PfSMAD1/5 Can Interact with PfSMAD4 to Inhibit PfMSX to Regulate Shell Biomineralization in Pinctada fucata martensii
文献类型:期刊论文
作者 | Shi, Yu; Zhao, Mi; He, Maoxian |
刊名 | MARINE BIOTECHNOLOGY
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出版日期 | 2020 |
卷号 | 22期号:2页码:246 |
关键词 | PfSMAD1 5 PfBMP2-SMADs-MSX signal pathway Biomineralization Pinctada fucata martensii |
ISSN号 | 1436-2228 |
DOI | 10.1007/s10126-020-09948-5 |
英文摘要 | The BMP2 signal transduced by SMAD1/5 plays an important role in osteoblast differentiation and bone formation. Shell formation of Pinctada fucata martensii is a typical biomineralization process that is similar to that of teeth/bone formation. However, whether the Pinctada fucata BMP2 (PfBMP2) signal transduced by PfSMAD1/5 occurs in P. f. martensii, how the PfBMP2 signal is transduced by PfSMAD1/5, and how PfSMAD1/5 regulates the biomineralization process in this species and other shellfish are poorly understood. Therefore, injection experiments of recombinant PfBMP2 and inhibitor dorsomorphin revealed that PfSMAD1/5 can transduce PfBMP2 signals. Subcellular localization and bimolecular fluorescence complementation assays indicated that PfSMAD1/5 phosphorylated by PfBMPR1b interacts with PfSMAD4 in the cytoplasm to form a complex, which translocates to the nucleus to transduce PfBMP2 signals. Co-immunoprecipitation and luciferase assays revealed that PfSMAD1/5 may interact with PfMSX to dislodge it from its binding element, resulting in initiation of mantle gene transcription. The in vivo functional assay showed that knockdown of PfMSAD1/5 decreased expression of shell matrix genes and disordered the nacreous layer, and the correlation assay of shell regeneration showed the concomitant expression pattern of PfSMAD1/5 and shell matrix genes. Together, these data showed that PfSMAD1/5 can transduce PfBMP2 signals to regulate shell biomineralization in P. f. martensii, which illustrated conservation of the BMP2-SMAD signal pathway among invertebrates. Particularly, the results suggest that there is only one PfMSX gene, which functions like the Hox gene in vertebrates, that interacts with PfSMAD1/5 in a protein-protein action form and plays the role of transcription repressor. |
资助机构 | National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [41606151]; Natural Science Foundation of Guangdong ProvinceNational Natural Science Foundation of Guangdong Province [2019A1515011968]; Science and Technology Planning Project of Guangdong Province [2017B0303014052]; Earmarked Fund for Modern Agro-industry Technology Research System [CARS-49] ; National Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [41606151]; Natural Science Foundation of Guangdong ProvinceNational Natural Science Foundation of Guangdong Province [2019A1515011968]; Science and Technology Planning Project of Guangdong Province [2017B0303014052]; Earmarked Fund for Modern Agro-industry Technology Research System [CARS-49] |
源URL | [http://ir.scsio.ac.cn/handle/344004/18468] ![]() |
专题 | 南海海洋研究所_中科院海洋生物资源可持续利用重点实验室 |
作者单位 | Chinese Acad Sci, South China Sea Inst Oceanol, CAS Key Lab Trop Marine Bioresources & Ecol, Guangdong Prov Key Lab Appl Marine Biol, 164 West Xingang Rd, Guangzhou 510301, Peoples R China |
推荐引用方式 GB/T 7714 | Shi, Yu,Zhao, Mi,He, Maoxian. PfSMAD1/5 Can Interact with PfSMAD4 to Inhibit PfMSX to Regulate Shell Biomineralization in Pinctada fucata martensii[J]. MARINE BIOTECHNOLOGY,2020,22(2):246, 262. |
APA | Shi, Yu,Zhao, Mi,&He, Maoxian.(2020).PfSMAD1/5 Can Interact with PfSMAD4 to Inhibit PfMSX to Regulate Shell Biomineralization in Pinctada fucata martensii.MARINE BIOTECHNOLOGY,22(2),246. |
MLA | Shi, Yu,et al."PfSMAD1/5 Can Interact with PfSMAD4 to Inhibit PfMSX to Regulate Shell Biomineralization in Pinctada fucata martensii".MARINE BIOTECHNOLOGY 22.2(2020):246. |
入库方式: OAI收割
来源:南海海洋研究所
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