Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI.
Sorting of GPI-anchored proteins into ER exit sites by p24 proteins is dependent on remodeled GPI.
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DOI：
10.1083/jcb.201012074
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发表时间：
2011-07-11
期刊：
影响因子：
--
通讯作者：
Kinoshita T
中科院分区：
文献类型：
--
作者：
Fujita M;Watanabe R;Jaensch N;Romanova-Michaelides M;Satoh T;Kato M;Riezman H;Yamaguchi Y;Maeda Y;Kinoshita T
p24 复合物充当货物受体，将 GPI 锚定蛋白分类到 COPII 囊泡中。蛋白质的糖基磷脂酰肌醇 (GPI) 锚定是发生在内质网 (ER) 中的翻译后修饰。 GPI 附着后，蛋白质通过外壳蛋白复合物 II (COPII) 包被的囊泡从 ER 转运。由于 GPI 锚定蛋白 (GPI-AP) 位于管腔中，因此它们不能直接与胞质 COPII 成分相互作用。将 GPI-AP 与 COPII 连接的受体被认为参与将 GPI-AP 有效包装到囊泡中；然而，GPI-AP 排序的机制尚不清楚。在这里，我们描述了由 PGAP1 和 PGAP5 介导的 GPI 锚的两种重塑反应，这是将 GPI-AP 分选到 ER 出口位点所必需的。 p24 蛋白家族识别重构的 GPI-AP 并将其分类到 COPII 囊泡中。 p24 蛋白与 GPI-AP 的结合具有 pH 依赖性，这表明它们在 ER 中结合并在 ER 后酸性区室中解离。我们的结果表明，p24 复合物充当正确重塑的 GPI-AP 的货物受体，将其分类到 COPII 囊泡中。
p24 complexes act as cargo receptors for sorting GPI-anchored proteins into COPII vesicles. Glycosylphosphatidylinositol (GPI) anchoring of proteins is a posttranslational modification occurring in the endoplasmic reticulum (ER). After GPI attachment, proteins are transported by coat protein complex II (COPII)-coated vesicles from the ER. Because GPI-anchored proteins (GPI-APs) are localized in the lumen, they cannot interact with cytosolic COPII components directly. Receptors that link GPI-APs to COPII are thought to be involved in efficient packaging of GPI-APs into vesicles; however, mechanisms of GPI-AP sorting are not well understood. Here we describe two remodeling reactions for GPI anchors, mediated by PGAP1 and PGAP5, which were required for sorting of GPI-APs to ER exit sites. The p24 family of proteins recognized the remodeled GPI-APs and sorted them into COPII vesicles. Association of p24 proteins with GPI-APs was pH dependent, which suggests that they bind in the ER and dissociate in post-ER acidic compartments. Our results indicate that p24 complexes act as cargo receptors for correctly remodeled GPI-APs to be sorted into COPII vesicles.
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