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Atf1 is a target of the mitogen-activated protein kinase Pmk1 and regulates cell integrity in fission yeast.
Mol Biol Cell. 2007 Dec; 18(12):4794-802.MB

Abstract

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.

Authors+Show Affiliations

Laboratory of Molecular Pharmacogenomics, School of Pharmaceutical Sciences, Kinki University, Higashi-Osaka, 577-8502, Japan.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17881729

Citation

Takada, Hirofumi, et al. "Atf1 Is a Target of the Mitogen-activated Protein Kinase Pmk1 and Regulates Cell Integrity in Fission Yeast." Molecular Biology of the Cell, vol. 18, no. 12, 2007, pp. 4794-802.
Takada H, Nishimura M, Asayama Y, et al. Atf1 is a target of the mitogen-activated protein kinase Pmk1 and regulates cell integrity in fission yeast. Mol Biol Cell. 2007;18(12):4794-802.
Takada, H., Nishimura, M., Asayama, Y., Mannse, Y., Ishiwata, S., Kita, A., Doi, A., Nishida, A., Kai, N., Moriuchi, S., Tohda, H., Giga-Hama, Y., Kuno, T., & Sugiura, R. (2007). Atf1 is a target of the mitogen-activated protein kinase Pmk1 and regulates cell integrity in fission yeast. Molecular Biology of the Cell, 18(12), 4794-802.
Takada H, et al. Atf1 Is a Target of the Mitogen-activated Protein Kinase Pmk1 and Regulates Cell Integrity in Fission Yeast. Mol Biol Cell. 2007;18(12):4794-802. PubMed PMID: 17881729.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Atf1 is a target of the mitogen-activated protein kinase Pmk1 and regulates cell integrity in fission yeast. AU - Takada,Hirofumi, AU - Nishimura,Masayuki, AU - Asayama,Yuta, AU - Mannse,Yoshiaki, AU - Ishiwata,Shunji, AU - Kita,Ayako, AU - Doi,Akira, AU - Nishida,Aiko, AU - Kai,Naoyuki, AU - Moriuchi,Sayako, AU - Tohda,Hideki, AU - Giga-Hama,Yuko, AU - Kuno,Takayoshi, AU - Sugiura,Reiko, Y1 - 2007/09/19/ PY - 2007/9/21/pubmed PY - 2008/3/20/medline PY - 2007/9/21/entrez SP - 4794 EP - 802 JF - Molecular biology of the cell JO - Mol Biol Cell VL - 18 IS - 12 N2 - 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. SN - 1059-1524 UR - https://www.unboundmedicine.com/medline/citation/17881729/Atf1_is_a_target_of_the_mitogen_activated_protein_kinase_Pmk1_and_regulates_cell_integrity_in_fission_yeast_ L2 - https://www.molbiolcell.org/doi/10.1091/mbc.e07-03-0282?url_ver=Z39.88-2003&rfr_id=ori:rid:crossref.org&rfr_dat=cr_pub=pubmed DB - PRIME DP - Unbound Medicine ER -