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

Satoh, Ryuji; Morita, Takahiro; Takada, Hirofumi; Kita, Ayako; Ishiwata, Shunji; Doi, Atsutoshi; Hagihara, Kanako; Taga, Atsushi; Matsumura, Yasuhiro; Tohda, Hideki; Sugiura, Reiko

doi:10.1091/mbc.e08-09-0893

Cited by 37 publications

(33 citation statements)

References 55 publications

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“…8B). It should be noted that in addition to our findings, other researchers have shown changes in Pmk1 phosphorylation during the cell cycle, with it reaching a maximum during the G1/S phase (Madrid et al, 2006;Satoh et al, 2009). Collectively, Pck2-Mkh1 localization at the cell tips closely coincided with Pmk1 activation at the G1/S phase, suggesting that the cell-tip localization of the upstream kinases (Pck2 and Mkh1) could stimulate Pmk1 MAPK, which leads to the oscillation of MAPK activation during the cell cycle.…”

Section: Pck2 and Mkh1 Localized To The Cell Tips In The G1/s Phase Osupporting

confidence: 83%

Skb5, an SH3 adaptor protein, regulates Pmk1 MAPK signaling by controlling the intracellular localization of Mkh1 MAPKKK

Kanda

Satoh

Matsumoto

et al. 2016

Journal of Cell Science

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The mitogen-activated protein kinase (MAPK) cascade is a highly conserved signaling module composed of MAPK kinase kinases (MAPKKKs), MAPK kinases (MAPKK) and MAPKs. The MAPKKK Mkh1 is an initiating kinase in Pmk1 MAPK signaling, which regulates cell integrity in fission yeast (Schizosaccharomyces pombe). Our genetic screen for regulators of Pmk1 signaling identified Shk1 kinase binding protein 5 (Skb5), an SH3-domain-containing adaptor protein.Here, we show that Skb5 serves as an inhibitor of Pmk1 MAPK signaling activation by downregulating Mkh1 localization to cell tips through its interaction with the SH3 domain. Consistent with this, the Mkh1 3PA mutant protein, with impaired Skb5 binding, remained in the cell tips, even when Skb5 was overproduced.

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Section: Pck2 and Mkh1 Localized To The Cell Tips In The G1/s Phase Osupporting

confidence: 83%

Skb5, an SH3 adaptor protein, regulates Pmk1 MAPK signaling by controlling the intracellular localization of Mkh1 MAPKKK

Kanda

Satoh

Matsumoto

et al. 2016

Journal of Cell Science

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“…Another candidate to perform such role is RNA binding protein Msa2/Nrd1, which interacts in vivo with Cpc2 and whose deletion causes initiation of sexual development without nutrient starvation (Tsukahara et al, 1998;Jeong et al, 2004). Also, Msa2/Nrd1 binds and stabilizes Cdc4 mRNA, encoding myosin II light chain, and Nrd1 phosphorylation by Pmk1 negatively regulates its binding activity to Cdc4 mRNA (Satoh et al, 2009). However, the opposite roles described for Cpc2 and Msa2/ Nrd1 in sexual differentiation (Jeong et al, 2004), together with the absence in Msa2-null cells of the main phenotypes associated to Cpc2 deletion, makes unlikely that this RNAbinding protein will be the Cpc2 binding partner involved in mRNA recruitment to the ribosome.…”

Section: Discussionmentioning

confidence: 99%

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

Núñez

Franco

Madrid

et al. 2009

MBoC

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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 NH 2 -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.

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“…Pmk1 is structurally similar to Slt2/Mpk1 from Saccharomyces cerevisiae (Toda et al 1996;Zaitsevskaya-Carter and Cooper 1997) and to the mammalian extracellular signal-regulated kinases (ERKs) (Roux and Blenis 2004). Several targets of Pmk1 MAPK have been described, including Atf1, the transcription factor that signals in the stress-activated MAPK pathway (SAPK), which includes Sty1/Spc1 (Takada et al 2007); Nrd1, an RNA recognition motif (RRM)-type RNA-binding protein (Satoh et al 2009); and the cell surface protein Ecm33 (Takada et al 2010). It has been proposed that Nrd1 may serve as a novel mechanism for the regulation of myosin mRNA and cytokinesis by the Pmk1 pathway (Satoh et al 2009).…”

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confidence: 99%

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

et al. 2013

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Rho1 GTPase is the main activator of cell wall glucan biosynthesis and regulates actin cytoskeleton in fungi, including Schizosaccharomyces pombe. We have obtained a fission yeast thermosensitive mutant strain carrying the rho1-596 allele, which displays reduced Rho1 GTPase activity. This strain has severe cell wall defects and a thermosensitive growth, which is partially suppressed by osmotic stabilization. In a global screening for rho1-596 multicopy suppresors the pmp1 + gene was identified. Pmp1 is a dual specificity phosphatase that negatively regulates the Pmk1 mitogen-activated protein kinase (MAPK) cell integrity pathway. Accordingly, elimination of Pmk1 MAPK partially rescued rho1-596 thermosensitivity, corroborating the unexpected antagonistic functional relationship of these genes. We found that rho1-596 cells displayed increased basal activation of the cell integrity MAPK pathway and therefore were hypersensitive to MgCl 2 and FK506. Moreover, the absence of calcineurin was lethal for rho1-596. We found a higher level of calcineurin activity in rho1-596 than in wild-type cells, and overexpression of constitutively active calcineurin partially rescued rho1-596 thermosensitivity. All together our results suggest that loss of Rho1 function causes an increase in the cell integrity MAPK activity, which is detrimental to the cells and turns calcineurin activity essential. RHO GTPases are conserved proteins that regulate the actin cytoskeleton organization in all eukaryots (Heasman and Ridley 2008). Additionally, in yeast and other fungi, these GTPases provide the coordinated regulation of cell wall biosynthesis and actin organization, which is required to maintain cell integrity and polarized growth (Levin 2005;Park and Bi 2007;Perez and Cansado 2010). The Schizosaccharomyces pombe genome contains six genes coding Rho GTPases. Among them, rho1 + is essential (Arellano et al. 1996). Rho1 function is mediated by its interaction with at least three different targets: the b(1,3)-glucan synthase (Arellano et al. 1996), which is responsible for the synthesis of the major cell wall component, and the kinases Pck1 and Pck2 Sayers et al. 2000). Through both kinases, Rho1 also regulates the cell wall synthesis. Rho2 also interacts with Pck2 and, therefore, both GTPases regulate the a-D-glucan synthesis through Pck2 (Katayama et al. 1999;Calonge et al. 2000). Lack of Rho1 is lethal, and this phenotype is not suppressed by osmotic stabilization (Arellano et al. 1997), suggesting that defective biosynthesis of the cell wall is not the unique cause of death. On the contrary, Rho2-less cells are viable, although they become slightly rounded and more sensitive to treatment with glucanases (Hirata et al. 1998). Rho2 and Pck2 participate in the activation of the cell integrity mitogen-activated protein kinase (MAPK) signaling pathway (Ma et al. 2006). This signaling cascade responds to different extracellular stress stimuli such as hyper-or hypotonic conditions, oxidative stress, cell wall damaging compounds, and g...

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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

Cited by 37 publications

References 55 publications

Skb5, an SH3 adaptor protein, regulates Pmk1 MAPK signaling by controlling the intracellular localization of Mkh1 MAPKKK

Skb5, an SH3 adaptor protein, regulates Pmk1 MAPK signaling by controlling the intracellular localization of Mkh1 MAPKKK

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

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

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