Please use this identifier to cite or link to this item: http://hdl.handle.net/2445/102334
Title: Ssp1 CaMKK: A Sensor of Actin Polarization That Controls Mitotic Commitment through Srk1 in Schizosaccharomyces pombe
Author: Gómez Hierro, Alba
Lambea Martínez, Eva
Giménez Zaragoza, David
López Avilés, Sandra
Yance Chávez, Tula del Carmen
Montserrat, Marta
Pujol Sobrevía, María Jesús
Bachs Valldeneu, Oriol
Aligué i Alemany, Rosa Maria
Keywords: Cicle cel·lular
Proteïnes quinases
Mitosi
Cell cycle
Protein kinases
Mitosis
Issue Date: 17-Nov-2015
Publisher: Public Library of Science (PLoS)
Abstract: Background Calcium/calmodulin-dependent protein kinase kinase (CaMKK) is required for diverse cellular functions. Mammalian CaMKK activates CaMKs and also the evolutionarily-conserved AMP-activated protein kinase (AMPK). The fission yeast Schizosaccharomyces pombe CaMKK, Ssp1, is required for tolerance to limited glucose through the AMPK, Ssp2, and for the integration of cell growth and division through the SAD kinase Cdr2. Results Here we report that Ssp1 controls the G2/M transition by regulating the activity of the CaMK Srk1. We show that inhibition of Cdc25 by Srk1 is regulated by Ssp1; and also that restoring growth polarity and actin localization of ssp1-deleted cells by removing the actin-monomer-binding protein, twinfilin, is sufficient to suppress the ssp1 phenotype. Conclusions These findings demonstrate that entry into mitosis is mediated by a network of proteins, including the Ssp1 and Srk1 kinases. Ssp1 connects the network of components that ensures proper polarity and cell size with the network of proteins that regulates Cdk1-cyclin B activity, in which Srk1 plays an inhibitory role.
Note: Reproducció del document publicat a: http://dx.doi.org/10.1371/journal.pone.0143037
It is part of: PLoS One, 2015, vol. 10, num. 11, p. e0143037
Related resource: http://dx.doi.org/10.1371/journal.pone.0143037
URI: http://hdl.handle.net/2445/102334
ISSN: 1932-6203
Appears in Collections:Articles publicats en revistes (Biomedicina)

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