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Structure of bone morphogenetic protein 9 procomplex.

Li-Zhi Mi1, Christopher T Brown2, Yijie Gao2

  • 1Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115; Program in Cellular and Molecular Medicine, Children's Hospital Boston, Boston, MA 02115; Department of Molecular and Structural Biology, School of Life Sciences, Tianjin University, Tianjin 300072, China;

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Bone morphogenetic proteins (BMPs) regulate development. This study reveals how BMP prodomain structures control their activation, offering insights into TGF-β family signaling and therapeutic potential.

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Area of Science:

  • Molecular Biology
  • Developmental Biology
  • Structural Biology

Background:

  • Bone morphogenetic proteins (BMPs) are crucial developmental regulators within the TGF-β superfamily.
  • BMPs function as procomplexes, comprising a growth factor dimer and prodomains, but the mechanisms governing their latent or active states remain unclear.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying the latency and activation of BMP procomplexes.
  • To understand how prodomain structure influences TGF-β family member regulation and receptor interactions.

Main Methods:

  • Comparative structural analysis of pro-BMP9, pro-BMP7, and pro-TGF-β1 conformations.
  • Investigation of prodomain interactions with growth factors and potential competition between regulatory elements.

Main Results:

  • Pro-BMP9 and pro-BMP7 exhibit an open-armed, nonlatent conformation, contrasting with the cross-armed, latent conformation of pro-TGF-β1.
  • Prodomain arm domains associate with growth factors, while N- and C-terminal elements differentially interact, potentially regulating latency.
  • Sequence conservation indicates pro-BMP9 can adopt both conformations, suggesting dynamic regulation.

Conclusions:

  • Prodomain structure is a key determinant of BMP latency and activation.
  • Extracellular matrix interactors may stabilize latent BMP conformations, controlling transitions to active states.
  • Understanding these mechanisms provides insights into TGF-β signaling pathways and potential therapeutic strategies.