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Autophagy

ESCRTing proteins for microautophagy

Nature Reviews Molecular Cell Biology volume 12, pages 136–137 (2011)Cite this article

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To examine lysosome- and late endosome-meditated autophagy in dendritic cells, the authors assessed the presence in these structures of the cytosolic proteins glyceraldehyde-3-phosphate dehydrogenase (GAPDH), aldolase and cyclophilin. GAPDH and aldolase harbour a KFERQ-like motif that is recognized by HSC70, which unfolds targets for translocation into the lysosome by lysosome-associated membrane glycoprotein 2A (LAMP2A) during CMA. GAPDH and aldolase were present in CMA-active, but not CMA-inactive, lysosomes, whereas cyclophilin was present in both. All three proteins were present in late endosomes, in which rates of protein translocation and degradation were higher than those of lysosomes.

To determine whether macroautophagy delivers proteins to late endosomes, the authors blocked this process by knocking down autophagy-related 7 (ATG7). The level of cytosolic proteins was only marginally decreased in late endosomes isolated from ATG7-depleted cells, suggesting that macroautophagy is not the main pathway by which cytosolic proteins reach late endosomes. Knockdown of LAMP2A reduced the level of GAPDH and aldolase in CMA-active lysosomes but not in late endosomes, suggesting that the internalization of proteins into late endosomes is also not through CMA.

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ORIGINAL RESEARCH PAPER

  1. Sahu, R. et al. Microautophagy of cytosolic proteins by late endosomes. Dev. Cell 20, 131–139 (2011) Article

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  1. Katharine H. Wrighton
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Wrighton, K. ESCRTing proteins for microautophagy. Nat Rev Mol Cell Biol 12, 136–137 (2011). https://doi.org/10.1038/nrm3075

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