| First Author | Takada R | Year | 2006 |
| Journal | Dev Cell | Volume | 11 |
| Issue | 6 | Pages | 791-801 |
| PubMed ID | 17141155 | Mgi Jnum | J:219624 |
| Mgi Id | MGI:5621264 | Doi | 10.1016/j.devcel.2006.10.003 |
| Citation | Takada R, et al. (2006) Monounsaturated fatty acid modification of Wnt protein: its role in Wnt secretion. Dev Cell 11(6):791-801 |
| abstractText | 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. |
