2010
DOI: 10.1074/jbc.m109.063578
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The Activity of Yeast Hog1 MAPK Is Required during Endoplasmic Reticulum Stress Induced by Tunicamycin Exposure

Abstract: Accumulation of unfolded proteins in the endoplasmic reticulum (ER) triggers the so-called unfolded protein response (UPR), a conserved signaling pathway that drives the transcription of genes such as chaperones and folding enzymes. Nevertheless, the activity of the UPR accounts only for a part of the gene expression program activated upon ER stress. Moreover, the mechanism(s) for how cells adapt and survive to this stress are largely unknown. Here, we show that the yeast high osmolarity glycerol (HOG) pathway… Show more

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Cited by 57 publications
(76 citation statements)
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“…KCl, 1 mM MgSO 4 ), and protein extracts were prepared and processed for galactosidase activity as previously described [106]. One unit is defined as the amount of enzyme that is able to convert 1 nmol of the substrate o-NPG per min under the assay conditions.…”
Section: Preparation Of Protein Extracts and Western Blot Analysismentioning
confidence: 99%
“…KCl, 1 mM MgSO 4 ), and protein extracts were prepared and processed for galactosidase activity as previously described [106]. One unit is defined as the amount of enzyme that is able to convert 1 nmol of the substrate o-NPG per min under the assay conditions.…”
Section: Preparation Of Protein Extracts and Western Blot Analysismentioning
confidence: 99%
“…Tunicamycin also induces cell wall stress, which may provide an explanation for why certain genes implicated in cell wall biogenesis were found to be upregulated during the UPR in tunicamycin-treated S. cerevisiae and C. albicans cells 11 , 58 , 60 . In contrast, the loss of Ire1 alone in C. glabrata did not confer a cell wall-defective phenotype, and the upregulation of some cell wall-related genes upon tunicamycin exposure was mainly dependent on calcineurin, but not Ire1 12 .…”
Section: Diversity In Ire1-dependent Stress Response Mechanisms Betwementioning
confidence: 99%
“…Another likely explanation would be that inhibition of the kinase activity of the Hog1 for a longer time leads to protein misfolding and thereby induction of heat shock protein responses. Hog1 kinase activity has been shown required to provide a necessary function to cope with unfolded protein accumulation due to ER stress [49]. Considering the fact that Hog1 becomes activated upon a wide variety of environmental cues and is involved in transcription, translation, transport, as well as cell cycle adaptations in response to different conditions [23] [24] [29], these are all plausible scenarios.…”
Section: Hog1 Kinase Inhibitor Treatment Leads To Elevated Arsenite Imentioning
confidence: 99%