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Differential regulation of activation and stabilization of PKC orthologs in fission yeast

AutorGómez Gil, E.; Soto, Teresa; Franco, Alejandro; Gacto, Mariano; Pérez, Pilar; Cansado, José; Madrid, Marisa
Fecha de publicación2017
CitaciónFEMS 2017
Resumen[Backgrounds]: The two Protein kinase C orthologs Pck1 and Pck2 operate in a redundant fashion in the fission yeast Schizosaccharomyces pombe to control essential functions including morphogenesis, cell wall biosynthesis, and the activity of the cell integrity pathway (CIP) and is core element MAP kinase Pmk1. [Objectives]: To identify the mechanisms responsible for maturation, catalytic activation, and stabilization of Pck1 and Pck2. [Methods]: We show that despite their strong structural similarity and functional redundancy, the mechanisms regulating their maturation, activation, and stabilization have a remarkably distinct biological impact on both kinases. Contrary to Pck2, putative in vivo phosphorylation of Pck1 within conserved activation loop, turn and hydrophobic motifs is essential for protein stability and biological functions. Constitutive activation promoted dephosphorylation and destabilization of Pck2, while it enhanced Pck1 stability to interfere with proper downstream signaling to the CIP triggered by Pck2. Importantly, whereas catalytic activity is essential for Pck1 functions, Pck2 remains partially functional in absence of kinase activity. [Conclusions]: Our findings suggest that early duplication from a single ancestor involved important changes in the mechanisms regulating catalytic activation and stability of PKC family members to allow for a flexible and dynamic control of downstream functions, including MAPK signaling.
DescripciónResumen del trabajo presentado al 7th Congress of European Microbiologists, celebrado en Valencia (España) del 9 al 13 de julio de 2017.-- et al.
Aparece en las colecciones: (IBFG) Comunicaciones congresos
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