MAPK/ERK-PK(Ser11) pathway regulates divergent thermal metabolism of two congeneric oyster species

Pyruvate kinase (PK), as a key rate-limiting enzyme in glycolysis, has been widely used to assess the stress tolerance and sensitivity of organisms. However, its phosphorylation regulatory mechanisms mainly focused on human cancer research, with no reports in marine organisms. In this study, we firs...

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Published iniScience Vol. 27; no. 7; p. 110321
Main Authors Wang, Chaogang, Du, Mingyang, Jiang, Zhuxiang, Cong, Rihao, Wang, Wei, Zhang, Taiping, Chen, Jincheng, Zhang, Guofan, Li, Li
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 19.07.2024
Elsevier
Subjects
Evolutionary biology
Molecular biology
Zoology
Evolutionary biology
Molecular biology
Zoology
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Summary:Pyruvate kinase (PK), as a key rate-limiting enzyme in glycolysis, has been widely used to assess the stress tolerance and sensitivity of organisms. However, its phosphorylation regulatory mechanisms mainly focused on human cancer research, with no reports in marine organisms. In this study, we firstly reported a conserved PK Ser11 phosphorylation site in mollusks, which enhanced enzyme activity by promoting substrate binding, thereby regulating divergent thermal metabolism of two allopatric congeneric oyster species with differential habitat temperature. It was phosphorylated by ERK kinase, and regulated by the classical MAPK pathway. The MAPK/ERK-PK signaling cascade responded to increased environmental temperature and exhibited stronger activation pattern in the relatively thermotolerant species (Crassostrea angulata), indicating its involvement in shaping temperature adaptation. These findings highlight the presence of complex and unique phosphorylation-mediated signaling transduction mechanisms in marine organisms, and provide new insights into the evolution and function of the crosstalk between classical pathways. [Display omitted] •The Ser11 site of PK is conserved in Gastropoda and Bivalvia•Phosphorylation of Ser11 site of PK significantly enhances its enzymatic activity•MAPK/ERK1/2 phosphorylates the Ser11 site of PK under heat stress•MAPK/ERK-PK cascade mediates divergent thermal metabolism capacity Zoology; Molecular biology; Evolutionary biology
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ISSN:2589-0042
2589-0042
DOI:10.1016/j.isci.2024.110321