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Gene Review

SHO1  -  Sho1p

Saccharomyces cerevisiae S288c

Synonyms: High osmolarity signaling protein SHO1, Osmosensor SHO1, SSU81, Suppressor of SUA8-1 mutation, Synthetic high osmolarity-sensitive protein 1, ...
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Disease relevance of SHO1

  • In this work, we show that the Hog1 MAPK is also activated by heat stress and that Sho1, previously identified as a membrane-bound osmosensor, is required for heat stress activation of Hog1 [1].

High impact information on SHO1

  • Alternatively, Pbs2p was activated by a mechanism that involves the binding of its amino terminal proline-rich motif to the Src homology 3 (SH3) domain of a putative transmembrane osmosensor Sho1p [2].
  • Msb2 is localized to polarized sites on the cell surface and interacts with Cdc42 and with the osmosensor for the high osmolarity glycerol response (HOG) pathway, Sho1 [3].
  • Taken together, our data suggest that Msb2 is a signaling mucin that interacts with general components, such as Cdc42 and Sho1, to promote their function in the FG pathway [3].
  • We suggest that Hog1p may prevent osmolarity-induced cross talk by inhibiting Sho1p, perhaps as part of a feedback control on the HOG pathway [4].
  • Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast [5].

Biological context of SHO1


Anatomical context of SHO1


Associations of SHO1 with chemical compounds

  • Dimethyl sulfoxide (DMSO) treatment, which rigidifies the cell membrane, also activates the HOG pathway in both SLN1 branch- and SHO1 branch-dependent manners [13].
  • Because loss of pheromone response pathway components leads to a synthetic growth defect in mannose utilization/protein glycosylation mutants, we suggest that the Sho1 --> Ste12 pathway contributes to maintenance of cell wall integrity in vegetative cells [6].

Physical interactions of SHO1

  • Pbs2p requires its Pro-rich motif for binding to the Src-homology3 (SH3) domain of Sho1p, but PbsB lacks a typical Pro-rich motif [14].
  • Hkr1 and Msb2 individually form a complex with Sho1, and, upon high external osmolarity stress, appear to induce Sho1 to generate an intracellular signal [15].

Regulatory relationships of SHO1

  • The cell fusion defect associated with fus1Delta mutants is suppressed by a sho1Delta deletion allele, suggesting that Fus1p negatively regulates Sho1p signaling to ensure efficient cell fusion [16].

Other interactions of SHO1

  • Finally, we have found that pseudohyphal growth exhibited by wild-type (HOG1) strains depends on SHO1, suggesting that Sho1p may be a receptor that feeds into the pseudohyphal growth pathway [4].
  • One of these proteins, Sho1, utilizes the MAP kinase kinase kinase Ste11 to activate Pbs2 [7].
  • A third osmosensing branch in Saccharomyces cerevisiae requires the Msb2 protein and functions in parallel with the Sho1 branch [7].
  • The yeast high osmolarity glycerol (HOG) signaling pathway can be activated by either of the two upstream pathways, termed the SHO1 and SLN1 branches [17].
  • Interestingly, these two Ste50p-SAM mutants were associated with increased activation of the mating and filamentous-growth pathways, but a reduction in the SHO1-dependent growth response to hyperosmolarity, relative to the wild-type Ste50p [18].

Analytical, diagnostic and therapeutic context of SHO1


  1. Heat stress activates the yeast high-osmolarity glycerol mitogen-activated protein kinase pathway, and protein tyrosine phosphatases are essential under heat stress. Winkler, A., Arkind, C., Mattison, C.P., Burkholder, A., Knoche, K., Ota, I. Eukaryotic Cell (2002) [Pubmed]
  2. Activation of yeast PBS2 MAPKK by MAPKKKs or by binding of an SH3-containing osmosensor. Maeda, T., Takekawa, M., Saito, H. Science (1995) [Pubmed]
  3. A signaling mucin at the head of the Cdc42- and MAPK-dependent filamentous growth pathway in yeast. Cullen, P.J., Sabbagh, W., Graham, E., Irick, M.M., van Olden, E.K., Neal, C., Delrow, J., Bardwell, L., Sprague, G.F. Genes Dev. (2004) [Pubmed]
  4. The Hog1 MAPK prevents cross talk between the HOG and pheromone response MAPK pathways in Saccharomyces cerevisiae. O'Rourke, S.M., Herskowitz, I. Genes Dev. (1998) [Pubmed]
  5. Protein-protein interaction affinity plays a crucial role in controlling the Sho1p-mediated signal transduction pathway in yeast. Marles, J.A., Dahesh, S., Haynes, J., Andrews, B.J., Davidson, A.R. Mol. Cell (2004) [Pubmed]
  6. Defects in protein glycosylation cause SHO1-dependent activation of a STE12 signaling pathway in yeast. Cullen, P.J., Schultz, J., Horecka, J., Stevenson, B.J., Jigami, Y., Sprague, G.F. Genetics (2000) [Pubmed]
  7. A third osmosensing branch in Saccharomyces cerevisiae requires the Msb2 protein and functions in parallel with the Sho1 branch. O'Rourke, S.M., Herskowitz, I. Mol. Cell. Biol. (2002) [Pubmed]
  8. The Saccharomyces cerevisiae Sln1p-Ssk1p two-component system mediates response to oxidative stress and in an oxidant-specific fashion. Singh, K.K. Free Radic. Biol. Med. (2000) [Pubmed]
  9. Candidate osmosensors from Candida utilis and Kluyveromyces lactis: structural and functional homology to the Sho1p putative osmosensor from Saccharomyces cerevisiae. Siderius, M., Kolen, C.P., van Heerikhuizen, H., Mager, W.H. Biochim. Biophys. Acta (2000) [Pubmed]
  10. The Sho1 adaptor protein links oxidative stress to morphogenesis and cell wall biosynthesis in the fungal pathogen Candida albicans. Román, E., Nombela, C., Pla, J. Mol. Cell. Biol. (2005) [Pubmed]
  11. Yeast Cdc42 GTPase and Ste20 PAK-like kinase regulate Sho1-dependent activation of the Hog1 MAPK pathway. Raitt, D.C., Posas, F., Saito, H. EMBO J. (2000) [Pubmed]
  12. Polarized localization of yeast Pbs2 depends on osmostress, the membrane protein Sho1 and Cdc42. Reiser, V., Salah, S.M., Ammerer, G. Nat. Cell Biol. (2000) [Pubmed]
  13. Activation of the HOG Pathway upon Cold Stress in Saccharomyces cerevisiae. Hayashi, M., Maeda, T. J. Biochem. (2006) [Pubmed]
  14. Aspergillus nidulans HOG pathway is activated only by two-component signalling pathway in response to osmotic stress. Furukawa, K., Hoshi, Y., Maeda, T., Nakajima, T., Abe, K. Mol. Microbiol. (2005) [Pubmed]
  15. Transmembrane mucins Hkr1 and Msb2 are putative osmosensors in the SHO1 branch of yeast HOG pathway. Tatebayashi, K., Tanaka, K., Yang, H.Y., Yamamoto, K., Matsushita, Y., Tomida, T., Imai, M., Saito, H. EMBO J. (2007) [Pubmed]
  16. Fus1p interacts with components of the Hog1p mitogen-activated protein kinase and Cdc42p morphogenesis signaling pathways to control cell fusion during yeast mating. Nelson, B., Parsons, A.B., Evangelista, M., Schaefer, K., Kennedy, K., Ritchie, S., Petryshen, T.L., Boone, C. Genetics (2004) [Pubmed]
  17. Adaptor functions of Cdc42, Ste50, and Sho1 in the yeast osmoregulatory HOG MAPK pathway. Tatebayashi, K., Yamamoto, K., Tanaka, K., Tomida, T., Maruoka, T., Kasukawa, E., Saito, H. EMBO J. (2006) [Pubmed]
  18. Mutations in the SAM domain of STE50 differentially influence the MAPK-mediated pathways for mating, filamentous growth and osmotolerance in Saccharomyces cerevisiae. Jansen, G., Bühring, F., Hollenberg, C.P., Ramezani Rad, M. Mol. Genet. Genomics (2001) [Pubmed]
  19. Response of Saccharomyces cerevisiae to severe osmotic stress: evidence for a novel activation mechanism of the HOG MAP kinase pathway. Van Wuytswinkel, O., Reiser, V., Siderius, M., Kelders, M.C., Ammerer, G., Ruis, H., Mager, W.H. Mol. Microbiol. (2000) [Pubmed]
  20. Sequence, map position and genome organization of the RPL17B gene, encoding ribosomal protein L17b in Saccharomyces cerevisiae. Berroteran, R.W., Hampsey, M. Yeast (1995) [Pubmed]
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