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Structural Basis of WLS/Evi-Mediated Wnt Transport and Secretion.
Nygaard, Rie; Yu, Jia; Kim, Jonathan; Ross, Daniel R; Parisi, Giacomo; Clarke, Oliver B; Virshup, David M; Mancia, Filippo.
Afiliación
  • Nygaard R; Department of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA.
  • Yu J; Programme in Cancer and Stem Cell Biology, Duke-NUS Medical School, Singapore 169857, Singapore.
  • Kim J; Department of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA.
  • Ross DR; Department of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA.
  • Parisi G; Department of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA.
  • Clarke OB; Department of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA; Department of Anesthesiology, Columbia University Irving Medical Center, New York, NY 10032, USA.
  • Virshup DM; Programme in Cancer and Stem Cell Biology, Duke-NUS Medical School, Singapore 169857, Singapore; Department of Pediatrics, Duke University School of Medicine, Durham, NC 27705, USA. Electronic address: david.virshup@duke-nus.edu.sg.
  • Mancia F; Department of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY 10032, USA. Electronic address: fm123@cumc.columbia.edu.
Cell ; 184(1): 194-206.e14, 2021 01 07.
Article en En | MEDLINE | ID: mdl-33357447
Wnts are evolutionarily conserved ligands that signal at short range to regulate morphogenesis, cell fate, and stem cell renewal. The first and essential steps in Wnt secretion are their O-palmitoleation and subsequent loading onto the dedicated transporter Wntless/evenness interrupted (WLS/Evi). We report the 3.2 Å resolution cryogenic electron microscopy (cryo-EM) structure of palmitoleated human WNT8A in complex with WLS. This is accompanied by biochemical experiments to probe the physiological implications of the observed association. The WLS membrane domain has close structural homology to G protein-coupled receptors (GPCRs). A Wnt hairpin inserts into a conserved hydrophobic cavity in the GPCR-like domain, and the palmitoleate protrudes between two helices into the bilayer. A conformational switch of highly conserved residues on a separate Wnt hairpin might contribute to its transfer to receiving cells. This work provides molecular-level insights into a central mechanism in animal body plan development and stem cell biology.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores Acoplados a Proteínas G / Péptidos y Proteínas de Señalización Intracelular / Proteínas Wnt Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Cell Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Receptores Acoplados a Proteínas G / Péptidos y Proteínas de Señalización Intracelular / Proteínas Wnt Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Cell Año: 2021 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos