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XB-ART-42502
Science 2010 Dec 17;3306011:1673-7. doi: 10.1126/science.1197048.
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The substrate of Greatwall kinase, Arpp19, controls mitosis by inhibiting protein phosphatase 2A.

Gharbi-Ayachi A , Labbé JC , Burgess A , Vigneron S , Strub JM , Brioudes E , Van-Dorsselaer A , Castro A , Lorca T .


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Initiation and maintenance of mitosis require the activation of protein kinase cyclin B-Cdc2 and the inhibition of protein phosphatase 2A (PP2A), which, respectively, phosphorylate and dephosphorylate mitotic substrates. The protein kinase Greatwall (Gwl) is required to maintain mitosis through PP2A inhibition. We describe how Gwl activation results in PP2A inhibition. We identified cyclic adenosine monophosphate-regulated phosphoprotein 19 (Arpp19) and α-Endosulfine as two substrates of Gwl that, when phosphorylated by this kinase, associate with and inhibit PP2A, thus promoting mitotic entry. Conversely, in the absence of Gwl activity, Arpp19 and α-Endosulfine are dephosphorylated and lose their capacity to bind and inhibit PP2A. Although both proteins can inhibit PP2A, endogenous Arpp19, but not α-Endosulfine, is responsible for PP2A inhibition at mitotic entry in Xenopus egg extracts.

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Species referenced: Xenopus laevis
Genes referenced: arpp19 cdk1 mastl ptpa

References :
Virshup, Cell biology. Enforcing the Greatwall in mitosis. 2010, Pubmed, Xenbase