Structural highlights
Function[Q9VUG1_DROME] Cell surface proteoglycan that bears heparan sulfate.[RuleBase:RU003519] Publication Abstract from PubMedA relatively small number of proteins have been suggested to act as morphogens-signalling molecules that spread within tissues to organize tissue repair and the specification of cell fate during development. Among them are Wnt proteins, which carry a palmitoleate moiety that is essential for signalling activity(1-3). How a hydrophobic lipoprotein can spread in the aqueous extracellular space is unknown. Several mechanisms, such as those involving lipoprotein particles, exosomes or a specific chaperone, have been proposed to overcome this so-called Wnt solubility problem(4-6). Here we provide evidence against these models and show that the Wnt lipid is shielded by the core domain of a subclass of glypicans defined by the Dally-like protein (Dlp). Structural analysis shows that, in the presence of palmitoleoylated peptides, these glypicans change conformation to create a hydrophobic space. Thus, glypicans of the Dlp family protect the lipid of Wnt proteins from the aqueous environment and serve as a reservoir from which Wnt proteins can be handed over to signalling receptors. Glypicans shield the Wnt lipid moiety to enable signalling at a distance.,McGough IJ, Vecchia L, Bishop B, Malinauskas T, Beckett K, Joshi D, O'Reilly N, Siebold C, Jones EY, Vincent JP Nature. 2020 Jul 22. pii: 10.1038/s41586-020-2498-z. doi:, 10.1038/s41586-020-2498-z. PMID:32699409[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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