Differential use of p24 family members as cargo receptors for the transport of glycosylphosphatidylinositol-anchored proteins and Wnt1
Differential use of p24 family members as cargo receptors for the transport of glycosylphosphatidylinositol-anchored proteins and Wnt1
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p24家族成员作为转运糖基磷脂酰肌醇锚定蛋白和Wnt1的货物受体的不同用途
DOI：
10.1093/jb/mvab108
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发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Kinoshita Taroh
中科院分区：
文献类型：
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作者：
Tashima Yuko;Hirata Tetsuya;Maeda Yusuke;Murakami Yoshiko;Kinoshita Taroh
p24蛋白的复合物作为转运COPII囊泡从内质网（ER）的货物受体。p24复合物的主要货物是通过共价连接的糖基磷脂酰肌醇（GPI）或脂肪酸与ER膜相连的亲水性蛋白质。已知每个p24复合物包含来自所有四个p24亚家族（p24α、p24β、p24γ和p24δ）的成员。然而，目前还不清楚如何货物的特异性p24复合物的成员化学计量的影响。在这里，我们报告的亚基组成的哺乳动物p24复合物参与运输GPI锚定蛋白和Wnt 1。我们发现，至少需要一个p24α形成p24复合物，并由p24α2，p24β1，p24γ2和p24δ1组成的p24复合物是必需的GPI锚定蛋白的有效运输。另一方面，包含p24α2、p24α3、p24β1、p24γ和p24δ1的p24复合物参与Wnt 1的转运。此外，p24α2和p24α3之间的相互作用对Wnt 1转运至关重要。因此，p24α和p24γ亚家族成员对于货物选择性是重要的。最后，我们的数据符合p24复合物的八聚体模型，而不是四聚体模型，其中每个复合物由来自每个p24亚家族的两种蛋白质组成。
Complexes of p24 proteins act as cargo receptors for the transport of COPII vesicles from the endoplasmic reticulum (ER). The major cargos of p24 complexes are hydrophilic proteins tethered to the ER membrane via a covalently attached glycosylphosphatidylinositol (GPI) or fatty acid. Each p24 complex is known to contain members from all four p24 subfamilies (p24α, p24β, p24γ and p24δ). However, it remains unclear how the cargo specificities of p24 complexes are influenced by member stoichiometry. Here, we report the subunit compositions of mammalian p24 complexes involved in the transport of GPI-anchored proteins and Wnt1. We show that at least one p24α is required for the formation of p24 complexes and that a p24 complex consisting of p24α2, p24β1, p24γ2 and p24δ1 is required for the efficient transport of GPI-anchored proteins. On the other hand, a p24 complex containing p24α2, p24α3, p24β1, p24γ and p24δ1 is involved in the transport of Wnt1. Further, interactions between p24α2 and p24α3 are critical for Wnt1 transport. Thus, p24α and p24γ subfamily members are important for cargo selectivity. Lastly, our data fit with an octamer, rather than a tetramer, model of p24 complexes, where each complex consists of two proteins from each p24 subfamily.