6tbu | pdb_00006tbu
Structure of Drosophila melanogaster Dispatched
Structural highlights
Function[DISP_DROME] Segment polarity protein which functions in hedgehog (Hh) signaling. Regulates the trafficking and the release of cholesterol-modified hedgehog protein from cells of the posterior compartment (P cells) and is hence required for the effective production of the Hh signal.[1] [2] [3] Publication Abstract from PubMedThe Hedgehog (Hh) signaling pathway controls embryonic development and adult tissue homeostasis in multicellular organisms. In Drosophila melanogaster, the pathway is primed by secretion of a dually lipid-modified morphogen, Hh, a process dependent on a membrane-integral protein Dispatched. Although Dispatched is a critical component of the pathway, the structural basis of its activity has, so far, not been described. Here, we describe a cryo-electron microscopy structure of the D. melanogaster Dispatched at 3.2-A resolution. The ectodomains of Dispatched adopt an open conformation suggestive of a receptor-chaperone role. A three-dimensional reconstruction of Dispatched bound to Hh confirms the ability of Dispatched to bind Hh but using a unique mode distinct from those previously observed in structures of Hh complexes. The structure may represent the state of the complex that precedes shedding of Hh from the surface of the morphogen-releasing cell. Cryo-EM structure of the Hedgehog release protein Dispatched.,Cannac F, Qi C, Falschlunger J, Hausmann G, Basler K, Korkhov VM Sci Adv. 2020 Apr 15;6(16):eaay7928. doi: 10.1126/sciadv.aay7928. eCollection, 2020 Apr. PMID:32494603[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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