Nim1 kinase promotes mitosis by inactivating Wee1 tyrosine kinase

@article{Wu1993Nim1KP,
  title={Nim1 kinase promotes mitosis by inactivating Wee1 tyrosine kinase},
  author={Lin Wu and Paul Russell},
  journal={Nature},
  year={1993},
  volume={363},
  pages={738-741}
}
IN most species, including the fission yeast Schizosaccharomyces pombe, the Cdc2/cyclin B mitosis-inducing kinase is maintained in an inhibited state during interphase as a result of phosphorylation of a tyrosine residue in the ATP-binding region of Cdc2 (refs 1–3). This site is phosphorylated by Wee1 kinase4–9 and dephosphorylated by Cdc25 phosphatase10–15. In fission yeast an additional element of the G2/M control Nim1/Cdr1 kinase, has been identified which functions as a potent mitotic… 
Roles of Wee1 and Nim1 protein kinases in regulating the switch from mitotic division to sexual development in Schizosaccharomyces pombe
TLDR
It is reported here that Wee1 activity is also important for mating, and findings indicate that Wee 1 and Rum1 act jointly to inhibit Cdc2 and promote sexual development in nitrogen-starved cells.
The protein kinase Cdr2, related to Nim1/Cdr1 mitotic inducer, regulates the onset of mitosis in fission yeast.
TLDR
It is described that a synthetic lethal genetic screen has identified cdr2(+), a gene that has an important role in the mitotic control and is consistent with a model in which Cdr2 negatively regulates Wee1.
Mechanism for inactivation of the mitotic inhibitory kinase Wee1 at M phase
TLDR
Xenopus egg and extract systems are used to show that the kinase activity of Xenopus somatic Wee1 (XeWee1B) is regulated by its N-terminal, small, well conserved region, termed here the Wee-box, and provide important insights into the mechanism of Wee1 inactivation at M phase.
A mechanism for how Cdr1/Nim1 kinase promotes mitotic entry by inhibiting Wee1
TLDR
It is shown that both Cdr1 and Cdr2 promote Wee1 phosphorylation in cells, but only Cdr3 inhibits Wee1 kinase activity, and a two-step model for inhibition of Wee1 by Cdr 1 and CDR2 at nodes is proposed.
A mechanism for how Cdr1/Nim1 kinase promotes mitotic entry by inhibiting Wee1
TLDR
It is shown that both Cdr1 and Cdr2 promote Wee1 phosphorylation in cells, but only Cdr3 inhibits Wee1 kinase activity, and a two-step model for inhibition of Wee1 by Cdr 1 and CDR2 at nodes is proposed.
Nif1, a novel mitotic inhibitor in Schizosaccharomyces pombe
TLDR
Observations strongly suggest that Nif1 negatively regulates the onset of mitosis by a novel mechanism, namely inhibiting Nim1 kinase.
Fission Yeast Receptor of Activated C Kinase (RACK1) Ortholog Cpc2 Regulates Mitotic Commitment through Wee1 Kinase*
TLDR
The results suggest that in fission yeast Cpc2/RACK1 positively regulates from the ribosome the mitotic onset by modulating both the protein levels and the activity of Wee1, a novel mechanism of translational control of cell cycle progression.
Slm9, a novel nuclear protein involved in mitotic control in fission yeast.
TLDR
The synthetic lethal mutants, slm9, encodes a novel protein of 807 amino acids that is most similar to Hir2, the histone gene regulator in budding yeast, and is defective in recovery from G(1) arrest after nitrogen starvation.
Cell-cycle control linked to extracellular environment by MAP kinase pathway in fission yeast
TLDR
It is reported here that a fission yeast MAP kinase pathway links the cell-cycle G2/M control with changes in the extracellular environment that affect cell physiology.
Evidence for a mammalian Nim1-like kinase pathway acting at the G0-1/S transition.
TLDR
Examination of the effect of Nim1 expression on the control of the mammalian cell cycle using a plasmid microinjection approach provides evidence for the existence of a Nim1-like kinase pathway acting at the G0-1/S transition in human cells.
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References

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Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15.
TLDR
It is conclusively prove that Wee1 kinases inhibit mitosis by directly phosphorylating p34cdc2 on Tyr15, and strongly indicate that human cells have independent kinase pathways directing the two inhibitor phosphorylations of p34CDc2.
Inactivation of the p34cdc2-cyclin B complex by the human WEE1 tyrosine kinase.
TLDR
Results indicate that the product of the WEE1Hu gene directly regulates the p34cdc2-cyclin B complex in human cells and that a kinase other than that encoded by WEE2Hu phosphorylates p34CDc2 on threonine 14.
Fission yeast p107wee1 mitotic inhibitor is a tyrosine/serine kinase
TLDR
The wee1+ gene product is representative of a novel class of protein kinase that phosphorylates both serine and tyrosine residues, and also phosphorylate an exogenous substrate, angiotensin II, on tyosine.
p80cdc25 mitotic inducer is the tyrosine phosphatase that activates p34cdc2 kinase in fission yeast.
TLDR
The data indicate that cDC25 proteins define a novel subclass of eukaryotic PTPases, and strongly argue that cdc25 proteins directly dephosphorylate and activate p34cdc2 kinase to induce M‐phase.
Dephosphorylation and activation of a p34cdc2/cyclin B complex in vitro by human CDC25 protein
TLDR
It is proposed that the cdc25+ gene product directly activates the p34cdc2–cyclin B complex, and the purified bacterially expressed product of the human homologue of the fission yeast cdc 25+ gene7 (p54CDC25H) triggers p34CDc2 dephosphorylation and activates HI histone kinase activity in this preparation.
Wee1 +-like gene in human cells
TLDR
It is reported here that overexpression of WEE1Hu in fission yeast generates very elongated cells as a result of inhibition of the G2-M transition in the cell cycle.
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