中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
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
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
DOI10.1007/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
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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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