RT Journal Article
T1 Dual Regulation of the mitotic exit network (MEN) by PP2A-Cdc55 phosphatase.
A1 Baro, Bárbara
A1 Rodríguez Rodríguez, José Antonio
A1 Calabria, Inés
A1 Hernáez Sánchez, Maria Luisa
A1 Gil, Concha
A1 Queralt, Ethel
AB Exit from mitosis in budding yeast is triggered by activation of the key mitotic phosphatase Cdc14. At anaphase onset, the protease separase and Zds1 promote the downregulation of PP2A(Cdc55) phosphatase, which facilitates Cdk1-dependent phosphorylation of Net1 and provides the first wave of Cdc14 activity. Once Cdk1 activity starts to decline, the mitotic exit network (MEN) is activated to achieve full Cdc14 activation. Here we describe how the PP2A(Cdc55) phosphatase could act as a functional link between FEAR and MEN due to its action on Bfa1 and Mob1. We demonstrate that PP2A(Cdc55) regulates MEN activation by facilitating Cdc5- and Cdk1-dependent phosphorylation of Bfa1 and Mob1, respectively. Downregulation of PP2A(Cdc55) initiates MEN activity up to Cdc15 by Bfa1 inactivation. Surprisingly, the premature Bfa1 inactivation observed does not entail premature MEN activation, since an additional Cdk1-Clb2 inhibitory signal acting towards Dbf2-Mob1 activity restrains MEN activity until anaphase. In conclusion, we propose a clear picture of how PP2A(Cdc55) functions affect the regulation of various MEN components, contributing to mitotic exit.
SN 1553-7404
YR 2013
FD 2013
LK https://hdl.handle.net/20.500.14352/35106
UL https://hdl.handle.net/20.500.14352/35106
LA eng
NO Ministerio de Ciencia e Innovación (MICINN)
NO Catalonian Government Agency AGAUR
DS Docta Complutense
RD 8 abr 2025