A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-α to the cell surface
A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-α to the cell surface
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DOI：
10.1016/s1097-2765(00)80470-0
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发表时间：
1999-04-01
期刊：
影响因子：
16
通讯作者：
Arribas, J
中科院分区：
文献类型：
--
作者：
Fernández-Larrea, J;Merlos-Suárez, A;Arribas, J
一般来说，质膜整体蛋白，如膜锚定生长因子protgf - α，被认为是通过不受调节的组成途径运输到细胞表面的。protgf - α c端突变体保留在早期分泌室中。在这里，使用双杂交筛选，我们鉴定了两个tacip (pro (T)在条形GF下-(a)在条形α α下(c)在条形细胞质域下-(i)在条形蛋白下相互作用(p))，它们含有PDZ结构域，不与protgf - α相互作用。c端突变体。其中之一TACIP18（先前鉴定并命名为Syntenin或mda-g）的结合特异性与可能介导protgf - α正常转运的成分的结合特异性一致。TACIP18与未成熟的细胞内形式的protgf - α共定位并特异性相互作用。因此，TACIP18在早期分泌途径中与protgf - α的相互作用似乎是后者靶向细胞表面的必要条件。
In general, plasma membrane integral proteins, such as the membrane-anchored growth factor proTGF-alpha, are assumed to be transported to the cell surface via a nonregulated, constitutive pathway. proTGF-alpha C-terminal mutants are retained in an early secretory compartment. Here, using a two-hybrid screen, we identify two TACIPs (pro (T) under bar GF-(a) under bar lpha (c) under bar ytoplasmic domain-(i) under bar nteracting (p) under bar roteins) that contain PDZ domains and do not interact with proTGF-alpha. C-terminal mutants. The binding specificity of one of them, TACIP18 (previously identified and named Syntenin or mda-g), coincides with that of the component that possibly mediates the normal trafficking of proTGF-alpha. TACIP18 colocalizes and interacts specifically with immature, intracellular forms of proTGF-alpha. Therefore, it appears that the interaction of TACIP18 with proTGF-alpha in the early secretory pathway is necessary for the targeting of the latter to the cell surface.