2011
DOI: 10.1016/j.devcel.2010.12.003
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Microautophagy of Cytosolic Proteins by Late Endosomes

Abstract: Summary Autophagy delivers cytosolic components to lysosomes for their degradation. The delivery of autophagic cargo to late endosomes for complete or partial degradation has also been described. In this report, we present evidence that distinct autophagic mechanisms control cytosolic protein delivery to late endosomes and identify a microautophagy-like process that delivers soluble cytosolic proteins to the vesicles of late endosomes/multivesicular bodies (MVB). This microautophagy-like process has selectivit… Show more

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Cited by 755 publications
(696 citation statements)
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References 26 publications
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“…Late endosomes (LE) also contribute to selective degradation of cytosolic proteins targeted to this compartment by hsc70 through a process known as endosomal microautophagy (e‐MI) (Sahu et al ., 2011; Uytterhoeven et al ., 2015). Using the same N2a cells expressing WT, A152T, and P301L tau, we analyzed changes in cellular levels of these forms of tau upon disrupting e‐MI.…”
Section: Resultsmentioning
confidence: 99%
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“…Late endosomes (LE) also contribute to selective degradation of cytosolic proteins targeted to this compartment by hsc70 through a process known as endosomal microautophagy (e‐MI) (Sahu et al ., 2011; Uytterhoeven et al ., 2015). Using the same N2a cells expressing WT, A152T, and P301L tau, we analyzed changes in cellular levels of these forms of tau upon disrupting e‐MI.…”
Section: Resultsmentioning
confidence: 99%
“…Using the same N2a cells expressing WT, A152T, and P301L tau, we analyzed changes in cellular levels of these forms of tau upon disrupting e‐MI. To that effect, we knocked down essential components of the endosomal sorting complex required for transport (ESCRT) (Sahu et al ., 2011). Contrary to WT tau, which accumulates in e‐MI‐defective cells, intracellular levels of A152T and P301L tau did not change in cells knocked down for Vps4, suggesting that both point mutations in tau compromise its ability to undergo degradation by this pathway (Fig.…”
Section: Resultsmentioning
confidence: 99%
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“…203 Recently, a microautophagy-like process involving HSPA8, called endosomal microautophagy, has been described in late endosomes/multivesicular bodies. 204 As in CMA, HSPA8 binds to KFERQ motif-containing proteins, but instead of binding to a lysosomal membrane receptor, the chaperone directly associates through electrostatic interaction with the phosphatidylserine moieties present in the lipid bilayer. Consequently, the protein substrate can be easily internalized and degraded through endosomal microautophagy Finally, recent studies have highlighted an involvement of HSPA8 in macroautophagy.…”
Section: Hspa8 and Autophagymentioning
confidence: 99%