The MAPK kinase Pek1 acts as a phosphorylation-dependent molecular switch

Reiko Sugiura, Takashi Toda, Susheela Dhut, Hisato Shuntoh, Takayoshi Kuno and Takayoshi Kuno
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Reiko Sugiura: Kobe University School of Medicine
Takashi Toda: Cell Regulation Laboratory, Imperial Cancer Research Fund
Susheela Dhut: Cell Regulation Laboratory, Imperial Cancer Research Fund
Hisato Shuntoh: Faculty of Health Science, Kobe University School of Medicine
Takayoshi Kuno: Kobe University School of Medicine
Takayoshi Kuno: Correspondence and requests for materials should be addressed to T.K. (tkuno@kobe-u.ac.jp). The nucleotide sequence of Pek1 has been deposited in DDBJ, EMBL and GenBank under accession number D82023.

Nature, 1999, vol. 399, issue 6735, 479-483

Abstract: Abstract The mitogen-activated protein kinase (MAPK) pathway is a highlyconserved eukaryotic signalling cascade that converts extracellular signals into various outputs, such as cell growth and differentiation1,2,3. MAPK is phosphorylated and activated by a specific MAPK kinase (MAPKK)4: MAPKK is therefore considered to be an activating regulator of MAPK. Pmk1 is a MAPK that regulates cell integrity5 and which, with calcineurin phosphatase, antagonizes chloride homeostasis6 in fission yeast. We have now identified Pek1, a MAPKK for Pmk1 MAPK. We show here that Pek1, in its unphosphorylated form, acts as a potent negative regulator of Pmk1 MAPK signalling. Mkh17, an upstream MAPKK kinase (MAPKKK), converts Pek1 from being an inhibitor to an activator. Our results indicate that Pek1 has a dual stimulatory and inhibitory function which depends on its phosphorylation state. This switch-like mechanism could contribute to the all-or-none physiological response mediated by the MAPK signalling pathway.

Date: 1999
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DOI: 10.1038/20951

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