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Título: | Paxillin-mediated recruitment of calcineurin to the contractile ring is required for the correct progression of cytokinesis in fission yeast |
Autor: | Martín-García, Rebeca CSIC ORCID; Arribas, Victor CSIC; Coll, Pedro M. CSIC; Pinar, Mario CSIC ORCID ; Viana, Raul A.; Rincón, Sergio A. CSIC ORCID; Correa-Bordes, Jaime; Ribas, Juan Carlos CSIC ORCID; Pérez, Pilar CSIC ORCID | Fecha de publicación: | 16-oct-2018 | Editor: | Elsevier | Citación: | Cell Reports 25:772–783 (2018) | Resumen: | 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 b-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. | Descripción: | 17 p.-7 fig.-1 tab. | Versión del editor: | https://doi.org//10.1016/j.celrep.2018.09.062 | URI: | http://hdl.handle.net/10261/171240 | DOI: | 10.1016/j.celrep.2018.09.062 | ISSN: | 2211-1247 | E-ISSN: | 2211-1247 |
Aparece en las colecciones: | (CIB) Artículos (IBFG) Artículos |
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