or ectopic expression of a fyve domain construct, which sequesters PI(3)P, blunts AA-induced mTOR Complex1 signaling ). AA activation of mTOR Complex1 increases growth through increased ribosome biogenesis and elevated rates of protein synthesis, while suppressing autophagy. Moreover, recent studies show AAs can directly mediate these responses by phosphorylation of IRS1 by S6K1 at specific sites residing at the amino and carboxy termini of IRS1, respectively. These observations are consistent with a potential role for hVps34 in distinct functions of early endosome signaling versus targeting of late endosomes to autophagic vesicles.
Molecular Mechanisms Linking Amino Acid The role of amino acids in liver protein metabolism Amino acids activate mTOR Complex1 via Ca2/CaM signaling MTor Signaling in Skeletal Muscle During Sepsis and Inflammation
Thesis grants for 2008
Dominican university of california senior thesis statement
In humans it is known that circulating AAs are often elevated in the obese and the insulin resistant state. Here we show 3d video compression thesis that AAs induce an increase in Ca2i, which acts to enhance the binding of Ca2/CaM to hVps34, resulting in increased PI(3)P levels and enhanced mTOR Complex1 signaling. The morbidity of obesity not only extends to diabetes and cardiovascular disease, but recently has been shown to be linked to 20 of cancer deaths. We have previously demonstrated that activation of S6K1 is associated with a Ca2-dependent shift of the kinase into a larger protein complex. A critical effector of nutrient signaling is the mTOR protein kinase, which exists in two distinct complexes. Given the ability of mTOR Complex1 to drive cell growth and to suppress autophagy, it will be critical to identify the mechanisms by which these two pathways interact at the cellular level. Consistent with such a model it was subsequently found that the ability Rheb to interact with mTOR Complex1 is inhibited in the absence of AAs. In contrast, AAs stimulate mTOR Complex1 activation through class 3 PI3K, or human vacuolar protein sorting 34 (hVps34) ).