Article
Osmosensing and scaffolding functions of the oligomeric four-transmembrane domain osmosensor Sho1.
Nature communications - 21 Apr 2015
Tatebayashi Kazuo, Yamamoto Katsuyoshi, Nagoya Miho, Takayama Tomomi, Nishimura Akiko, Sakurai Megumi, Momma Takashi, Saito Haruo
Abstract excerpt
The yeast high osmolarity glycerol (HOG) pathway activates the Hog1 MAP kinase, which coordinates adaptation to high osmolarity conditions. Here we demonstrate that the four-transmembrane (TM) domain protein Sho1 is an osmosensor in the HKR1 sub-branch of the HOG pathway. Crosslinking studies indicate that Sho1 forms planar oligomers of the dimers-of-trimers architecture by dimerizing at the TM1/TM4 interface and...
Topics
- Adaptor Proteins, Signal Transducing
- Gene Expression Regulation, Fungal
- Membrane Proteins
- Mutation
- Osmotic Pressure
- Plasmids
- Protein Binding
- Protein Structure, Tertiary
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins