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Editorial
. 2015 Nov 3;6(34):35147-8.
doi: 10.18632/oncotarget.5903.

Lysosomal mTORC2/PHLPP1/Akt axis: a new point of control of chaperone-mediated autophagy

Esperanza Arias  1
Affiliations
Editorial

Lysosomal mTORC2/PHLPP1/Akt axis: a new point of control of chaperone-mediated autophagy

Esperanza Arias. Oncotarget. .
No abstract available

Keywords: cell signaling; kinase; lysosomes; membrane proteins; phosphatase.

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Figures

Figure 1
Figure 1. Chaperone-mediated autophagy activity is regulated by the phosphorylation state of lysosomal Akt
Phosphorylation of lysosome-associated Akt by mTORC2 represses CMA activation by negatively regulating the assembly of LAMP-2A into the CMA translocation complex, in part through phosphorylation of GFAP. Activation of CMA in response to stress is attained by the recruitment to lysosomes of the phosphatase PHLPP1 (that dephosphorylates Akt) and the GTPase Rac1 (that stabilizes PHLPP1 at the membrane). Reduced Akt activity enhances CMA by increasing the stability of the CMA translocation complex at the lysosomal membrane.
See this image and copyright information in PMC

References

    1. Arias E, et al. Current Opinion in Cell Biology. 2011;23:184–189. - PMC - PubMed
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    1. Arias E, et al. Mol Cell. 2015;59:270–284. - PMC - PubMed

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