Abstract
Lysosomal mTORC2/PHLPP1/Akt axis: a new point of control of chaperone-mediated autophagy.
Highlights
Chaperone-mediated autophagy (CMA), a mechanism for degradation of cytosolic proteins in lysosomes, is one of the most selective types of autophagy in mammals [1]
Quite on the contrary, growing evidence supports coordinated functioning of the different autophagic pathways that co-exist in the cell and direct cross-talk between macroautophagy and CMA
In our search for signaling mechanisms that regulate CMA and that could participate in the autophagic crosstalk, we focused our attention on the mammalian target of rapamycin, a serine/ threonine kinase that serves as one of the main cellular nutritional sensors. mTOR senses and integrates different nutritional inputs, including growth factors, energy levels, cellular stress, and amino acids. mTOR is present in two distinct complexes, mTORC1 and mTORC2
Summary
Chaperone-mediated autophagy (CMA), a mechanism for degradation of cytosolic proteins in lysosomes, is one of the most selective types of autophagy in mammals [1]. Quite on the contrary, growing evidence supports coordinated functioning of the different autophagic pathways that co-exist in the cell and direct cross-talk between macroautophagy and CMA (both maximally activated in response to stress). Understanding the basis of this bi-directional cross-talk between macroautophagy and CMA becomes important, especially in pathological conditions with blockage of one of these autophagic pathways.
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