Disease relevance of wis1

• Heterothalic phh1 dsiruptant is phenotypically indistinguishable from wis1 deletion mutant, both displaying the same extent of partial sterility and enhanced sensitivity to a variety of stress [1].

High impact information on wis1

• We find that wis1-dependent induction of pyp2 mRNA is responsible for tyrosine dephosphorylation of Sty1 in vivo on prolonged exposure to osmotic stress [2].
• We find that sty2 is allelic to the wis1 MAP kinase kinase and that delta sty1 and delta wis1 cells are unable to grow in high osmolarity medium [2].
• The Schizosaccharomyces pombe wis1(+) gene is essential for cell survival under stress conditions [3].
• The wis1 protein kinase is a dosage-dependent regulator of mitosis in Schizosaccharomyces pombe [4].
• Increased levels of wis1+ expression cause mitotic initiation to occur at a reduced cell size [4].

Biological context of wis1

• Mutations in the spc1+ and wis1+ genes cause a G2 cell cycle delay that is exacerbated during stress [5].

Associations of wis1 with chemical compounds

• The wis1+ gene potentially encodes a 66 kDa protein with homology to the serine/threonine family of protein kinases. wis1+ plays an important role in the regulation of entry into mitosis, as it shares with cdc25+ and nim1+/cdr1+ the property of inducing mitosis in a dosage-dependent manner [4].
• In addition, glyoxalase I activity was increased in stress-activated protein kinase-deficient mutants (wis1 and spc1) [6].

Regulatory relationships of wis1

• We provide evidence that this osmotic induction of gpd1+ in S. pombe is under the control of a MAP-signaling pathway involving the wis1+ gene-product, which is a homologue of MAP-kinase kinases [7].

Other interactions of wis1

• Consistent with this, we have found that the wis1 mutation, which is defective in a MAP-kinase kinase of the pathway, suppresses the sts5 mutation [8].

References