Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 2, Pages 370-377Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1119197109
Keywords
development; morphogenesis; pattern; palmitoylation; lipid modification
Categories
Funding
- Howard Hughes Medical Institute
- National Institutes of Health
- Swiss National Science Foundation
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Lipid-modified Wnt/Wingless (Wg) proteins can signal to their target cells in a short-or long-range manner. How these hydrophobic proteins travel through the extracellular environment remains an outstanding question. Here, we report on a Wg binding protein, Secreted Wg-interacting molecule (Swim), that facilitates Wg diffusion through the extracellular matrix. Swim, a putative member of the Lipocalin family of extracellular transport proteins, binds to Wg with nanomolar affinity in a lipid-dependent manner. In quantitative signaling assays, Swim is sufficient to maintain the solubility and activity of purified Wg. In Drosophila, swim RNAi phenotypes resemble wg loss-of-function phenotypes in long-range signaling. We propose that Swim is a cofactor that promotes long-range Wg signaling in vivo by maintaining the solubility of Wg.
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