TY  - GEN
T1  - Endoplasmic reticulum stress-regulated degradation of a translocon-associated protein is independent of integrated stress response transcription factor Gcn4p
AU  - Richards, Kyle A
AU  - Rubenstein, Eric M
DO  - 10.17912/micropub.biology.000239
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000239/
AB  - Most eukaryotic proteins that reside in the secretory pathway or that are released to the extracellular space cross the endoplasmic reticulum (ER) membrane by passing through the Sec61p translocon channel (Lang et al. 2017). Arrested translocation prevents the movement of other proteins and impairs cellular fitness (Izawa et al. 2012; Ast et al. 2016). Eukaryotes have evolved multiple quality control mechanisms to degrade proteins that aberrantly and persistently engage the translocon. Proteins that stall in the Saccharomyces cerevisiae translocon are targeted for proteasomal degradation by the Hrd1p (Rubenstein et al. 2012) or Ltn1p/Rkr1p (Crowder et al. 2015) ubiquitin ligases or cleaved by the Ste24p protease (Ast et al. 2016). These mechanisms have been intensively investigated in yeast and are likely conserved in mammalian systems (Fisher et al. 2011; von der Malsburg et al. 2015; Ast et al. 2016).
PY  - 2020
JO  - microPublication Biology
ER  -