Monounsaturated fatty acid modification of Wnt protein: its role in Wnt secretion.
Dev Cell
; 11(6): 791-801, 2006 Dec.
Article
en En
| MEDLINE
| ID: mdl-17141155
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.
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Banco de datos:
MEDLINE
Asunto principal:
Xenopus laevis
/
Ácidos Grasos Monoinsaturados
/
Transporte de Proteínas
/
Proteínas Wnt
Límite:
Animals
Idioma:
En
Revista:
Dev Cell
Asunto de la revista:
EMBRIOLOGIA
Año:
2006
Tipo del documento:
Article
País de afiliación:
Japón