Stress-activated Protein Kinase-mediated Down-Regulation of the Cell Integrity Pathway Mitogen-activated Protein Kinase Pmk1p by Protein Phosphatases

Madrid, Marisa; Núñez, Andrés; Soto, Teresa; Vicente-Soler, Jero; Gacto, Mariano; Cansado, José

doi:10.1091/mbc.e07-05-0484

Cited by 43 publications

(76 citation statements)

References 48 publications

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“…Cells from this mutant were grown to the log phase at 25°C, shifted to 37°C for 4 h to synchronize the cells in the G2 phase, and then shifted back to 25°C. As shown in Figure 9A, changes in Pmk1 phosphorylation as detected by antiphospho-p42/44 antibodies were noted during the cell cycle, reaching a maximum during cytokinesis, which is consistent with previous observations (Madrid et al, 2007).…”

Section: Cell Cycle-dependent Regulation Of Pmk1-nrd1 Signalingsupporting

confidence: 92%

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Role of the RNA-binding Protein Nrd1 and Pmk1 Mitogen-activated Protein Kinase in the Regulation of Myosin mRNA Stability in Fission Yeast

Satoh

Morita

Takada

et al. 2009

MBoC

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Myosin II is an essential component of the actomyosin contractile ring and plays a crucial role in cytokinesis by generating the forces necessary for contraction of the actomyosin ring. Cdc4 is an essential myosin II light chain in fission yeast and is required for cytokinesis. In various eukaryotes, the phosphorylation of myosin is well documented as a primary means of activating myosin II, but little is known about the regulatory mechanisms of Cdc4. Here, we isolated Nrd1, an RNA-binding protein with RNA-recognition motifs, as a multicopy suppressor of cdc4 mutants. Notably, we demonstrated that Nrd1 binds and stabilizes Cdc4 mRNA, thereby suppressing the cytokinesis defects of the cdc4 mutants. Importantly, Pmk1 mitogen-activated protein kinase (MAPK) directly phosphorylates Nrd1, thereby negatively regulating the binding activity of Nrd1 to Cdc4 mRNA. Consistently, the inactivation of Pmk1 MAPK signaling, as well as Nrd1 overexpression, stabilized the Cdc4 mRNA level, thereby suppressing the cytokinesis defects associated with the cdc4 mutants. In addition, we demonstrated the cell cycle-dependent regulation of Pmk1/Nrd1 signaling. Together, our results indicate that Nrd1 plays a role in the regulation of Cdc4 mRNA stability; moreover, our study is the first to demonstrate the posttranscriptional regulation of myosin expression by MAPK signaling.

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Section: Cell Cycle-dependent Regulation Of Pmk1-nrd1 Signalingsupporting

confidence: 92%

“…In a recent study, Madrid et al (2007) reported that the phosphorylation state of Pmk1 oscillates as a function of the cell cycle. This prompted us to examine the hypothesis that Nrd1 RNA-binding activity and Cdc4 mRNA abundance are also regulated by the cell cycle.…”

Section: Cell Cycle-dependent Regulation Of Pmk1-nrd1 Signalingmentioning

confidence: 99%

Role of the RNA-binding Protein Nrd1 and Pmk1 Mitogen-activated Protein Kinase in the Regulation of Myosin mRNA Stability in Fission Yeast

Satoh

Morita

Takada

et al. 2009

MBoC

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“…Atf1) to regulate gene expression through the cell integrity and stress response pathway respectively (Figure 3). Furthermore, a considerable functional overlap between the two pathways exists, with their role in controlling cellular morphogenesis being equally important (Madrid et al, 2007). Nevertheless, cellular protection against environmental insults depends heavily on the Sty1 pathway, as demonstrated by sensitivity tests with relevant deletion mutants (Pérez & Cansado, 2010).…”

Section: Stress Signaling Pathways: the Central Role Of The Mapk Familymentioning

confidence: 99%

Oxidative stress response pathways: Fission yeast as archetype

Papadakis¹,

Workman²

2015

Critical Reviews in Microbiology

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Schizosaccharomyces pombe is a popular model eukaryotic organism to study diverse aspects of mammalian biology, including responses to cellular stress triggered by redox imbalances within its compartments. The review considers the current knowledge on the signaling pathways that govern the transcriptional response of fission yeast cells to elevated levels of hydrogen peroxide. Particular attention is paid to the mechanisms that yeast cells employ to promote cell survival in conditions of intermediate and acute oxidative stress. The role of the Sty1/Spc1/Phh1 mitogen-activated protein kinase in regulating gene expression at multiple levels is discussed in detail.

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“…Total cell homogenates were prepared under native conditions as described (38), employing chilled acid-washed glass beads and lysis buffer (10% glycerol, 50 mM Tris-HCl, pH 7.5, 150 mM NaCl, 0.1% Nonidet P-40, plus specific protease and phosphatase inhibitor mixtures for fungal and yeast extracts, obtained from Sigma). The lysates were cleared by centrifugation at 20,000 ϫ g for 30 min and resolved in 6 -12% SDSpolyacrylamide gels, depending on the relative size of the fusion protein, and transferred to filters.…”

Section: Gene Disruption and Epitope Tagging-the Cpc2mentioning

confidence: 99%

Fission Yeast Receptor of Activated C Kinase (RACK1) Ortholog Cpc2 Regulates Mitotic Commitment through Wee1 Kinase

Núñez¹,

Franco²,

Soto

et al. 2010

Journal of Biological Chemistry

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In the fission yeast Schizosaccharomyces pombe, Wee1-dependent inhibitory phosphorylation of the highly conserved Cdc2/Cdk1 kinase determines the mitotic onset when cells have reached a defined size. The receptor of activated C kinase (RACK1) is a scaffolding protein strongly conserved among eukaryotes which binds to other proteins to regulate multiple processes in mammalian cells, including the modulation of cell cycle progression during G 1 /S transition. We have recently described that Cpc2, the fission yeast ortholog to RACK1, controls from the ribosome the activation of MAPK cascades and the cellular defense against oxidative stress by positively regulating the translation of specific genes whose products participate in the above processes. Intriguingly, mutants lacking Cpc2 display an increased cell size at division, suggesting the existence of a specific cell cycle defect at the G 2 /M transition. In this work we show that protein levels of Wee1 mitotic inhibitor are increased in cells devoid of Cpc2, whereas the levels of Cdr2, a Wee1 inhibitor, are down-regulated in the above mutant. On the contrary, the kinetics of G 1 /S transition was virtually identical both in control and Cpc2-less strains. Thus, our results suggest that in fission yeast Cpc2/RACK1 positively regulates from the ribosome the mitotic onset by modulating both the protein levels and the activity of Wee1. This novel mechanism of translational control of cell cycle progression might be conserved in higher eukaryotes.Cell reproduction involves the passing through a series of events collectively known as the cell cycle, which consists of alternative stages involving DNA replication (S phase), chromosome segregation and nuclear division (mitosis), as well as cell division (cytokinesis). Entry into mitosis is induced by the activation of a cyclin B-bound Cdc2/Cdk1 kinase, which is highly conserved among eukaryotic cells (1). In the fission yeast Schizosaccharomyces pombe, the inhibitory phosphorylation at a conserved tyrosine 15 (Tyr 15 ) in Cdc2 regulates its kinase activity that determines the mitotic onset and the start of division when the cells have reached a defined size (2). The kinase Wee1 down-regulates Cdc2 by inhibitory Tyr 15 phosphorylation, which is reversed by Cdc25 phosphatase, leading to Cdc2 activation and triggering of mitotic entry (3-6). Consequently, fission yeast cells lacking Wee1 activity enter mitosis before reaching a critical size to produce two small daughter cells (7). On the contrary, mutants in Cdc25 enter mitosis at an increased cell size, indicating that the activities/levels of both Cdc25 and Wee1 must be tightly regulated to provide an accurate control of the mitotic onset. In fission yeast, Wee1 is in turn phosphorylated and its activity negatively regulated by two SAD family kinases, Nim1 (also known as Cdr1 (8 -12) and Cdr2 (13,14). Recently, it has been described that gradients from the cell ends involving the DYRK family kinase Pom1 play a key role in the control of the progression of the cell cycle b...

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Stress-activated Protein Kinase-mediated Down-Regulation of the Cell Integrity Pathway Mitogen-activated Protein Kinase Pmk1p by Protein Phosphatases

Cited by 43 publications

References 48 publications

Role of the RNA-binding Protein Nrd1 and Pmk1 Mitogen-activated Protein Kinase in the Regulation of Myosin mRNA Stability in Fission Yeast

Role of the RNA-binding Protein Nrd1 and Pmk1 Mitogen-activated Protein Kinase in the Regulation of Myosin mRNA Stability in Fission Yeast

Oxidative stress response pathways: Fission yeast as archetype

Fission Yeast Receptor of Activated C Kinase (RACK1) Ortholog Cpc2 Regulates Mitotic Commitment through Wee1 Kinase

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