Hog1-Mediated Rds2 Phosphorylation Alters Glycerophospholipid Composition To Coordinate Osmotic Stress in .

Under stress conditions, Hog1 is required for cell survival through transiently phosphorylating downstream targets and reprogramming gene expression. Here, we report that Hog1 (Hog1) interacts with and phosphorylates Rds2, a zinc cluster transcription factor, in response to osmotic stress. Additionally, we found that deletion of led to decreases in cell growth and cell survival by 23.4% and 39.6%, respectively, at 1.5 M NaCl, compared with levels of the wild-type strain. This is attributed to significant downregulation of the expression levels of glycerophospholipid metabolism genes. As a result, the content of total glycerophospholipid decreased by 30.3%. Membrane integrity also decreased 47.6% in the Δ strain at 1.5 M NaCl. In contrast, overexpression of increased the cell growth and cell survival by 10.2% and 6.3%, respectively, owing to a significant increase in the total glycerophospholipid content and increased membrane integrity by 27.2% and 12.1%, respectively, at 1.5 M NaCl, compared with levels for the wild-type strain. However, a strain in which the gene encodes the replacement of Ser64 and Thr97 residues with alanines ( ), harboring a Rds2 protein that was not phosphorylated by Hog1, failed to promote glycerophospholipid metabolism and membrane integrity at 1.5 M NaCl. Thus, the above results demonstrate that Hog1-mediated Rds2 phosphorylation enhanced glycerophospholipid composition and membrane integrity to resist osmotic stress in This study explored the role of Hog1-mediated Rds2 phosphorylation in response to osmotic stress in Hog1 interacts with and phosphorylates Rds2, a zinc cluster transcription factor, under osmotic stress. Phosphorylated Rds2 plays an important role in increasing glycerophospholipid composition and membrane integrity, thereby enhancing cell growth and survival.