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首页> 外文期刊>Developmental cell >Monounsaturated fatty acid modification of Wnt protein: Its role in Wnt secretion
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Monounsaturated fatty acid modification of Wnt protein: Its role in Wnt secretion

机译：Wnt蛋白的单不饱和脂肪酸修饰：在Wnt分泌中的作用

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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.
机译：Wnt蛋白的分泌和细胞外运输被认为是调控良好的过程。已知Wnt在保守的半胱氨酸残基（鼠Wnt-3a中的Cys77）上被棕榈酸酰化，并且该残基似乎是控制细胞外转运所必需的。在这里，我们表明，鼠Wnt-3a也被保守的丝氨酸残基（Ser209）酰化。值得注意的是，我们证明了该残基已被单不饱和脂肪酸棕榈油酸改性。在Ser209上酰化缺陷的Wnt-3a不会从培养细胞或非洲爪蟾胚胎中分泌，但会保留在内质网（ER）中。此外，Ser209依赖的酰化以及从ER转运Wnt-3a分泌都需要豪猪蛋白（一种与膜结合的O-酰基转移酶具有结构相似性的蛋白质）。这些结果强烈表明，Wnt蛋白需要特殊的脂质修饰，以在分泌过程中正确地进行细胞内运输。

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