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N-linked glycosylation restricts the function of Short gastrulation to bind and shuttle BMPs.
- Source :
-
Development (Cambridge, England) [Development] 2018 Nov 19; Vol. 145 (22). Date of Electronic Publication: 2018 Nov 19. - Publication Year :
- 2018
-
Abstract
- Disorders of N-linked glycosylation are increasingly reported in the literature. However, the targets that are responsible for the associated developmental and physiological defects are largely unknown. Bone morphogenetic proteins (BMPs) act as highly dynamic complexes to regulate several functions during development. The range and strength of BMP activity depend on interactions with glycosylated protein complexes in the extracellular milieu. Here, we investigate the role of glycosylation for the function of the conserved extracellular BMP antagonist Short gastrulation (Sog). We identify conserved N-glycosylated sites and describe the effect of mutating these residues on BMP pathway activity in Drosophila Functional analysis reveals that loss of individual Sog glycosylation sites enhances BMP antagonism and/or increases the spatial range of Sog effects in the tissue. Mechanistically, we provide evidence that N-terminal and stem glycosylation controls extracellular Sog levels and distribution. The identification of similar residues in vertebrate Chordin proteins suggests that N-glycosylation may be an evolutionarily conserved process that adds complexity to the regulation of BMP activity.<br />Competing Interests: Competing interestsThe authors declare no competing or financial interests.<br /> (© 2018. Published by The Company of Biologists Ltd.)
- Subjects :
- Amino Acid Sequence
Animals
Conserved Sequence
Drosophila Proteins chemistry
Drosophila melanogaster embryology
Drosophila melanogaster metabolism
Embryo, Nonmammalian metabolism
Extracellular Space metabolism
Glycosylation
Mutant Proteins metabolism
Polysaccharides metabolism
Protein Binding
Wings, Animal metabolism
Bone Morphogenetic Proteins metabolism
Drosophila Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1477-9129
- Volume :
- 145
- Issue :
- 22
- Database :
- MEDLINE
- Journal :
- Development (Cambridge, England)
- Publication Type :
- Academic Journal
- Accession number :
- 30355725
- Full Text :
- https://doi.org/10.1242/dev.167338