The adaptor protein-1 μ1B subunit expands the repertoire of basolateral sorting signal recognition in epithelial cells.
The adaptor protein-1 μ1B subunit expands the repertoire of basolateral sorting signal recognition in epithelial cells.
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DOI：
10.1016/j.devcel.2013.10.006
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发表时间：
2013-11-11
影响因子：
11.8
通讯作者：
Bonifacino JS
中科院分区：
文献类型：
--
作者：
Guo X;Mattera R;Ren X;Chen Y;Retamal C;González A;Bonifacino JS
在蛋白质分选中，一个突出的问题是为什么极化上皮细胞表达AP-1网格蛋白接头复合体的μ1亚基的两种亚型：普遍存在的μ1A和上皮特异性的μ1B。先前的研究认为，μ1A和μ1B主要介导基侧分选，分别来自反式高尔基网络（TGN）和循环核内体。然而，利用改进的分析工具，我们发现μ1A和μ1B在很大程度上是共域的。它们也与TGN和再循环内小体标记物以及通过生物合成和内吞再循环路线的基侧货物有类似程度的共定位。相反，这两种异构体在信号识别特异性上有所不同。特别是，μ1B优先结合来自以μ1B依赖方式进行基底侧分类的货物的信号子集。我们得出结论，上皮细胞中不同μ1同种异构体的表达扩大了AP-1识别的信号库，用于将更大范围的货物分选到基底外侧表面。
An outstanding question in protein sorting is why polarized epithelial cells express two isoforms of the μ1 subunit of the AP-1 clathrin adaptor complex: the ubiquitous μ1A and the epithelial-specific μ1B. Previous studies led to the notion that μ1A and μ1B mediate basolateral sorting predominantly from the trans-Golgi network (TGN) and recycling endosomes, respectively. Using improved analytical tools, however, we find that μ1A and μ1B largely colocalize with each other. They also colocalize to similar extents with TGN and recycling endosome markers, as well as with basolateral cargoes transiting biosynthetic and endocytic-recycling routes. Instead, the two isoforms differ in their signal-recognition specificity. In particular, μ1B preferentially binds a subset of signals from cargoes that are sorted basolaterally in a μ1B-dependent manner. We conclude that expression of distinct μ1 isoforms in epithelial cells expands the repertoire of signals recognized by AP-1 for sorting of a broader range of cargoes to the basolateral surface.
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