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Ssp1 CaMKK: A Sensor of Actin Polarization That Controls Mitotic Commitment through Srk1 in Schizosaccharomyces pombe
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 toler...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4648557/ https://www.ncbi.nlm.nih.gov/pubmed/26575035 http://dx.doi.org/10.1371/journal.pone.0143037 |
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author | Gómez-Hierro, Alba Lambea, Eva Giménez-Zaragoza, David López-Avilés, Sandra Yance-Chávez, Tula Montserrat, Marta Pujol, M. Jesús Bachs, Oriol Aligue, Rosa |
author_facet | Gómez-Hierro, Alba Lambea, Eva Giménez-Zaragoza, David López-Avilés, Sandra Yance-Chávez, Tula Montserrat, Marta Pujol, M. Jesús Bachs, Oriol Aligue, Rosa |
author_sort | Gómez-Hierro, Alba |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-4648557 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-46485572015-11-25 Ssp1 CaMKK: A Sensor of Actin Polarization That Controls Mitotic Commitment through Srk1 in Schizosaccharomyces pombe Gómez-Hierro, Alba Lambea, Eva Giménez-Zaragoza, David López-Avilés, Sandra Yance-Chávez, Tula Montserrat, Marta Pujol, M. Jesús Bachs, Oriol Aligue, Rosa PLoS One Research Article 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. Public Library of Science 2015-11-17 /pmc/articles/PMC4648557/ /pubmed/26575035 http://dx.doi.org/10.1371/journal.pone.0143037 Text en © 2015 Gómez-Hierro et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Gómez-Hierro, Alba Lambea, Eva Giménez-Zaragoza, David López-Avilés, Sandra Yance-Chávez, Tula Montserrat, Marta Pujol, M. Jesús Bachs, Oriol Aligue, Rosa Ssp1 CaMKK: A Sensor of Actin Polarization That Controls Mitotic Commitment through Srk1 in Schizosaccharomyces pombe |
title | Ssp1 CaMKK: A Sensor of Actin Polarization That Controls Mitotic Commitment through Srk1 in Schizosaccharomyces pombe
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title_full | Ssp1 CaMKK: A Sensor of Actin Polarization That Controls Mitotic Commitment through Srk1 in Schizosaccharomyces pombe
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title_fullStr | Ssp1 CaMKK: A Sensor of Actin Polarization That Controls Mitotic Commitment through Srk1 in Schizosaccharomyces pombe
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title_full_unstemmed | Ssp1 CaMKK: A Sensor of Actin Polarization That Controls Mitotic Commitment through Srk1 in Schizosaccharomyces pombe
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title_short | Ssp1 CaMKK: A Sensor of Actin Polarization That Controls Mitotic Commitment through Srk1 in Schizosaccharomyces pombe
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title_sort | ssp1 camkk: a sensor of actin polarization that controls mitotic commitment through srk1 in schizosaccharomyces pombe |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4648557/ https://www.ncbi.nlm.nih.gov/pubmed/26575035 http://dx.doi.org/10.1371/journal.pone.0143037 |
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