Monounsaturated fatty acid modification of Wnt protein: its role in Wnt secretion
- PMID: 17141155
- DOI: 10.1016/j.devcel.2006.10.003
Monounsaturated fatty acid modification of Wnt protein: its role in Wnt secretion
Abstract
The secretion and extracellular transport of Wnt protein are thought to be well-regulated processes. Wnt is known to be acylated with palmitic acid at a conserved cysteine residue (Cys77 in murine Wnt-3a), and this residue appears to be required for the control of extracellular transport. Here, we show that murine Wnt-3a is also acylated at a conserved serine residue (Ser209). Of note, we demonstrated that this residue is modified with a monounsaturated fatty acid, palmitoleic acid. Wnt-3a defective in acylation at Ser209 is not secreted from cells in culture or in Xenopus embryos, but it is retained in the endoplasmic reticulum (ER). Furthermore, Porcupine, a protein with structural similarities to membrane-bound O-acyltransferases, is required for Ser209-dependent acylation, as well as for Wnt-3a transport from the ER for secretion. These results strongly suggest that Wnt protein requires a particular lipid modification for proper intracellular transport during the secretory process.
Comment in
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Wnt lipid modifications: not as saturated as we thought.Dev Cell. 2006 Dec;11(6):751-2. doi: 10.1016/j.devcel.2006.11.007. Dev Cell. 2006. PMID: 17141148
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