Synergistic interaction of tubby and tubby-like protein 1 (Tulp1).
Synergistic interaction of tubby and tubby-like protein 1 (Tulp1).
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DOI：
10.1007/978-1-4614-3209-8_64
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发表时间：
2014
影响因子：
--
通讯作者：
Caberoy, Nora Blanca
中科院分区：
文献类型：
--
作者：
Caberoy, Nora Blanca
关键词：
tubby或tubby样蛋白1（Tulp1）的突变导致视网膜变性，机制不明。我们最近确定了这两种蛋白质与非常规分泌作为新的MerTK特异性的吞噬配体视网膜色素上皮细胞（RPE）。利用我们新开发的开放阅读框（ORF）噬菌体展示技术，我们鉴定了Tulp 1为Tubby结合蛋白。通过酵母双杂交和蛋白质下拉实验验证了tubby和Tulp1的相互作用。Tubby和Tulp1形成异源二聚体或异源寡聚体，它们的相互作用在功能上通过它们对RPE吞噬作用的协同刺激来揭示。Tubby和Tulp1通过MerTK依赖性信号传导介导吞噬作用，非肌肉肌球蛋白II再分布导致吞噬囊泡与重排的NMMIIA共定位。
Mutations in either tubby or tubby-like protein 1 (Tulp1) cause retinal degeneration with undefined mechanisms. We recently identified both proteins with unconventional secretion as novel MerTK-specific phagocytosis ligands for retinal pigment epithelium (RPE) cells. Using our newly-developed open reading frame (ORF) phage display as a technology for protein-protein interactions, we identified Tulp1 as a Tubby-binding protein. The interaction of tubby and Tulp1 was verified by yeast two-hybrid and protein pull-down assays. Tubby and Tulp1 form heterodimer or heterooligomer and their interaction was functionally revealed by their synergistic stimulation of RPE phagocytosis. Tubby and Tulp1 mediated phagocytosis through MerTK-dependent signaling with non-muscle myosin II redistribution leading to colocalization of phagocytosed vesicles with rearranged NMMIIA.
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