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Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction network

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Title: Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction network
Authors: Jianlei Jia, Jipeng Jin, Qian Chen, Zan Yuan, Haiqin Li, Junhao Bian, Linsheng Gui
Source: Biological Research, Vol 53, Iss 1, Pp 1-13 (2020)
Publisher Information: BMC, 2020.
Publication Year: 2020
Collection: LCC:Biology (General)
Subject Terms: Sheep, BMPR-1B, Co-immunoprecipitation, Mass spectrometry, Protein–protein interaction, Biology (General), QH301-705.5
More Details: 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.
Document Type: article
File Description: electronic resource
Language: English
ISSN: 0717-6287
Relation: http://link.springer.com/article/10.1186/s40659-020-00290-7; https://doaj.org/toc/0717-6287
DOI: 10.1186/s40659-020-00290-7
Access URL: https://doaj.org/article/c6575b276c0a46bd90447a40658ddb6e
Accession Number: edsdoj.6575b276c0a46bd90447a40658ddb6e
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  Data: Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction network
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  Data: <searchLink fieldCode="AR" term="%22Jianlei+Jia%22">Jianlei Jia</searchLink><br /><searchLink fieldCode="AR" term="%22Jipeng+Jin%22">Jipeng Jin</searchLink><br /><searchLink fieldCode="AR" term="%22Qian+Chen%22">Qian Chen</searchLink><br /><searchLink fieldCode="AR" term="%22Zan+Yuan%22">Zan Yuan</searchLink><br /><searchLink fieldCode="AR" term="%22Haiqin+Li%22">Haiqin Li</searchLink><br /><searchLink fieldCode="AR" term="%22Junhao+Bian%22">Junhao Bian</searchLink><br /><searchLink fieldCode="AR" term="%22Linsheng+Gui%22">Linsheng Gui</searchLink>
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  Data: Biological Research, Vol 53, Iss 1, Pp 1-13 (2020)
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  Data: BMC, 2020.
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  Data: 2020
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  Data: <searchLink fieldCode="DE" term="%22Sheep%22">Sheep</searchLink><br /><searchLink fieldCode="DE" term="%22BMPR-1B%22">BMPR-1B</searchLink><br /><searchLink fieldCode="DE" term="%22Co-immunoprecipitation%22">Co-immunoprecipitation</searchLink><br /><searchLink fieldCode="DE" term="%22Mass+spectrometry%22">Mass spectrometry</searchLink><br /><searchLink fieldCode="DE" term="%22Protein–protein+interaction%22">Protein–protein interaction</searchLink><br /><searchLink fieldCode="DE" term="%22Biology+%28General%29%22">Biology (General)</searchLink><br /><searchLink fieldCode="DE" term="%22QH301-705%2E5%22">QH301-705.5</searchLink>
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  Data: 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.
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