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- W2034251131 abstract "When unfolded proteins accumulate in the endoplasmic reticulum (ER) causing ER stress, the unfolded protein response (UPR) responds rapidly to induce a transcriptional program that functions to alleviate the stress. However, under extreme conditions, when UPR activation is not sufficient to alleviate ER stress, the stress may persist long term. Very little is known about how the cell responds to persistent ER stress that is not resolved by the immediate activation of the UPR. We show that Hog1 MAP kinase becomes phosphorylated during the late stage of ER stress and helps the ER regain homeostasis. Although Hog1 is well known to function in osmotic stress and cell wall integrity pathways, we show that the activation mechanism for Hog1 during ER stress is distinct from both of these pathways. During late stage ER stress, upon phosphorylation, Hog1 translocates into the nucleus and regulates gene expression. Subsequently, Hog1 returns to the cytoplasm, where its phosphorylation levels remain high. From its cytoplasmic location, Hog1 contributes to the activation of autophagy by enhancing the stability of Atg8, a critical autophagy protein. Thus, Hog1 coordinates a multifaceted response to persistent ER stress." @default.
- W2034251131 created "2016-06-24" @default.
- W2034251131 creator A5004842583 @default.
- W2034251131 creator A5030069081 @default.
- W2034251131 creator A5069025755 @default.
- W2034251131 date "2010-06-01" @default.
- W2034251131 modified "2023-10-17" @default.
- W2034251131 title "Late Phase of the Endoplasmic Reticulum Stress Response Pathway Is Regulated by Hog1 MAP Kinase" @default.
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- W2034251131 doi "https://doi.org/10.1074/jbc.m109.084681" @default.
- W2034251131 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2878519" @default.
- W2034251131 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20382742" @default.
- W2034251131 hasPublicationYear "2010" @default.
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