分拣连接蛋白 11（SNX11）的结构揭示了一个新颖的扩展 PHox 同源（PX）结构域，对于抑制 SNX10 诱导的空泡形成至关重要。
Structure of sorting nexin 11 (SNX11) reveals a novel extended phox homology (PX) domain critical for inhibition of SNX10-induced vacuolation.
机构信息
State Key Laboratory of Respiratory Disease, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530; School of Life Sciences, University of Science and Technology of China, Hefei 230026.
Key Laboratory of Regenerative Biology, South China Institute for Stem Cell Biology and Regenerative Medicine, Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China.
出版信息
J Biol Chem. 2013 Jun 7;288(23):16598-16605. doi: 10.1074/jbc.M112.449306. Epub 2013 Apr 24.
Sorting nexins are phox homology (PX) domain-containing proteins involved in diverse intracellular endosomal trafficking pathways. The PX domain binds to certain phosphatidylinositols and is recruited to vesicles rich in these lipids. The structure of the PX domain is highly conserved, containing a three-stranded β-sheet, followed by three α-helices. Here, we report the crystal structures of truncated human SNX11 (sorting nexin 11). The structures reveal that SNX11 contains a novel PX domain, hereby named the extended PX (PXe) domain, with two additional α-helices at the C terminus. We demonstrate that these α-helices are indispensible for the in vitro functions of SNX11. We propose that this PXe domain is present in SNX10 and is responsible for the vacuolation activity of SNX10. Thus, this novel PXe domain constitutes a structurally and functionally important PX domain subfamily.
分选连接蛋白是含有 PH 结构域的蛋白，参与多种细胞内的内体运输途径。PX 结构域可以结合特定的磷脂酰肌醇，并募集到富含这些脂质的小泡。PX 结构域的结构高度保守，包含一个三股β-折叠，后面跟着三个α-螺旋。在这里，我们报告了截断的人类 SNX11（分选连接蛋白 11）的晶体结构。这些结构表明，SNX11 包含一个新的 PX 结构域，命名为扩展 PX（PXe）结构域，在 C 端有另外两个α-螺旋。我们证明这些α-螺旋对于 SNX11 的体外功能是必不可少的。我们提出，这个 PXe 结构域存在于 SNX10 中，负责 SNX10 的空泡化活性。因此，这个新的 PXe 结构域构成了一个结构和功能上重要的 PX 结构域亚家族。
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