Characterization and cloning of a receptor for BMP-2 and BMP-4 from NIH 3T3 cells Journal Article
| Authors: | Koenig, B. B.; Cook, J. S.; Wolsing, D. H.; Ting, J.; Tiesman, J. P.; Correa, P. E.; Olson, C. A.; Pecquet, A. L.; Ventura, F.; Grant, R. A.; Chen, G. X.; Wrana, J. L.; Massagué, J.; Rosenbaum, J. S. |
| Article Title: | Characterization and cloning of a receptor for BMP-2 and BMP-4 from NIH 3T3 cells |
| Abstract: | The bone morphogenetic proteins (BMPs) are a group of transforming growth factor β (TGF-β)-related factors whose only receptor identified to date is the product of the daf-4 gene from Caenorhabditis elegans. Mouse embryonic NIH 3T3 fibroblasts display high-affinity 125I-BMP-4 binding sites. Binding assays are not possible with the isoform 125I-BMP-2 unless the positively charged N-terminal sequence is removed to create a modified BMP- 2, 125I-DR-BMP-2. Cross-competition experiments reveal that BMP-2 and BMP- 4 interact with the same binding sites. Affinity cross-linking assays show that both BMPs interact with cell surface proteins corresponding in size to the type I (57- to 62-kDa) and type II (75- to 82-kDa) receptor components for TGF-β and activin. Using a PCR approach, we have cloned a cDNA from NIH 3T3 cells which encodes a novel member of the transmembrane serine/threonine kinase family most closely resembling the cloned type I receptors for TGF-β and activin. Transient expression of this receptor in COS-7 cells leads to an increase in specific 125I-BMP-4 binding and the appearance of a major affinity-labeled product of ~64 kDa that can be labeled by either tracer. This receptor has been named BRK-1 in recognition of its ability to bind BMP- 2 and BMP-4 and its receptor kinase structure. Although BRK-1 does not require cotransfection of a type II receptor in order to bind ligand in COS cells, complex formation between BRK-1 and the BMP type II receptor DAF-4 can be demonstrated when the two receptors are coexpressed, affinity labeled, and immunoprecipitated with antibodies to either receptor subunit. We conclude that BRK-1 is a putative BMP type I receptor capable of interacting with a known type II receptor for BMPs. |
| Keywords: | controlled study; nonhuman; polymerase chain reaction; animal cell; mouse; bone morphogenetic protein; transforming growth factor beta; animalia; molecular cloning; amino terminal sequence; isotope labeling; caenorhabditis elegans; monkey; cell strain 3t3; receptor binding; complementary dna; cell surface receptor; growth factor receptor; avidin; priority journal; article |
| Journal Title: | Molecular and Cellular Biology |
| Volume: | 14 |
| Issue: | 9 |
| ISSN: | 0270-7306 |
| Publisher: | American Society for Microbiology |
| Date Published: | 1994-09-01 |
| Start Page: | 5961 |
| End Page: | 5974 |
| Language: | English |
| DOI: | 10.1128/mcb.14.9.5961 |
| PROVIDER: | scopus |
| PMCID: | PMC359122 |
| PUBMED: | 8065329 |
| DOI/URL: | |
| Notes: | Export Date: 14 January 2019 -- Article -- CODEN: MCEBD C2 -- Source: Scopus |
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