Novel Ser74 of NF-κB/IκBα phosphorylated by MAPK/ERK regulates temperature adaptation in oysters.
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| Auteurs principaux: | , , , , , , , , |
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| Format: | Artículo científico |
| Langue: | en |
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Cell communication and signaling : CCS
2024
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| _version_ | 1868266282449633281 |
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| author | Wang, Chaogang Jiang, Zhuxiang Du, Mingyang Cong, Rihao Wang, Wei Zhang, Taiping Chen, Jincheng Zhang, Guofan Li, Li |
| author_facet | Wang, Chaogang Jiang, Zhuxiang Du, Mingyang Cong, Rihao Wang, Wei Zhang, Taiping Chen, Jincheng Zhang, Guofan Li, Li Wang, Chaogang Jiang, Zhuxiang Du, Mingyang Cong, Rihao Wang, Wei Zhang, Taiping Chen, Jincheng Zhang, Guofan Li, Li |
| collection | PubMed - marine biology |
| contents | Novel Ser74 of NF-κB/IκBα phosphorylated by MAPK/ERK regulates temperature adaptation in oysters. Wang, Chaogang Jiang, Zhuxiang Du, Mingyang Cong, Rihao Wang, Wei Zhang, Taiping Chen, Jincheng Zhang, Guofan Li, Li Animals Phosphorylation NF-kappa B Ostreidae NF-KappaB Inhibitor alpha Serine MAP Kinase Signaling System Temperature Ubiquitination Adaptation, Physiological Amino Acid Sequence Extracellular Signal-Regulated MAP Kinases Phosphorylation of Ser32 and Ser36 controls the degradation of IκBα is the conserved cascade mechanisms of immune core signaling pathway, NF-κB pathway in metazoans, but it's response to abiotic stress and the presence of novel phosphorylation mechanisms in other species remain unclear. Herein, we reported a novel heat-induced phosphorylation site (Ser74) at oysters' major IκBα, which independently regulated ubiquitination-proteasome degradation without the requirement of phosphorylation at S32 and S36. And this site was phosphorylated by ERK/MAPK pathway, which then promoted REL nuclear translocation to activate cell survival related genes to defend heat-stress. The MAPK-NF-κB cascade exhibited divergent thermal responses and adaptation patterns between two congeneric oyster species with differential habitat temperatures, indicating its involvement in shaping temperature adaptation. This study demonstrated that the existence of complex and unique phosphorylation-mediated signaling transduction mechanism in marine invertebrates, and expanded our understanding of the evolution and function of established classical pathway crosstalk mechanisms. |
| format | Artículo científico |
| id | pubmed_39529137 |
| institution | PubMed |
| language | en |
| publishDate | 2024 |
| publisher | Cell communication and signaling : CCS |
| record_format | pubmed |
| spellingShingle | Novel Ser74 of NF-κB/IκBα phosphorylated by MAPK/ERK regulates temperature adaptation in oysters. Wang, Chaogang Jiang, Zhuxiang Du, Mingyang Cong, Rihao Wang, Wei Zhang, Taiping Chen, Jincheng Zhang, Guofan Li, Li Animals Phosphorylation NF-kappa B Ostreidae NF-KappaB Inhibitor alpha Serine MAP Kinase Signaling System Temperature Ubiquitination Adaptation, Physiological Amino Acid Sequence Extracellular Signal-Regulated MAP Kinases Novel Ser74 of NF-κB/IκBα phosphorylated by MAPK/ERK regulates temperature adaptation in oysters. Wang, Chaogang Jiang, Zhuxiang Du, Mingyang Cong, Rihao Wang, Wei Zhang, Taiping Chen, Jincheng Zhang, Guofan Li, Li Animals Phosphorylation NF-kappa B Ostreidae NF-KappaB Inhibitor alpha Serine MAP Kinase Signaling System Temperature Ubiquitination Adaptation, Physiological Amino Acid Sequence Extracellular Signal-Regulated MAP Kinases Phosphorylation of Ser32 and Ser36 controls the degradation of IκBα is the conserved cascade mechanisms of immune core signaling pathway, NF-κB pathway in metazoans, but it's response to abiotic stress and the presence of novel phosphorylation mechanisms in other species remain unclear. Herein, we reported a novel heat-induced phosphorylation site (Ser74) at oysters' major IκBα, which independently regulated ubiquitination-proteasome degradation without the requirement of phosphorylation at S32 and S36. And this site was phosphorylated by ERK/MAPK pathway, which then promoted REL nuclear translocation to activate cell survival related genes to defend heat-stress. The MAPK-NF-κB cascade exhibited divergent thermal responses and adaptation patterns between two congeneric oyster species with differential habitat temperatures, indicating its involvement in shaping temperature adaptation. This study demonstrated that the existence of complex and unique phosphorylation-mediated signaling transduction mechanism in marine invertebrates, and expanded our understanding of the evolution and function of established classical pathway crosstalk mechanisms. |
| title | Novel Ser74 of NF-κB/IκBα phosphorylated by MAPK/ERK regulates temperature adaptation in oysters. |
| topic | Animals Phosphorylation NF-kappa B Ostreidae NF-KappaB Inhibitor alpha Serine MAP Kinase Signaling System Temperature Ubiquitination Adaptation, Physiological Amino Acid Sequence Extracellular Signal-Regulated MAP Kinases |
| url | https://pubmed.ncbi.nlm.nih.gov/39529137/ |