction between FKBP12- rapamycin
and TOR and have demonstrated that this interaction requires the conserved
Ser residue. We have found that a small fragment of wild- type yeast TOR2
spanning Ser1975 is capable of interacting with human FKBP12 in the
presence of rapamycin, whereas an Arg1975 mutant fails to interact. This
effect is dependent upon rapamycin and is antagonized by FK506.
Interaction between FKBP12-rapamycin and TOR involves a conserved serine residue
Department of Biochemistry, Robert Wood Johnson Medical School, University of Medicine and Dentistry of New Jersey, Piscataway 08854.
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