PI3K-AKT-mediated phosphorylation of Thr260 in CgCaspase-3/6/7 regulates heat-induced activation in oysters
文献类型：期刊论文
| 作者 | Wang, Chaogang2,3,4,8 ; Du, Mingyang1,2,3; Jiang, Zhuxiang1,2,3; Cong, Rihao2,3,4,7; Wang, Wei2,3,6; Zhang, Taiping1,2,3; Chen, Jincheng1,2,3; Zhang, Guofan2,3,4,5,7,8; Li, Li1,2,3,5,6,8
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| 刊名 | COMMUNICATIONS BIOLOGY
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| 出版日期 | 2024-11-07 |
| 卷号 | 7期号:1页码:15 |
| DOI | 10.1038/s42003-024-07184-4 |
| 通讯作者 | Li, Li(lili@qdio.ac.cn) |
| 英文摘要 | Cysteine-aspartic proteases (caspases) are critical drivers of apoptosis, exhibiting expansion and domain shuffling in mollusks. However, the functions and regulatory mechanisms of these caspases remain unclear. In this study, we identified a group of Caspase-3/6/7 in Bivalvia and Gastropoda with a long inter-subunit linker (IL) that inhibits cleavage activation. Within this region, we found that conserved phosphorylation at Thr260 in oysters, mediated by the PI3K-AKT pathway, suppresses heat-induced activation. This mechanism is involved in divergent temperature adaptation between two allopatric congeneric oyster species, the relatively cold-adapted Crassostrea gigas and warm-adapted Crassostrea angulata. Our study elucidates the role of these effector caspase members and their long IL in bivalves, revealing that the PI3K-AKT pathway phosphorylates Thr260 on CgCASP3/6/7's linker to inhibit heat-induced activation. These findings provide insights into the evolution and function of apoptotic regulatory mechanisms in bivalves. Caspase phosphorylation determines differences in heat stress response and apoptosis between oyster species. |
| WOS关键词 | 3-PHOSPHOINOSITIDE-DEPENDENT PROTEIN KINASE-1 ; IN-VITRO ; APOPTOSIS ; CASPASES ; AKT ; BLOCKS ; IDENTIFICATION ; EXPRESSION ; SURVIVAL ; 3-KINASE |
| 资助项目 | National Key R&D Program of China[2022YFD2400304] ; Key Research and Development Program of Shandong[2022LZGC015] ; Key Research and Development Program of Shandong[ZFJH202309] ; China Agriculture Research System of MOF[CARS-49] |
| WOS研究方向 | Life Sciences & Biomedicine - Other Topics ; Science & Technology - Other Topics |
| 语种 | 英语 |
| WOS记录号 | WOS:001351597700007 |
| 出版者 | NATURE PORTFOLIO |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/199399]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 通讯作者 | Li, Li |
| 作者单位 | 1.Univ Chinese Acad Sci, Beijing, Peoples R China 2.Natl & Local Joint Engn Lab Ecol Mariculture, Qingdao, Peoples R China 3.Chinese Acad Sci, Inst Oceanol, Shandong Prov Key Lab Expt Marine Biol, Qingdao, Peoples R China 4.Qingdao Marine Sci & Technol Ctr, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China 5.Shandong Technol Innovat Ctr Oyster Seed Ind, Qingdao, Peoples R China 6.Qingdao Marine Sci & Technol Ctr, Lab Marine Fisheries Sci & Food Prod Proc, Qingdao, Peoples R China 7.Southern Marine Sci & Engn Guangdong Lab Zhanjiang, Zhanjiang, Peoples R China 8.Chinese Acad Sci, Inst Oceanol, Key Lab Breeding Biotechnol & Sustainable Aquacult, Qingdao, Peoples R China |
| 推荐引用方式 GB/T 7714 | Wang, Chaogang,Du, Mingyang,Jiang, Zhuxiang,et al. PI3K-AKT-mediated phosphorylation of Thr260 in CgCaspase-3/6/7 regulates heat-induced activation in oysters[J]. COMMUNICATIONS BIOLOGY,2024,7(1):15. |
| APA | Wang, Chaogang.,Du, Mingyang.,Jiang, Zhuxiang.,Cong, Rihao.,Wang, Wei.,...&Li, Li.(2024).PI3K-AKT-mediated phosphorylation of Thr260 in CgCaspase-3/6/7 regulates heat-induced activation in oysters.COMMUNICATIONS BIOLOGY,7(1),15. |
| MLA | Wang, Chaogang,et al."PI3K-AKT-mediated phosphorylation of Thr260 in CgCaspase-3/6/7 regulates heat-induced activation in oysters".COMMUNICATIONS BIOLOGY 7.1(2024):15. |
入库方式： OAI收割
来源：海洋研究所
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