The M Phase Kinase Greatwall (Gwl) Promotes Inactivation of PP2A/B55δ, a Phosphatase Directed Against CDK Phosphosites
نویسندگان
چکیده
منابع مشابه
Greatwall kinase protects mitotic phosphosites from barbarian phosphatases.
T he basic outline of the events controlling entry into mitosis has been clear for more than 20 y: the essential mitotic driver Mphase promoting factor [MPF; a cyclindependent kinase (CDK) composed of CDK1 and cyclin B] becomes rapidly activated and phosphorylates a wide variety of targets, creating mitotic phosphoproteins that contribute to nuclear membrane breakdown, chromosome condensation, ...
متن کاملCorrection: PP2A/B55 and Fcp1 Regulate Greatwall and Ensa Dephosphorylation during Mitotic Exit
Entry into mitosis is triggered by activation of Cdk1 and inactivation of its counteracting phosphatase PP2A/B55. Greatwall kinase inactivates PP2A/B55 via its substrates Ensa and ARPP19. Both Greatwall and Ensa/ARPP19 are regulated by phosphorylation, but the dynamic regulation of Greatwall activity and the phosphatases that control Greatwall kinase and its substrates are poorly understood. To...
متن کاملFcp1 phosphatase controls Greatwall kinase to promote PP2A-B55 activation and mitotic progression
During cell division, progression through mitosis is driven by a protein phosphorylation wave. This wave namely depends on an activation-inactivation cycle of cyclin B-dependent kinase (Cdk) 1 while activities of major protein phosphatases, like PP1 and PP2A, appear directly or indirectly repressed by Cdk1. However, how Cdk1 inactivation is coordinated with reactivation of major phosphatases at...
متن کاملRoles of Greatwall kinase in the regulation of cdc25 phosphatase.
We previously reported that immunodepletion of Greatwall kinase prevents Xenopus egg extracts from entering or maintaining M phase due to the accumulation of inhibitory phosphorylations on Thr14 and Tyr15 of Cdc2. M phase-promoting factor (MPF) in turn activates Greatwall, implying that Greatwall participates in an MPF autoregulatory loop. We show here that activated Greatwall both accelerates ...
متن کاملGreatwall-phosphorylated Endosulfine is both an inhibitor and a substrate of PP2A-B55 heterotrimers
During M phase, Endosulfine (Endos) family proteins are phosphorylated by Greatwall kinase (Gwl), and the resultant pEndos inhibits the phosphatase PP2A-B55, which would otherwise prematurely reverse many CDK-driven phosphorylations. We show here that PP2A-B55 is the enzyme responsible for dephosphorylating pEndos during M phase exit. The kinetic parameters for PP2A-B55's action on pEndos are o...
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ژورنال
عنوان ژورنال: Molecular Biology of the Cell
سال: 2009
ISSN: 1059-1524,1939-4586
DOI: 10.1091/mbc.e09-07-0643