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Vol. 14, Issue 3, 1204-1220, March 2003
Tor1p and Tor2p kinases, targets of the immune-suppressive
antibiotic rapamycin, are components of a highly conserved signaling network that couples nutrient availability and cell growth. To gain
insight into the molecular basis underlying Tor-dependent signaling, we
used cell fractionation and immunoaffinity chromatography to examine
the physical environment of Tor2p. We found that the majority of Tor2p
associates with a membrane-bound compartment along with at least four
other proteins, Avo1p-Avo3p and Lst8p. Using immunogold electron
microscopy, we observed that Tor2p, as well as Tor1p, localizes in
punctate clusters to regions adjacent to the plasma membrane and within
the cell interior, often in association with characteristic membranous
tracks. Cell fractionation, coimmunoprecipitation, and immunogold
electron microscopy experiments confirmed that Lst8 associates
with both Tor2p as well as Tor1p at these membranous sites. In
contrast, we find that Kog1, the yeast homologue of the mammalian Tor
regulatory protein Raptor, interacts preferentially with Tor1p. These
findings provide evidence for the existence of Tor signaling complexes
that contain distinct as well as overlapping components. That these
complexes colocalize to a membrane-bound compartment suggests an
intimate relationship between membrane-mediated signaling and Tor activity.
Section of Molecular and Cellular Biology
and Center for Genetics and Development, Division of Biological
Sciences, University of California, Davis, Davis, California 95616;
Department of Cell Biology, The Scripps
Research Institute, La Jolla, California 92037; and
§Integrated Imaging Center and Department of
Biology, Johns Hopkins University, Baltimore, Maryland 21218
Corresponding author: E-mail address:
tpowers{at}ucdavis.edu.
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