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The Lst1-Sec23 complex helps sort important proteins into tiny bubbles called vesicles, which move from the endoplasmic reticulum (ER) to another part of the cell called the Golgi.
When proteins are not shaped correctly, they get stuck in the ER and are destroyed instead of moving on.
Scientists discovered that Lst1-Sec23 also helps get rid of damaged parts of the ER through a process called ER-phagy, which is important for keeping the cell healthy and working well.
Article Abstract
The COPII-cargo adaptor complex Lst1-Sec23 selectively sorts proteins into vesicles that bud from the endoplasmic reticulum (ER) and traffic to the Golgi. Improperly folded proteins are prevented from exiting the ER and are degraded. ER-phagy is an autophagic degradation pathway that uses ER-resident receptors. Working in yeast, we found an unexpected role for Lst1-Sec23 in ER-phagy that was independent from its function in secretion. Up-regulation of the stress-inducible ER-phagy receptor Atg40 induced the association of Lst1-Sec23 with Atg40 at distinct ER domains to package ER into autophagosomes. Lst1-mediated ER-phagy played a vital role in maintaining cellular homeostasis by preventing the accumulation of an aggregation-prone protein in the ER. Lst1 function appears to be conserved because its mammalian homolog, SEC24C, was also required for ER-phagy.
