Data suggest Greatwall kinase (Gwl) associates with protein phosphatase 1 (PP1), particularly PP1gamma subunit, which mediates dephosphorylation of Gwl Ser-883; consistent with mitotic activation of Gwl, its association with PP1 is disrupted in mitotic cells; subunits PPP1R3B and PPP1R13L associate with Gwl; thus, PPP1R3B appears to act as cell cycle regulator in oocytes that functions by governing Gwl dephosphorylation. | Cell cycle-dependent regulation of Greatwall kinase by protein phosphatase 1 and regulatory subunit 3B. Ren D, Fisher LA, Zhao J, Wang L, Williams BC, Goldberg ML, Peng A., Free PMC Article | 07/8/2017 |
Full dephosphorylation of Gwl results in complete inactivation of Arpp19 and ENSA, and dephosphorylation of mitotic substrates. this feed-back loop irreversibly induces mitotic exit. | Greatwall dephosphorylation and inactivation upon mitotic exit is triggered by PP1. Ma S, Vigneron S, Robert P, Strub JM, Cianferani S, Castro A, Lorca T. | 12/31/2016 |
study provides evidence that PP1 targets the auto-phosphorylation site of Gwl, resulting in efficient Gwl inactivation; this step is necessary to facilitate subsequent complete dephosphorylation of Gwl by PP2A-B55 | Protein phosphatase 1 is essential for Greatwall inactivation at mitotic exit. Heim A, Konietzny A, Mayer TU., Free PMC Article | 08/20/2016 |
we showed that the Gwl nuclear localization is indispensable for the biochemical function of Gwl in promoting mitotic entry. | Regulation of Greatwall kinase by protein stabilization and nuclear localization. Yamamoto TM, Wang L, Fisher LA, Eckerdt FD, Peng A., Free PMC Article | 09/26/2015 |
PP2A-B55delta, Greatwall and ARPP19 are not only required for entry into meiotic divisions, but are also pivotal effectors within the Cdk1 auto-regulatory loop responsible for its independence with respect to the PKA-negative control. | The phosphorylation of ARPP19 by Greatwall renders the auto-amplification of MPF independently of PKA in Xenopus oocytes. Dupré A, Buffin E, Roustan C, Nairn AC, Jessus C, Haccard O., Free PMC Article | 04/26/2014 |
Greatwall kinase and cyclin B-Cdk1 are both critical constituents of M-phase-promoting factor. | Greatwall kinase and cyclin B-Cdk1 are both critical constituents of M-phase-promoting factor. Hara M, Abe Y, Tanaka T, Yamamoto T, Okumura E, Kishimoto T., Free PMC Article | 02/2/2013 |
inhibition of PP2A-B55delta results from Ensa, that is phosphorylated in mitosis by the protein kinase Greatwall; this converts Ensa into specific inhibitor of PP2A-B55delta; this pathway represents a previously unknown element in mitosis control | Greatwall phosphorylates an inhibitor of protein phosphatase 2A that is essential for mitosis. Mochida S, Maslen SL, Skehel M, Hunt T. | 11/26/2012 |
3 phosphorylation sites (phosphosites) critical to Gwl activation (pT193, pT206, and pS883 in Xenopus laevis) located in evolutionarily conserved domains that differentiate Gwl from related kinases | Determinants for activation of the atypical AGC kinase Greatwall during M phase entry. Blake-Hodek KA, Williams BC, Zhao Y, Castilho PV, Chen W, Mao Y, Yamamoto TM, Goldberg ML., Free PMC Article | 06/30/2012 |
Coordinated interplays between Plx1 and Gwl are required for reactivation of these kinases from the G(2)/M DNA damage checkpoint and efficient checkpoint recovery. | Greatwall and Polo-like kinase 1 coordinate to promote checkpoint recovery. Peng A, Wang L, Fisher LA., Free PMC Article | 10/22/2011 |
mitotic entry and maintenance is not only mediated by the activation of cyclin B-Cdc2 but also by the regulation of PP2A by GW | Greatwall maintains mitosis through regulation of PP2A. Vigneron S, Brioudes E, Burgess A, Labbé JC, Lorca T, Castro A., Free PMC Article | 09/12/2011 |
[review] The kinase Greatwall phosphorylates small protein ARPP-19 and converts it into a potent antimitotic PP2A inhibitor. | Greatwall kinase, ARPP-19 and protein phosphatase 2A: shifting the mitosis paradigm. Haccard O, Jessus C. | 08/27/2011 |