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Osmosensing and scaffolding functions of the oligomeric four-transmembrane domain osmosensor Sho1

Author

Listed:
  • Kazuo Tatebayashi

    (Institute of Medical Science, The University of Tokyo
    Graduate School of Science, The University of Tokyo)

  • Katsuyoshi Yamamoto

    (Institute of Medical Science, The University of Tokyo)

  • Miho Nagoya

    (Institute of Medical Science, The University of Tokyo)

  • Tomomi Takayama

    (Institute of Medical Science, The University of Tokyo
    Graduate School of Science, The University of Tokyo)

  • Akiko Nishimura

    (Institute of Medical Science, The University of Tokyo
    Graduate School of Science, The University of Tokyo)

  • Megumi Sakurai

    (Institute of Medical Science, The University of Tokyo
    Graduate School of Science, The University of Tokyo)

  • Takashi Momma

    (Institute of Medical Science, The University of Tokyo)

  • Haruo Saito

    (Institute of Medical Science, The University of Tokyo
    Graduate School of Science, The University of Tokyo)

Abstract

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 trimerizing at the TM2/TM3 interface. High external osmolarity induces structural changes in the Sho1 TM domains and Sho1 binding to the cytoplasmic adaptor protein Ste50, which leads to Hog1 activation. Besides its osmosensing function, the Sho1 oligomer serves as a scaffold. By binding to the TM proteins Opy2 and Hkr1 at the TM1/TM4 and TM2/TM3 interface, respectively, Sho1 forms a multi-component signalling complex that is essential for Hog1 activation. Our results illuminate how the four TM domains of Sho1 dictate the oligomer structure as well as its osmosensing and scaffolding functions.

Suggested Citation

  • Kazuo Tatebayashi & Katsuyoshi Yamamoto & Miho Nagoya & Tomomi Takayama & Akiko Nishimura & Megumi Sakurai & Takashi Momma & Haruo Saito, 2015. "Osmosensing and scaffolding functions of the oligomeric four-transmembrane domain osmosensor Sho1," Nature Communications, Nature, vol. 6(1), pages 1-15, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms7975
    DOI: 10.1038/ncomms7975
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