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首页> 外文期刊>Molecular and Cellular Biology >YPXL/I Is a Protein Interaction Motif Recognized by Aspergillus PalA and Its Human Homologue, AIP1/Alix
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YPXL/I Is a Protein Interaction Motif Recognized by Aspergillus PalA and Its Human Homologue, AIP1/Alix

机译：YPXL / I是曲霉PalA及其人类同源物AIP1 / Alix公认的蛋白质相互作用母题。

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摘要

The zinc finger transcription factor PacC undergoes two-step proteolytic activation in response to alkaline ambient pH. PalA is a component of the fungal ambient pH signal transduction pathway. Its mammalian homologue AIP1/Alix interacts with the apoptosis-linked protein ALG-2. We show that both PalA and AIP1/Alix recognize a protein-protein binding motif that we denote YPXL/I, where Tyr, Pro, and Leu/Ile are crucial for its interactive properties. Two such motifs flanking the signaling protease cleavage site mediate direct binding of PalA to PacC, required for the first and only pH-regulated cleavage of this transcription factor. PalA can bind the “closed” (i.e., wild-type full-length) conformer of PacC, suggesting that PalA binding constitutes the first stage in the two-step proteolytic cascade, recruiting or facilitating access of the signaling protease, presumably PalB. In addition to recognizing YPXL/I motifs, both PalA and AIP1/Alix interact with the Aspergillus class E Vps protein Vps32 homologue, a member of a protein complex involved in the early steps of the multivesicular body pathway, suggesting that this interaction is an additional feature of proteins of the PalA/AIP1/Alix family.
机译：锌指转录因子PacC响应碱性环境pH值经历两步蛋白水解激活。 PalA是真菌环境pH信号转导途径的组成部分。它的哺乳动物同系物AIP1 / Alix与凋亡相关蛋白ALG-2相互作用。我们显示，PalA和AIP1 / Alix都识别我们表示YPXL / I的蛋白质-蛋白质结合基序，其中Tyr，Pro和Leu / Ile对于其相互作用特性至关重要。信号蛋白酶切割位点两侧的两个这样的基序介导PalA与PacC的直接结合，这是该转录因子的第一次也是唯一的pH调节切割所需要的。 PalA可以结合PacC的“封闭”（即野生型全长）构象异构体，表明PalA结合构成了两步蛋白水解级联反应的第一阶段，募集或促进了信号转导蛋白酶（大概是PalB）的进入。除了识别YPXL / I基元之外，PalA和AIP1 / Alix都与曲霉 E类Vps蛋白Vps32同源物相互作用，后者是参与多囊体途径早期阶段的蛋白复合物的成员，提示这种相互作用是PalA / AIP1 / Alix家族蛋白的另一个特征。

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