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首页> 美国卫生研究院文献>other >Progressive Rod-Cone Degeneration (PRCD) Protein Requires N-Terminal S-Acylation and Rhodopsin Binding for Photoreceptor Outer Segment Localization and Maintaining Intracellular Stability
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Progressive Rod-Cone Degeneration (PRCD) Protein Requires N-Terminal S-Acylation and Rhodopsin Binding for Photoreceptor Outer Segment Localization and Maintaining Intracellular Stability

机译：渐进式杆状锥变性（PRCD）蛋白需要N末端S-酰化和视紫红质结合才能使感光器外段定位并保持细胞内稳定性

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摘要

The light-sensing outer segments of photoreceptor cells harbor hundreds of flattened membranous discs containing the visual pigment, rhodopsin, and all the proteins necessary for visual signal transduction. PRCD (Progressive Rod-Cone Degeneration) is one of a few proteins residing specifically in photoreceptor discs, and the only one with completely unknown function. The importance of PRCD is highlighted by its mutations causing photoreceptor degeneration and blindness in canine and human patients. Here we report that PRCD is S-acylated at its N-terminal cysteine and anchored to the cytosolic surface of disc membranes. We also showed that mutating the S-acylated cysteine to tyrosine, a common cause of blindness in dogs and found in affected human families, causes PRCD to be completely mislocalized from the photoreceptor outer segment. We next undertook a proteomic search for PRCD interacting partners in disc membranes and found that it binds rhodopsin. This interaction was confirmed by reciprocal precipitation and co-chromatography experiments. We further demonstrated this interaction to be critically important for supporting the intracellular stability of PRCD, as the knockout of rhodopsin caused a drastic reduction in the photoreceptor content of PRCD. These data reveal the cause of photoreceptor disease in PRCD mutant dogs, and implicate rhodopsin to be involved in PRCD’s unknown, yet essential function in photoreceptors.
机译：感光细胞的感光外部部分带有数百个扁平的膜状盘，其中包含视觉色素，视紫红质和视觉信号转导所需的所有蛋白质。 PRCD（渐进杆状锥变性）是专门存在于感光盘中的几种蛋白质之一，也是唯一功能完全未知的蛋白质。 PRCD的重要性通过其突变导致犬类和人类患者的感光细胞变性和失明而突出。在这里我们报告说PRCD在其N端半胱氨酸被S酰化，并锚定到椎间盘膜的胞质表面。我们还表明，将S-酰化的半胱氨酸突变为酪氨酸（酪氨酸是犬失明的常见原因，并在受影响的人类家庭中发现）会导致PRCD从感光器外部部分完全错位。接下来，我们对在圆盘膜上的PRCD相互作用伙伴进行了蛋白质组学搜索，发现它与视紫红质结合。相互沉淀和共色谱实验证实了这种相互作用。我们进一步证明了这种相互作用对于支持PRCD的细胞内稳定性至关重要，因为视紫红质的敲除会导致PRCD感光受体含量的急剧减少。这些数据揭示了PRCD突变犬中感光细胞疾病的病因，并暗示视紫红质参与了PRCD在感光细胞中未知但必不可少的功能。

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