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PMID: 9689081 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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 of the United States of America ·Vol. 95 ·No. 16 ·1998-08-04 ·Pages 9337-42

Iemura S, Yamamoto TS, Takagi C, Uchiyama H, Natsume T, Shimasaki S, Sugino H, Ueno N

Abstract

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.

MeSH Terms
Animals Base Sequence Bone Morphogenetic Proteins/metabolism Cell Lineage DNA Primers Embryo, Nonmammalian Epidermal Cells Follistatin Glycoproteins/metabolism Protein Binding Xenopus/embryology
Chemicals
Bone Morphogenetic Proteins DNA Primers Follistatin Glycoproteins
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Iemura S
Department of Developmental Biology, National Institute for Basic Biology, 38 Nishigonaka, Myodaiji, Okazaki, 444-8585 Japan.
Yamamoto T S
Takagi C
Uchiyama H
Natsume T
Shimasaki S
Sugino H
Ueno N
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.95.16.9337
Published
1998-08-04
Pages
9337-42
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC21339
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.95.16.9337 PMC Full Text View journal details
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