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首页> 外文期刊>Cellular Signalling >Phosphorylation at Ser729 specifies a Golgi localisation for protein kinase C epsilon (PKC epsilon,) in 3T3 fibroblasts
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Phosphorylation at Ser729 specifies a Golgi localisation for protein kinase C epsilon (PKC epsilon,) in 3T3 fibroblasts

机译：Ser729处的磷酸化为3T3成纤维细胞中的蛋白激酶Cε（PKCε）指定了高尔基体定位

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We demonstrate that GFP-PKC epsilon concentrates at a perinuclear site in living fibroblasts and that cell passage induces rapid translocation of PKC epsilon to the periphery where it appears to colocalise with F-actin. When newly passaged cells have adhered and are proliferating again, GFP-PKC epsilon returns to its perinuclear site. GFP-PKC epsilon co-localises with wheat germ agglutinin suggesting that it is associated with the Golgi at the perinuclear site. In support, PKC epsilon is detected in a Golgi-enriched fraction in pre-passage cells but is lost from the fraction after passage. PKC epsilon at the perinuclear Golgi site is phosphorylated at Ser729 but cell passage induces the loss of the phosphate at this site as reported previously [England et al. (2001) J. Biol. Chem. 276, 10437-10442]. PKC epsilon S729A, S729E and S729T mutants, which are not recognised by a specific antiphosphoPKC epsilon (Ser729) antibody, do not concentrate at a perinuclear/Golgi site in proliferating fibroblasts. This suggests that both phosphorylation and serine rather than threonine are needed at position 729 to locate PKC epsilon at its perinuclear/Golgi site. Phorbol ester induced translocation of PKC epsilon to the nucleus also requires dephosphorylation at Ser729; after translocation nuclear PKC epsilon lacks a phosphate at Ser729. Sulphation and secretion of glycosaminoglycan (GAG) chains from fibroblasts increases on passage and returns to basal as cells proliferate showing that cell passage influences secretory events at the Golgi. The results indicate that Ser729 phosphorylation plays a role in determining PKC epsilon localisation in fibroblasts. (c) 2007 Elsevier Inc. All rights reserved.
机译：我们证明GFP-PKC epsilon集中在活的成纤维细胞的核周部位，并且该细胞传代诱导PKC epsilon向其似乎与F-肌动蛋白共定位的外围快速移位。当新传代的细胞粘附并再次增殖时，GFP-PKCε返回其核周位点。 GFP-PKCε与小麦胚芽凝集素共定位，表明它与核周部位的高尔基体有关。在支持下，在传代前细胞的高尔基体富集级分中检测到PKCε，但在传代后从级分中丢失。如先前报道，核高尔基周缘的PKCε在Ser729处被磷酸化，但细胞传代会导致该位点的磷酸损失。 （2001）J.Biol。化学276，10437-10442]。 PKC epsilon S729A，S729E和S729T突变体没有被特定的抗磷酸PKC epsilon（Ser729）抗体识别，它们不会在增殖的成纤维细胞中集中在核周/高尔基体位点。这表明在位置729处既需要磷酸化又需要丝氨酸而不是苏氨酸，才能将PKCε定位在其核周/高尔基体位点。由佛波酯诱导的PKCε易位至细胞核也需要在Ser729处进行去磷酸化。易位后核PKC epsilon在Ser729缺少磷酸。成纤维细胞中糖胺聚糖（GAG）链的硫酸化和分泌在传代时增加，并随着细胞增殖而恢复为基础，表明细胞传代会影响高尔基体的分泌事件。结果表明，Ser729磷酸化在确定成纤维细胞中PKCε定位中起作用。 （c）2007 Elsevier Inc.保留所有权利。

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