The Subcellular Localization of Tubby-Like Proteins and Participation in Stress Signaling and Root Colonization by the Mutualist Piriformospora indica1[W]
The Subcellular Localization of Tubby-Like Proteins and Participation in Stress Signaling and Root Colonization by the Mutualist Piriformospora indica1[W]
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DOI：
10.1104/pp.112.201319
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发表时间：
2012-06
期刊：
影响因子：
7.4
通讯作者：
Marco U. Reitz;Jeff Kweku Bissue;K. Zocher;A. Attard;R. Hückelhoven;K. Becker;J. Imani;R. Eichmann-R.-Eichma
中科院分区：
文献类型：
--
作者：
Marco U. Reitz;Jeff Kweku Bissue;K. Zocher;A. Attard;R. Hückelhoven;K. Becker;J. Imani;R. Eichmann-R.-Eichma
Tubby和Tubby样蛋白（TLPs）首先在哺乳动物中发现，它们参与神经细胞的发育和功能。由于它们作为质膜（PM）束缚的转录因子或囊泡运输的介质的重要性，它们的缺乏导致肥胖和其他疾病综合征。羧基末端Tubby结构域的磷脂酰肌醇4，5-二磷酸结合将这些蛋白质附着于PM和囊泡，并且对于功能是必需的。TLPs在包括植物在内的真核生物界中是保守的，这表明TLPs具有基本的生物学功能。植物类TLPs具有一个氨基末端的F盒结构域，这使它们与其他真核类TLPs区别开来。拟南芥（Arabidopsis thaliana）编码11个AtTLPs，分为6个进化分支。我们确定了AtTLPs的互惠真菌梨形孢印度拟南芥根定殖的意义。我们的研究结果进一步表明保守的磷脂酰肌醇4，5-二磷酸结合位点的Tubby域所需的PM锚定AtTLPs。更详细的研究揭示了磷脂酶C触发的AtTLP 3从PM释放，表明哺乳动物Tubby和TLP 3的保守机制。我们进一步表明，过氧化氢刺激AtTLP 3从PM释放，大概是为了激活下游事件。与哺乳动物同源物不同，几乎所有AtTLPs的氨基末端部分具有核质和质体定位模式。因此，很容易假设TLPs将活性氧电流转化为信号传导，不仅用于核中的转录调控，而且在从PM释放后影响质体相关功能。
Tubby and Tubby-like proteins (TLPs) were first discovered in mammals, where they are involved in the development and function of neuronal cells. Due to their importance as plasma membrane (PM)-tethered transcription factors or mediators of vesicle trafficking, their lack causes obesity and other disease syndromes. Phosphatidylinositol 4,5-bisphosphate binding of the carboxyl-terminal Tubby domain attaches these proteins to the PM and vesicles and is essential for function. TLPs are conserved across eukaryotic kingdoms including plants, suggesting fundamental biological functions of TLPs. Plant TLPs possess an amino-terminal F-box domain that distinguishes them from other eukaryotic TLPs. Arabidopsis (Arabidopsis thaliana) encodes 11 AtTLPs that fall into six phylogenetic clades. We identified the significance of AtTLPs for root colonization of Arabidopsis by the mutualistic fungus Piriformospora indica. Our results further indicate conserved phosphatidylinositol 4,5-bisphosphate-binding sites in the Tubby domains that are required for PM anchoring of AtTLPs. More detailed studies revealed phospholipase C-triggered release of AtTLP3 from the PM, indicating a conserved mechanism as reported for mammalian Tubby and TLP3. We further show that hydrogen peroxide stimulates the release of AtTLP3 from the PM, presumably for activating downstream events. Different from mammalian homologs, the amino-terminal part of almost all AtTLPs has nucleocytosolic and plastidial localization patterns. Thus, it is tempting to assume that TLPs translate reactive oxygen species currents into signaling not only for transcriptional regulation in the nucleus but also affect plastid-associated functions after release from the PM.