Methionine Restriction Impairs Degradation of a Protein that Aberrantly Engages the Endoplasmic Reticulum Translocon.
Methionine Restriction Impairs Degradation of a Protein that Aberrantly Engages the Endoplasmic Reticulum Translocon.
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DOI:
10.17912/micropub.biology.001021
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发表时间:
2023
影响因子:
--
通讯作者:
Rubenstein, Eric M
中科院分区:
文献类型:
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作者:
Runnebohm, Avery M;Indovina, Christopher J;Turk, Samantha M;Bailey, Connor G;Orchard, Cade J;Wade, Lauren;Overton, Danielle L;Snow, Brian J;Rubenstein, Eric M
Proteins that persistently engage endoplasmic reticulum (ER) translocons are degraded by multiple translocon quality control (TQC) mechanisms. In Saccharomyces cerevisiae , the model translocon-associated protein Deg1 -Sec62 is subject to ER-associated degradation (ERAD) by the Hrd1 ubiquitin ligase and, to a lesser extent, proteolysis mediated by the Ste24 protease. In a recent screen, we identified nine methionine-biosynthetic genes as candidate TQC regulators. Here, we found methionine restriction impairs Hrd1-independent Deg1 -Sec62 degradation. Beyond revealing methionine as a novel regulator of TQC, our results urge caution when working with laboratory yeast strains with auxotrophic mutations, often presumed not to influence cellular processes under investigation.