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Gene Review

MSG5  -  Msg5p

Saccharomyces cerevisiae S288c

Synonyms: N2480, Tyrosine-protein phosphatase MSG5, YNL053W, YNL2480W
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High impact information on MSG5


Biological context of MSG5

  • Throughout the range of pheromone concentrations sufficient to cause cell cycle arrest, Gpa1 stimulates adaptive mechanisms that are partially dependent on Msg5 and Mpt5 [3].

Anatomical context of MSG5

  • Consistent with a role of this phosphatase on cell wall physiology, cells lacking Msg5 displayed an increased sensitivity to the cell wall-interfering compound Congo Red. We have observed that the N-terminal non-catalytic region of this phosphatase was responsible for binding to the kinase domain of Slt2, the MAPK that operates in this pathway [4].

Physical interactions of MSG5

  • Truncation of the Kap104 cargo-binding domain blocked the effect of both Gpa1(E364K) and Msg5 on Fus3-GFP localization [5].

Enzymatic interactions of MSG5

  • Reciprocally, Slt2 phosphorylated Msg5 as a consequence of the activation of the cell integrity pathway [4].

Regulatory relationships of MSG5

  • POG1 confers alpha-factor resistance when overexpressed and enhances alpha-factor sensitivity when deleted in the background of an msg5 mutant [6].

Other interactions of MSG5

  • CLN2 overexpression represses Fus3 kinase activity, independently of the phosphatase Msg5 [7].
  • In addition, alternative use of translation initiation sites at MSG5 resulted in two protein forms that are functional on Slt2 and became equally phosphorylated following activation of this MAPK [4].
  • We have isolated a novel gene, POG1, whose promotion of recovery parallels that of the MAPK phosphatase Msg5 [6].
  • Accumulation of Fus3-GFP in the nuclei of stimulated cells was also inhibited by overexpression of either wild-type Gpa1, the E364K hyperadaptive mutant form of Gpa1, or the Msg5 dually specific phosphatase [5].


  1. Differential input by Ste5 scaffold and Msg5 phosphatase route a MAPK cascade to multiple outcomes. Andersson, J., Simpson, D.M., Qi, M., Wang, Y., Elion, E.A. EMBO J. (2004) [Pubmed]
  2. MSG5, a novel protein phosphatase promotes adaptation to pheromone response in S. cerevisiae. Doi, K., Gartner, A., Ammerer, G., Errede, B., Shinkawa, H., Sugimoto, K., Matsumoto, K. EMBO J. (1994) [Pubmed]
  3. The yeast pheromone-responsive G alpha protein stimulates recovery from chronic pheromone treatment by two mechanisms that are activated at distinct levels of stimulus. Zhou, J., Arora, M., Stone, D.E. Cell Biochem. Biophys. (1999) [Pubmed]
  4. Reciprocal regulation between Slt2 MAPK and isoforms of Msg5 dual-specificity protein phosphatase modulates the yeast cell integrity pathway. Flández, M., Cosano, I.C., Nombela, C., Martín, H., Molina, M. J. Biol. Chem. (2004) [Pubmed]
  5. Effect of the pheromone-responsive G(alpha) and phosphatase proteins of Saccharomyces cerevisiae on the subcellular localization of the Fus3 mitogen-activated protein kinase. Blackwell, E., Halatek, I.M., Kim, H.J., Ellicott, A.T., Obukhov, A.A., Stone, D.E. Mol. Cell. Biol. (2003) [Pubmed]
  6. POG1, a novel yeast gene, promotes recovery from pheromone arrest via the G1 cyclin CLN2. Leza, M.A., Elion, E.A. Genetics (1999) [Pubmed]
  7. Overexpression of the G1-cyclin gene CLN2 represses the mating pathway in Saccharomyces cerevisiae at the level of the MEKK Ste11. Wassmann, K., Ammerer, G. J. Biol. Chem. (1997) [Pubmed]
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