A Lipid Linchpin for Wnt-Fz Docking

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Science  06 Jul 2012:
Vol. 337, Issue 6090, pp. 44-45
DOI: 10.1126/science.1224468

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This year marks the 30th anniversary of the discovery of Wnt1 (1), the founding member of a family of conserved secreted factors that define signaling pathways with pivotal roles in animal development, tissue homeostasis, and numerous diseases, including cancer (2, 3). Much later, the transmembrane proteins of the Frizzled (Fz) family were identified as the Wnt receptors (4). Wnt proteins proved extremely challenging to purify as active proteins; they require a lipid modification for activity (5), rendering them hydrophobic and insoluble in the absence of detergent. The resulting lack of structural data has hampered mechanistic progress. The structure of the Wnt-Fz complex reported by Janda et al. on page 59 of this issue (6) provides important insights into how Wnt ligands interact with their receptors.