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Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo
Open accessAbstract
In early development of Xenopus laevis, it is known that activities of polypeptide growth factors are negatively regulated by their binding proteins. In this study, follistatin, originally known as an activin-binding protein, was shown to inhibit all aspects of bone morphogenetic protein (BMP) activity in early Xenopus embryos. Furthermore, using a surface plasmon resonance biosensor, we demonstrated that follistatin can directly interact with multiple BMPs at significantly high affinities. Interestingly, follistatin was found to be noncompetitive with the BMP receptor for ligand binding and to form a trimeric complex with BMP and its receptor. The results suggest that follistatin acts as an organizer factor in early amphibian embryogenesis by inhibiting BMP activities by a different mechanism from that used by chordin and noggin.
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Citations
Cited by
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Lee, S.-J. (2004) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.20.012103.135836 · Cited by 819
The establishment of spemann's organizer and patterning of the vertebrate embryo
De Robertis, E. M., Larraín, J., Oelgeschläger, M., & Wessely, O. (2000) · Nature Reviews Genetics · doi:10.1038/35042039 · Cited by 429
Follistatin complexes Myostatin and antagonises Myostatin-mediated inhibition of myogenesis
Amthor, H., Nicholas, G., McKinnell, I., Kemp, C. F., Sharma, M., Kambadur, R., & Patel, K. (2004) · Developmental Biology · doi:10.1016/j.ydbio.2004.01.046 · Cited by 401
Matrix GLA Protein, a Regulatory Protein for Bone Morphogenetic Protein-2
Zebboudj, A. F., Imura, M., & Boström, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109683200 · Cited by 357
HtrA1 serine protease inhibits signaling mediated by Tgfβ family proteins
Oka, C., Tsujimoto, R., Kajikawa, M., Koshiba-Takeuchi, K., Ina, J., Yano, M., Tsuchiya, A., Ueta, Y., Soma, A., Kanda, H., et al. (2004) · Development · doi:10.1242/dev.00999 · Cited by 334
Metadata
- Authors
- Iemura, S.-I., Yamamoto, T. S., Takagi, C., Uchiyama, H., Natsume, T., Shimasaki, S., Sugino, H., & Ueno, N.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-08-04
- Volume
- 95
- Issue
- 16
- Pages
- 9337-9342
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2131304500
- Cited by
- 450
- References
- 0
- FWCI
- 10.47
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo. https://app.cochat.ai/papers/10.1073/pnas.95.16.9337
- The paper
- Iemura, S.-I., Yamamoto, T. S., Takagi, C., Uchiyama, H., Natsume, T., Shimasaki, S., Sugino, H., & Ueno, N. (1998). Direct binding of follistatin to a complex of bone-morphogenetic protein and its receptor inhibits ventral and epidermal cell fates in early Xenopus embryo. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.16.9337
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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