mTOR
signaling complex and pathway
The
mammalian Target Of Rapamycin
(mTOR) protein was discovered in studies into the mechanism
of action of rapamycin, a macrolide antibiotic produced by
a streptomyces species of bacteria. When rapamycin enters
mammalian cells it binds to a small protein called FKBP12
to create a drug-receptor complex that interacts with mTOR,
a large protein kinase related to PI3-kinase. Exactly how
FKBP12-rapamycin perturbs mTOR function is not known. mTOR
is evolutionarily conserved and integrates nutrient-and growth
factor-derived signals to control the cell growth machinery.
Within cells mTOR is part of a large protein complex that
includes several other components including raptor and GbL,
two novel proteins we have recently discovered. We seek to
understand how nutrients and growth factors regulate the mTOR
complex and to identify the functions of the different components
at the cell and organism levels. In addition, we are interested
in the potential roles of deregulated mTOR signaling in diabetes
and cancer. We have recently discovered that mTOR also exists
as part of distinct complex that contains mTOR and GbL but
instead of raptor the novel protein rictor. We are just starting
to understand rictor function.
| mTOR
and its associated proteins are at the center of many
inputs and outputs that regulate cell growth |
Links
relating to rapamycin (generic name: sirolimus; trade name:
rapamune)
|
