Sphingolipids Regulate the Yeast High-Osmolarity Glycerol Response Pathway

Author:

Tanigawa Mirai1,Kihara Akio2,Terashima Minoru1,Takahara Terunao1,Maeda Tatsuya1

Affiliation:

1. Institute of Molecular and Cellular Biosciences, The University of Tokyo, Tokyo, Japan

2. Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan

Abstract

ABSTRACT The yeast high-osmolarity glycerol response (HOG) mitogen-activated protein (MAP) kinase pathway is activated in response to hyperosmotic stress via two independent osmosensing branches, the Sln1 branch and the Sho1 branch. While the mechanism by which the osmosensing machinery activates the downstream MAP kinase cascade has been well studied, the mechanism by which the machinery senses and responds to hyperosmotic stress remains to be clarified. Here we report that inhibition of the de novo sphingolipid synthesis pathway results in activation of the HOG pathway via both branches. Inhibition of ergosterol biosynthesis also induces activation of the HOG pathway. Sphingolipids and sterols are known to be tightly packed together in cell membranes to form partitioned domains called rafts. Raft-enriched detergent-resistant membranes (DRMs) contain both Sln1 and Sho1, and sphingolipid depletion and hyperosmotic stress have similar effects on the osmosensing machinery of the HOG pathway: dissociation of an Sln1-containing protein complex and elevated association of Sho1 with DRMs. These observations reveal the sphingolipid-mediated regulation of the osmosensing machinery of the HOG pathway.

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

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