Paxillin-mediated recruitment of calcineurin to the contractile ring is required for the correct progression of cytokinesis in fission yeast

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Paxillin-mediated recruitment of calcineurin to the contractile ring is required for the correct progression of cytokinesis in fission yeast

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Title: Paxillin-mediated recruitment of calcineurin to the contractile ring is required for the correct progression of cytokinesis in fission yeast
Author: Martín García, Rebeca; Arribas Antón, Victor; Coll Fresno, Pedro Miguel; Pinar Sala, Mario; Alonso Viana, Raúl; Rincón Padilla, Sergio; Correa Bordes, Jaime; Ribas Elcorobarrutia, Juan Carlos; Pérez González, Pilar
Abstract: La paxilina es una proteína de andamiaje que participa en la señalización de adhesión focal en las células de los mamíferos. La levadura de fisión paxillina ortholog, Pxl1, es necesaria para la integridad del anillo de actomiosina contráctil (CAR) y colabora con la β-glucano sintasa Bgs1 en la formación del septo. Aquí mostramos que la función principal de Pxl1 es reclutar fosfatasa de calcineurina (CN) para el anillo de actomiosina; por lo tanto, la ausencia de Pxl1 o de calcineurina causa defectos de citoquinesis similares. A su vez, la CN participa en la desfosforilación de la proteína Cdc15 F-BAR, que recluta y concentra la Pxl1 en la CAR. Nuestros hallazgos sugieren la existencia de un bucle de retroalimentación positiva entre Pxl1 y CN y establecen que Pxl1 es un componente crucial de la vía de señalización de CN durante la citoquinesis.Paxillin is a scaffold protein that participates in focal adhesion signaling in mammalian cells. Fission yeast paxillin ortholog, Pxl1, is required for contractile actomyosin ring (CAR) integrity and collaborates with the β-glucan synthase Bgs1 in septum formation. We show here that Pxl1’s main function is to recruit calcineurin (CN) phosphatase to the actomyosin ring; and thus the absence of either Pxl1 or calcineurin causes similar cytokinesis defects. In turn, CN participates in the dephosphorylation of the Cdc15 F-BAR protein, which recruits and concentrates Pxl1 at the CAR. Our findings suggest the existence of a positive feedback loop between Pxl1 and CN and establish that Pxl1 is a crucial component of the CN signaling pathway during cytokinesis.
URI: http://hdl.handle.net/10662/10917
Date: 2018


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