scholarly journals Negative Functional Interaction Between Cell Integrity MAPK Pathway and Rho1 GTPase in Fission Yeast

Genetics ◽  
2013 ◽  
Vol 195 (2) ◽  
pp. 421-432 ◽  
Author(s):  
Raul A. Viana ◽  
Mario Pinar ◽  
Teresa Soto ◽  
Pedro M. Coll ◽  
Jose Cansado ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Mapk Pathway ◽  
Cell Integrity ◽  
Functional Interaction

scholarly journals Rho1 GTPase and PKC Ortholog Pck1 Are Upstream Activators of the Cell Integrity MAPK Pathway in Fission Yeast

PLoS ONE ◽  
2014 ◽  
Vol 9 (1) ◽  
pp. e88020 ◽  
Author(s):  
Laura Sánchez-Mir ◽  
Teresa Soto ◽  
Alejandro Franco ◽  
Marisa Madrid ◽  
Raúl A. Viana ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Mapk Pathway ◽  
Cell Integrity

scholarly journals Role of the fission yeast cell integrity MAPK pathway in response to glucose limitation

2013 ◽  
Vol 13 (1) ◽  
pp. 34 ◽  
Author(s):  
Marisa Madrid ◽  
Jesús Fernández-Zapata ◽  
Laura Sánchez-Mir ◽  
Teresa Soto ◽  
Alejandro Franco ◽  
...  
Keyword(s):  
Yeast Cell ◽  
Fission Yeast ◽  
Mapk Pathway ◽  
Cell Integrity ◽  
Glucose Limitation ◽  
Fission Yeast Cell

scholarly journals Rga4 Modulates the Activity of the Fission Yeast Cell Integrity MAPK Pathway by Acting as a Rho2 GTPase-activating Protein

2010 ◽  
Vol 285 (15) ◽  
pp. 11516-11525 ◽  
Author(s):  
Teresa Soto ◽  
Maria Antonia Villar-Tajadura ◽  
Marisa Madrid ◽  
Jero Vicente ◽  
Mariano Gacto ◽  
...  
Keyword(s):  
Yeast Cell ◽  
Fission Yeast ◽  
Mapk Pathway ◽  
Cell Integrity ◽  
Gtpase Activating Protein ◽  
Fission Yeast Cell

scholarly journals Role for RACK1 Orthologue Cpc2 in the Modulation of Stress Response in Fission Yeast

2009 ◽  
Vol 20 (18) ◽  
pp. 3996-4009 ◽  
Author(s):  
Andrés Núñez ◽  
Alejandro Franco ◽  
Marisa Madrid ◽  
Teresa Soto ◽  
Jero Vicente ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Fission Yeast ◽  
Mammalian Cells ◽  
Mapk Pathway ◽  
Ribosomal Subunit ◽  
Mitogen Activated Protein Kinase ◽  
Specific Gene ◽  
Cell Integrity ◽  
Mapk Cascades ◽  
Mitogen Activated Protein

The receptor of activated C kinase (RACK1) is a protein highly conserved among eukaryotes. In mammalian cells, RACK1 functions as an adaptor to favor protein kinase C (PKC)-mediated phosphorylation and subsequent activation of c-Jun NH2-terminal kinase mitogen-activated protein kinase. Cpc2, the RACK1 orthologue in the fission yeast Schizosaccharomyces pombe, is involved in the control of G2/M transition and interacts with Pck2, a PKC-type protein member of the cell integrity Pmk1 mitogen-activated protein kinase (MAPK) pathway. Both RACK1 and Cpc2 are structural components of the 40S ribosomal subunit, and recent data suggest that they might be involved in the control of translation. In this work, we present data supporting that Cpc2 negatively regulates the cell integrity transduction pathway by favoring translation of the tyrosine-phosphatases Pyp1 and Pyp2 that deactivate Pmk1. In addition, Cpc2 positively regulates the synthesis of the stress-responsive transcription factor Atf1 and the cytoplasmic catalase, a detoxificant enzyme induced by treatment with hydrogen peroxide. These results provide for the first time strong evidence that the RACK1-type Cpc2 protein controls from the ribosome the extent of the activation of MAPK cascades, the cellular defense against oxidative stress, and the progression of the cell cycle by regulating positively the translation of specific gene products involved in key biological processes.

scholarly journals Atf1 Is a Target of the Mitogen-activated Protein Kinase Pmk1 and Regulates Cell Integrity in Fission Yeast

2007 ◽  
Vol 18 (12) ◽  
pp. 4794-4802 ◽  
Author(s):  
Hirofumi Takada ◽  
Masayuki Nishimura ◽  
Yuta Asayama ◽  
Yoshiaki Mannse ◽  
Shunji Ishiwata ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Fission Yeast ◽  
Mapk Pathway ◽  
Mapk Signaling ◽  
Negative Regulator ◽  
Mitogen Activated Protein Kinase ◽  
Mrna Levels ◽  
Cell Integrity ◽  
Dual Specificity ◽  
Mitogen Activated Protein

In fission yeast, knockout of the calcineurin gene resulted in hypersensitivity to Cl−, and the overexpression of pmp1+ encoding a dual-specificity phosphatase for Pmk1 mitogen-activated protein kinase (MAPK) or the knockout of the components of the Pmk1 pathway complemented the Cl− hypersensitivity of calcineurin deletion. Here, we showed that the overexpression of ptc1+ and ptc3+, both encoding type 2C protein phosphatase (PP2C), previously known to inactivate the Wis1–Spc1–Atf1 stress-activated MAPK signaling pathway, suppressed the Cl− hypersensitivity of calcineurin deletion. We also demonstrated that the mRNA levels of these two PP2Cs and pyp2+, another negative regulator of Spc1, are dependent on Pmk1. Notably, the deletion of Atf1, but not that of Spc1, displayed hypersensitivity to the cell wall-damaging agents and also suppressed the Cl− hypersensitivity of calcineurin deletion, both of which are characteristic phenotypes shared by the mutation of the components of the Pmk1 MAPK pathway. Moreover, micafungin treatment induced Pmk1 hyperactivation that resulted in Atf1 hyperphosphorylation. Together, our results suggest that PP2C is involved in a negative feedback loop of the Pmk1 signaling, and results also demonstrate that Atf1 is a key component of the cell integrity signaling downstream of Pmk1 MAPK.

scholarly journals Specific Functional Features of the Cell Integrity MAP Kinase Pathway in the Dimorphic Fission Yeast Schizosaccharomyces japonicus

2021 ◽  
Vol 7 (6) ◽  
pp. 482
Author(s):  
Elisa Gómez-Gil ◽  
Alejandro Franco ◽  
Beatriz Vázquez-Marín ◽  
Francisco Prieto-Ruiz ◽  
Armando Pérez-Díaz ◽  
...  
Keyword(s):  
Fission Yeast ◽  
Environmental Changes ◽  
Yeast Species ◽  
Mapk Signaling ◽  
Fine Tuning ◽  
Mitogen Activated Protein Kinase ◽  
Major Influence ◽  
Cell Integrity ◽  
Mitogen Activated Protein ◽  
Functional Features

Mitogen activated protein kinase (MAPK) signaling pathways execute essential functions in eukaryotic organisms by transducing extracellular stimuli into adaptive cellular responses. In the fission yeast model Schizosaccharomyces pombe the cell integrity pathway (CIP) and its core effector, MAPK Pmk1, play a key role during regulation of cell integrity, cytokinesis, and ionic homeostasis. Schizosaccharomyces japonicus, another fission yeast species, shows remarkable differences with respect to S. pombe, including a robust yeast to hyphae dimorphism in response to environmental changes. We show that the CIP MAPK module architecture and its upstream regulators, PKC orthologs Pck1 and Pck2, are conserved in both fission yeast species. However, some of S. pombe’s CIP-related functions, such as cytokinetic control and response to glucose availability, are regulated differently in S. japonicus. Moreover, Pck1 and Pck2 antagonistically regulate S. japonicus hyphal differentiation through fine-tuning of Pmk1 activity. Chimeric MAPK-swapping experiments revealed that S. japonicus Pmk1 is fully functional in S. pombe, whereas S. pombe Pmk1 shows a limited ability to execute CIP functions and promote S. japonicus mycelial development. Our findings also suggest that a modified N-lobe domain secondary structure within S. japonicus Pmk1 has a major influence on the CIP signaling features of this evolutionarily diverged fission yeast.

scholarly journals The Cell Surface Protein Geneecm33+Is a Target of the Two Transcription Factors Atf1 and Mbx1 and Negatively Regulates Pmk1 MAPK Cell Integrity Signaling in Fission Yeast

2010 ◽  
Vol 21 (4) ◽  
pp. 674-685 ◽  
Author(s):  
Hirofumi Takada ◽  
Aiko Nishida ◽  
Mitsuhiro Domae ◽  
Ayako Kita ◽  
Yuki Yamano ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Cell Surface ◽  
Binding Site ◽  
Fission Yeast ◽  
Tandem Repeats ◽  
Surface Protein ◽  
Luciferase Reporter ◽  
Cell Surface Protein ◽  
Cell Integrity ◽  
Negative Feedback Regulation

The highly conserved fission yeast Pmk1 MAPK pathway plays a key role in cell integrity by regulating Atf1, which belongs to the ATF/cAMP-responsive element-binding (CREB) protein family. We identified and characterized ecm33+, which encodes a glycosyl-phosphatidylinositol (GPI)-anchored cell surface protein as a transcriptional target of Pmk1 and Atf1. We demonstrated that the gene expression of Ecm33 is regulated by two transcription factors Atf1 and a MADS-box-type transcription factor Mbx1. We identified a putative ATF/CREB-binding site and an RLM1-binding site in the ecm33+promoter region and monitored the transcriptional activity of Atf1 or Mbx1 in living cells using a destabilized luciferase reporter gene fused to three tandem repeats of the CRE and six tandem repeats of the Rlm1-binding sequence, respectively. These reporter genes reflect the activation of the Pmk1 pathway by various stimuli, thereby enabling the real-time monitoring of the Pmk1 cell integrity pathway. Notably, the Δecm33 cells displayed hyperactivation of the Pmk1 signaling together with hypersensitivity to Ca2+and an abnormal morphology, which were almost abolished by simultaneous deletion of the components of the Rho2/Pck2/Pmk1 pathway. Our results suggest that Ecm33 is involved in the negative feedback regulation of Pmk1 cell integrity signaling and is linked to cellular Ca2+signaling.

scholarly journals Fission yeast Cyk3p is a transglutaminase-like protein that participates in cytokinesis and cell morphogenesis

2012 ◽  
Vol 23 (13) ◽  
pp. 2433-2444 ◽  
Author(s):  
Luther W. Pollard ◽  
Masayuki Onishi ◽  
John R. Pringle ◽  
Matthew Lord
Keyword(s):  
Fission Yeast ◽  
Primary Role ◽  
Cell Integrity ◽  
Cell Morphogenesis ◽  
Contractile Ring ◽  
Physiological Importance ◽  
Complex Process ◽  
Catalytic Active Site ◽  
Thiol Proteases ◽  
Ring Constriction

Cell morphogenesis is a complex process that relies on a diverse array of proteins and pathways. We have identified a transglutaminase-like protein (Cyk3p) that functions in fission yeast morphogenesis. The phenotype of a cyk3 knockout strain indicates a primary role for Cyk3p in cytokinesis. Correspondingly, Cyk3p localizes both to the actomyosin contractile ring and the division septum, promoting ring constriction, septation, and subsequent cell separation following ring disassembly. In addition, Cyk3p localizes to polarized growth sites and plays a role in cell shape determination, and it also appears to contribute to cell integrity during stationary phase, given its accumulation as dynamic puncta at the cortex of such cells. Our results and the conservation of Cyk3p across fungi point to a role in cell wall synthesis and remodeling. Cyk3p possesses a transglutaminase domain that is essential for function, even though it lacks the catalytic active site. In a wider sense, our work illustrates the physiological importance of inactive members of the transglutaminase family, which are found throughout eukaryotes. We suggest that the proposed evolution of animal transglutaminase cross-linking activity from ancestral bacterial thiol proteases was accompanied by the emergence of a subclass whose function does not depend on enzymatic activity.

scholarly journals The Rho1p Exchange Factor Rgf1p Signals Upstream from the Pmk1 Mitogen-activated Protein Kinase Pathway in Fission Yeast

2009 ◽  
Vol 20 (2) ◽  
pp. 721-731 ◽  
Author(s):  
Patricia Garcia ◽  
Virginia Tajadura ◽  
Yolanda Sanchez
Keyword(s):  
Mapk Pathway ◽  
Osmotic Shock ◽  
Mapk Signaling ◽  
Mitogen Activated Protein Kinase ◽  
Cell Integrity ◽  
Actin Reorganization ◽  
Exchange Factor ◽  
Mitogen Activated Protein ◽  
Chlorine Ion ◽  
Kinase Pathway

The Schizosaccharomyces pombe exchange factor Rgf1p specifically regulates Rho1p during polarized growth. Rgf1p activates the β-glucan synthase (GS) complex containing the catalytic subunit Bgs4p and is involved in the activation of growth at the second end, a transition that requires actin reorganization. In this work, we investigated Rgf1p signaling and observed that Rgf1p acted upstream from the Pck2p-Pmk1p MAPK signaling pathway. We noted that Rgf1p and calcineurin play antagonistic roles in Cl− homeostasis; rgf1Δ cells showed the vic phenotype (viable in the presence of immunosuppressant and chlorine ion) and were unable to grow in the presence of high salt concentrations, both phenotypes being characteristic of knockouts of the MAPK components. In addition, mutations that perturb signaling through the MAPK pathway resulted in defective cell integrity (hypersensitivity to caspofungin and β-glucanase). Rgf1p acts by positively regulating a subset of stimuli toward the Pmk1p-cell integrity pathway. After osmotic shock and cell wall damage HA-tagged Pmk1p was phosphorylated in wild-type cells but not in rgf1Δ cells. Finally, we provide evidence to show that Rgf1p regulates Pmk1p activation in a process that involves the activation of Rho1p and Pck2p, and we demonstrate that Rgf1p is unique in this signaling process, because Pmk1p activation was largely independent of the other two Rho1p-specific GEFs, Rgf2p and Rgf3p.

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