Selective autophagy represents the major quality control mechanism that ensures proper turnover of exhausted or harmful organelles, among them the endoplasmic reticulum (ER), which is fragmented and delivered to the lysosome for degradation via a specific type of autophagy called ER-phagy. The recent discovery of ER-resident proteins that bind to mammalian Atg8 proteins has revealed that the selective elimination of ER involves different receptors that are specific for different ER subdomains or ER stresses. FAM134B (also known as RETREG1) and RTN3 are reticulon-type proteins that are able to remodel the ER network and ensure the basal membrane turnover. SEC62 and CCPG1 are transmembrane ER receptors that function in response to ER stress signals. This task sharing reflects the complexity of the ER in terms of biological functions and morphology. In this Cell Science at a Glance article and the accompanying poster, we summarize the most recent findings about ER-phagy in yeast and in mammalian cells.

ER-phagy at a glance

Grumati, Paolo;
2018

Abstract

Selective autophagy represents the major quality control mechanism that ensures proper turnover of exhausted or harmful organelles, among them the endoplasmic reticulum (ER), which is fragmented and delivered to the lysosome for degradation via a specific type of autophagy called ER-phagy. The recent discovery of ER-resident proteins that bind to mammalian Atg8 proteins has revealed that the selective elimination of ER involves different receptors that are specific for different ER subdomains or ER stresses. FAM134B (also known as RETREG1) and RTN3 are reticulon-type proteins that are able to remodel the ER network and ensure the basal membrane turnover. SEC62 and CCPG1 are transmembrane ER receptors that function in response to ER stress signals. This task sharing reflects the complexity of the ER in terms of biological functions and morphology. In this Cell Science at a Glance article and the accompanying poster, we summarize the most recent findings about ER-phagy in yeast and in mammalian cells.
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11588/899985
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