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Article

Different requirements for proteolytic processing of bone morphogenetic protein 5/6/7/8 ligands in Drosophila melanogaster.

The Journal of biological chemistry - 17 Feb 2012

Fritsch Cornelia, Sawala Annick, Harris Robin, Maartens Aidan, Sutcliffe Catherine, Ashe Hilary L, Ray Robert P

Abstract excerpt

Bone morphogenetic proteins (BMPs) are synthesized as proproteins that undergo proteolytic processing by furin/subtilisin proprotein convertases to release the active ligand. Here we study processing of BMP5/6/7/8 proteins, including the Drosophila orthologs Glass Bottom Boat (Gbb) and Screw (Scw) and human BMP7. Gbb and Scw have three functional furin/subtilisin proprotein convertase cleavage sites; two between...

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Source

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Identifiers

PMID: 22199351
DOI: 10.1074/jbc.M111.316745
PMCID: PMC3285362

Genes

BMP7
BMP5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Different requirements for proteolytic processing of bone morphogenetic protein 5/6/7/8 ligands in Drosophila melanogaster.PMID 22199351Read ↗

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The prodomain of BMP4 is necessary and sufficient to generate stable BMP4/7 heterodimers with enhanced bioactivity in vivoSemantic proximity Read ↗

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Simultaneous rather than ordered cleavage of two sites within the BMP4 prodomain leads to loss of ligand in mice.Semantic proximity Read ↗

SPC4, SPC6, and the novel protease SPC7 are coexpressed with bone morphogenetic proteins at distinct sites during embryogenesis.Semantic proximity Read ↗

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Genetic analysis of the bone morphogenetic protein-related gene, gbb, identifies multiple requirements during Drosophila development.Semantic proximity Read ↗

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