scholarly journals Regulation of LRG1 expression by RNA‐binding protein Puf5 in the budding yeast cell wall integrity pathway

2018 ◽  
Vol 23 (12) ◽  
pp. 988-997 ◽  
Author(s):  
Nguyen Thi Minh Viet ◽  
Duong Long Duy ◽  
Kazuhiro Saito ◽  
Kaoru Irie ◽  
Yasuyuki Suda ◽  
...  
2016 ◽  
Vol 291 (11) ◽  
pp. 5461-5472 ◽  
Author(s):  
Esmeralda Alonso-Rodríguez ◽  
Pablo Fernández-Piñar ◽  
Almudena Sacristán-Reviriego ◽  
María Molina ◽  
Humberto Martín

2011 ◽  
Vol 10 (10) ◽  
pp. 1340-1347 ◽  
Author(s):  
Wataru Ito ◽  
Xia Li ◽  
Kaoru Irie ◽  
Tomoaki Mizuno ◽  
Kenji Irie

ABSTRACT The Saccharomyces cerevisiae RNA-binding protein Khd1/Hek2 associates with hundreds of potential mRNA targets preferentially, including the mRNAs encoding proteins localized to the cell wall and plasma membrane. We have previously revealed that Khd1 positively regulates expression of MTL1 mRNA encoding a membrane sensor in the cell wall integrity (CWI) pathway. However, a khd1 Δ mutation has no detectable phenotype on cell wall synthesis. Here we show that the khd1 Δ mutation causes a severe cell lysis when combined with the deletion of the CCR4 gene encoding a cytoplasmic deadenylase. We identified the ROM2 mRNA, encoding a guanine nucleotide exchange factor (GEF) for Rho1, as a target for Khd1 and Ccr4. The ROM2 mRNA level was decreased in the khd1 Δ ccr4 Δ mutant, and ROM2 overexpression suppressed the cell lysis of the khd1 Δ ccr4 Δ mutant. We also found that Ccr4 negatively regulates expression of the LRG1 mRNA encoding a GTPase-activating protein (GAP) for Rho1. The LRG1 mRNA level was increased in the ccr4 Δ and khd1 Δ ccr4 Δ mutants, and deletion of LRG1 suppressed the cell lysis of the khd1 Δ ccr4 Δ mutant. Our results presented here suggest that Khd1 and Ccr4 modulate a signal from Rho1 in the CWI pathway by regulating the expression of RhoGEF and RhoGAP.


2020 ◽  
Author(s):  
Lin-Chun Chang ◽  
Yu-Chieh Wu ◽  
Yu-Yun Chang ◽  
Fang-Jen Lee

AbstractThe yeast cell wall integrity (CWI) MAPK pathway is a signaling cascade function in maintaining cell wall integrity under stressful environmental conditions. Recently, the activity and signaling of Slt2p (Mpk1p) MAP kinase has been shown to control assembly of the processing body (P-body) upon cell wall stresses, implicating its posttranscriptional role in decay of cell wall mRNAs. However, how Slt2p MAP kinase directly regulates the stability of cell wall transcripts during cell wall stress remains unclear. Here, we reported that the RNA-binding protein Rbp1p (Ngr1p) is a downstream effector and target of Slt2p MAP kinase during activation of the cell wall stress signaling cascade. In addition to the well-defined target mitochondrial porin mRNA, we found that Rbp1p also negatively regulates the stability of a subset of Slt2p-regulated cell wall transcripts. Deletion of RBP1 increases the level of cell wall transcripts and partially suppresses the hypersensitivity of the slt2Δ deletion strain to cell wall damage. Slt2p is necessary for cell wall stress-induced stabilization of cell wall transcripts. Deletion of RBP1 compromises the destabilization of cell wall transcripts in slt2Δ mutants under cell wall stress. Notably, C-terminal deleted Slt2p impairs its function in promoting turnover of the Rbp1p protein and fails to stabilize cell wall transcripts, although it can complement the growth defect of the slt2Δ strain upon cell wall stress. Altogether, our results demonstrate that MAP kinase Slt2p attenuates CWI mRNA decay in response to cell wall damage by downregulating the activity of the RNA-binding protein Rbp1p.


2009 ◽  
Vol 84 (4) ◽  
pp. 269-276 ◽  
Author(s):  
Mizuho Sekiya ◽  
Satoru Nogami ◽  
Yoshikazu Ohya

2016 ◽  
Vol 18 (9) ◽  
pp. 1251-1267 ◽  
Author(s):  
Christian Kock ◽  
Henning Arlt ◽  
Christian Ungermann ◽  
Jürgen J. Heinisch

FEBS Letters ◽  
2013 ◽  
Vol 587 (22) ◽  
pp. 3675-3680 ◽  
Author(s):  
José M. Rodríguez-Peña ◽  
Sonia Díez-Muñiz ◽  
Clara Bermejo ◽  
César Nombela ◽  
Javier Arroyo

2019 ◽  
Vol 30 (4) ◽  
pp. 441-452 ◽  
Author(s):  
Allison E. Hall ◽  
Mark D. Rose

During mating, Saccharomyces cerevisiae cells must degrade the intervening cell wall to allow fusion of the partners. Because improper timing or location of cell wall degradation would cause lysis, the initiation of cell fusion must be highly regulated. Here, we find that yeast cell fusion is negatively regulated by components of the cell wall integrity (CWI) pathway. Loss of the cell wall sensor, MID2, specifically causes “mating-induced death” after pheromone exposure. Mating-induced death is suppressed by mutations in cell fusion genes ( FUS1, FUS2, RVS161, CDC42), implying that mid2Δ cells die from premature fusion without a partner. Consistent with premature fusion, mid2Δ shmoos had thinner cell walls and lysed at the shmoo tip. Normally, Cdc42p colocalizes with Fus2p to form a focus only when mating cells are in contact (prezygotes) and colocalization is required for cell fusion. However, Cdc42p was aberrantly colocalized with Fus2p to form a focus in mid2Δ shmoos. A hyperactive allele of the CWI kinase Pkc1p ( PKC1*) caused decreased cell fusion and Cdc42p localization in prezygotes. In shmoos, PKC1* increased Cdc42p localization; however, it was not colocalized with Fus2p or associated with cell death. We conclude that Mid2p and Pkc1p negatively regulate cell fusion via Cdc42p and Fus2p.


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