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Proc Natl Acad Sci U S A 1998 Aug 04;9516:9337-42. doi: 10.1073/pnas.95.16.9337.
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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.

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

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.

PubMed ID: 9689081
PMC ID: PMC21339
Article link: Proc Natl Acad Sci U S A

Species referenced: Xenopus laevis
Genes referenced: acvr1 bmp4 bmp7.1 bmpr1a chrd.1 fst gsc inhba nog

Article Images: [+] show captions
References [+] :
Akiyama, Constitutively active BMP type I receptors transduce BMP-2 signals without the ligand in C2C12 myoblasts. 1997, Pubmed