ArticleThe Journal of biological chemistry2025
Marfan syndrome variation of the POGLUT2 and POGLUT3 consensus sequence can produce aberrant fibrillin-1 O-glucosylation.
Article in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Structural basis of EGF-repeat O-glucosylation by the protein O-glucosyltransferase POGLUT2.The Journal of biological chemistry · 2026Article
- POGLUT2/3 mediated EGF O-glucosylation promotes separation of digits 2 and 3 by influencing fibrillin network reorganization, signaling, and cell dynamics.Developmental biology · 2025Article
- DifferentialProceedings of the National Academy of Sciences of the United States of America · 2025Article
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5 authors.
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Abstract
Fibrillin-1 (FBN1) is an essential component of the extracellular matrix, forming microfibril bundles that are important for the proper development of elastic tissues found in the aorta and lung, as well as nonelastic tissue found in the eyes and skeleton. Many missense mutations in the FBN1 gene are associated with Marfan syndrome (MFS), a common developmental disorder. FBN1 contains 47 epidermal growth factor-like (EGF) repeats, which are protein domains characterized by six cysteines (C) and three disulfide bonds. Over half of these EGF repeats are modified with an O-glucose monosaccharide added by protein O-glucosyltransferase 2 and/or 3 (POGLUT2/3). Previous studies showed that O-glucose modifies the serine within the putative consensus sequence between C three and four: C
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