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 c...
Guardado en:
| Autores principales: | , , , , , , |
|---|---|
| Lenguaje: | English |
| Publicado: |
Sociedad de Biología de Chile
2020
|
| Materias: | |
| Acceso en línea: | http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602020000100220 |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| id |
oai:scielo:S0716-97602020000100220 |
|---|---|
| record_format |
dspace |
| spelling |
oai:scielo:S0716-976020200001002202020-06-25Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction networkJia,JianleiJin,JipengChen,QianYuan,ZanLi,HaiqinBian,JunhaoGui,Linsheng Sheep BMPR-1B Co-immunoprecipitation Mass spectrometry Protein–protein interaction 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.info:eu-repo/semantics/openAccessSociedad de Biología de ChileBiological Research v.53 20202020-01-01text/htmlhttp://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602020000100220en10.1186/s40659-020-00290-7 |
| institution |
Scielo Chile |
| collection |
Scielo Chile |
| language |
English |
| topic |
Sheep BMPR-1B Co-immunoprecipitation Mass spectrometry Protein–protein interaction |
| spellingShingle |
Sheep BMPR-1B Co-immunoprecipitation Mass spectrometry Protein–protein interaction Jia,Jianlei Jin,Jipeng Chen,Qian Yuan,Zan Li,Haiqin Bian,Junhao Gui,Linsheng Eukaryotic expression, Co-IP and MS identify BMPR-1B protein–protein interaction network |
| 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. |
| author |
Jia,Jianlei Jin,Jipeng Chen,Qian Yuan,Zan Li,Haiqin Bian,Junhao Gui,Linsheng |
| author_facet |
Jia,Jianlei Jin,Jipeng Chen,Qian Yuan,Zan Li,Haiqin Bian,Junhao Gui,Linsheng |
| author_sort |
Jia,Jianlei |
| title |
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_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_sort |
eukaryotic expression, co-ip and ms identify bmpr-1b protein–protein interaction network |
| publisher |
Sociedad de Biología de Chile |
| publishDate |
2020 |
| url |
http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0716-97602020000100220 |
| work_keys_str_mv |
AT jiajianlei eukaryoticexpressioncoipandmsidentifybmpr1bprotein8211proteininteractionnetwork AT jinjipeng eukaryoticexpressioncoipandmsidentifybmpr1bprotein8211proteininteractionnetwork AT chenqian eukaryoticexpressioncoipandmsidentifybmpr1bprotein8211proteininteractionnetwork AT yuanzan eukaryoticexpressioncoipandmsidentifybmpr1bprotein8211proteininteractionnetwork AT lihaiqin eukaryoticexpressioncoipandmsidentifybmpr1bprotein8211proteininteractionnetwork AT bianjunhao eukaryoticexpressioncoipandmsidentifybmpr1bprotein8211proteininteractionnetwork AT guilinsheng eukaryoticexpressioncoipandmsidentifybmpr1bprotein8211proteininteractionnetwork |
| _version_ |
1718441604850647040 |