Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction network
Abstract Background BMPR-1B is part of the transforming growth factor β super family and plays a pivotal role in ewe litter size. Functional loss of exon-8 mutations in the BMPR-1B gene (namely the FecB gene) can increase both the ewe ovulation rate and litter size. Results This study constructed a...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2020-05-01
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| Series: | Biological Research |
| Subjects: | |
| Online Access: | http://link.springer.com/article/10.1186/s40659-020-00290-7 |
| _version_ | 1818720417237434368 |
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| author | Jianlei Jia Jipeng Jin Qian Chen Zan Yuan Haiqin Li Junhao Bian Linsheng Gui |
| author_facet | Jianlei Jia Jipeng Jin Qian Chen Zan Yuan Haiqin Li Junhao Bian Linsheng Gui |
| author_sort | Jianlei Jia |
| collection | DOAJ |
| description | Abstract Background BMPR-1B is part of the transforming growth factor β super family and plays a pivotal role in ewe litter size. Functional loss of exon-8 mutations in the BMPR-1B gene (namely the FecB gene) can increase both the ewe ovulation rate and litter size. Results This study constructed a eukaryotic expression system, prepared a monoclonal antibody, and characterized BMPR-1B/FecB protein–protein interactions (PPIs). Using Co-immunoprecipitation coupled to mass spectrometry (Co-IP/MS), 23 proteins were identified that specifically interact with FecB in ovary extracts of ewes. Bioinformatics analysis of selected PPIs demonstrated that FecB associated with several other BMPs, primarily via signal transduction in the ovary. FecB and its associated interaction proteins enriched the reproduction process via BMP2 and BMP4 pathways. Signal transduction was identified via Smads proteins and TGF-beta signaling pathway by analyzing the biological processes and pathways. Moreover, other target proteins (GDF5, GDF9, RhoD, and HSP 10) that interact with FecB and that are related to ovulation and litter size in ewes were identified. Conclusions In summary, this research identified a novel pathway and insight to explore the PPi network of BMPR-1B. |
| first_indexed | 2024-12-17T20:22:30Z |
| format | Article |
| id | doaj.art-c6575b276c0a46bd90447a40658ddb6e |
| institution | Directory Open Access Journal |
| issn | 0717-6287 |
| language | English |
| last_indexed | 2024-12-17T20:22:30Z |
| publishDate | 2020-05-01 |
| publisher | BMC |
| record_format | Article |
| series | Biological Research |
| spelling | doaj.art-c6575b276c0a46bd90447a40658ddb6e2022-12-21T21:33:53ZengBMCBiological Research0717-62872020-05-0153111310.1186/s40659-020-00290-7Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction networkJianlei Jia0Jipeng Jin1Qian Chen2Zan Yuan3Haiqin Li4Junhao Bian5Linsheng Gui6Key of Laboratory of Plateau Ecology and Agriculture, Qinghai UniversityKey of Laboratory of Plateau Ecology and Agriculture, Qinghai UniversityCollege of Agriculture and Animal Husbandry, Qinghai UniversityCollege of Agriculture and Animal Husbandry, Qinghai UniversityCollege of Agriculture and Animal Husbandry, Qinghai UniversityCollege of Agriculture and Animal Husbandry, Qinghai UniversityKey of Laboratory of Plateau Ecology and Agriculture, Qinghai UniversityAbstract Background BMPR-1B is part of the transforming growth factor β super family and plays a pivotal role in ewe litter size. Functional loss of exon-8 mutations in the BMPR-1B gene (namely the FecB gene) can increase both the ewe ovulation rate and litter size. Results This study constructed a eukaryotic expression system, prepared a monoclonal antibody, and characterized BMPR-1B/FecB protein–protein interactions (PPIs). Using Co-immunoprecipitation coupled to mass spectrometry (Co-IP/MS), 23 proteins were identified that specifically interact with FecB in ovary extracts of ewes. Bioinformatics analysis of selected PPIs demonstrated that FecB associated with several other BMPs, primarily via signal transduction in the ovary. FecB and its associated interaction proteins enriched the reproduction process via BMP2 and BMP4 pathways. Signal transduction was identified via Smads proteins and TGF-beta signaling pathway by analyzing the biological processes and pathways. Moreover, other target proteins (GDF5, GDF9, RhoD, and HSP 10) that interact with FecB and that are related to ovulation and litter size in ewes were identified. Conclusions In summary, this research identified a novel pathway and insight to explore the PPi network of BMPR-1B.http://link.springer.com/article/10.1186/s40659-020-00290-7SheepBMPR-1BCo-immunoprecipitationMass spectrometryProtein–protein interaction |
| spellingShingle | Jianlei Jia Jipeng Jin Qian Chen Zan Yuan Haiqin Li Junhao Bian Linsheng Gui Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction network Biological Research Sheep BMPR-1B Co-immunoprecipitation Mass spectrometry Protein–protein interaction |
| title | Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction network |
| title_full | Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction network |
| title_fullStr | Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction network |
| title_full_unstemmed | Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction network |
| title_short | Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction network |
| title_sort | eukaryotic expression co ip and ms identify bmpr 1b protein protein interaction network |
| topic | Sheep BMPR-1B Co-immunoprecipitation Mass spectrometry Protein–protein interaction |
| url | http://link.springer.com/article/10.1186/s40659-020-00290-7 |
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