Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein.

@article{GarrigueAntar2002PosttranslationalMO,
  title={Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein.},
  author={Laure Garrigue-Antar and Nichola Hartigan and Karl E Kadler},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 45},
  pages={43327-34}
}
Bone morphogenetic protein (BMP)-1 is a glycosylated metalloproteinase that is fundamental to the synthesis of a normal extracellular matrix because it cleaves type I procollagen, as well as other precursor proteins. Sequence analysis suggests that BMP-1 has six potential N-linked glycosylation sites (i.e. NXS/T) namely: Asn(91) (prodomain), Asn(142) (metalloproteinase domain), Asn(332) and Asn(363) (CUB1 domain), Asn(599) (CUB3 domain), and Asn(726) in the C-terminal-specific domain. In this… CONTINUE READING

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