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Abstract：
Photoreceptor disc component (PRCD) is a small protein which is exclusively localized to photoreceptor outer segments, and is involved in the formation of photoreceptor outer segment discs. Mutations in PRCD are associated with retinal degeneration in humans, mice, and dogs. The purpose of this work was to identify PRCD-binding proteins in the retina. PRCD protein-protein interactions were identified when implementing the Ras recruitment system (RRS), a cytoplasmic-based yeast two-hybrid system, on a bovine retina cDNA library. An interaction between PRCD and tubby-like protein 1 (TULP1) was identified. Co-immunoprecipitation in transfected mammalian cells confirmed that PRCD interacts with TULP1, as well as with its homolog, TUB. These interactions were mediated by TULP1 and TUB highly conserved C-terminal tubby domain. PRCD localization was altered in the retinas of TULP1- and TUB-deficient mice. These results show that TULP1 and TUB, which are involved in the vesicular trafficking of several photoreceptor proteins from the inner segment to the outer segment, are also required for PRCD exclusive localization to photoreceptor outer segment discs.
摘要：
光感受器盘成分（PRCD）是一种小的蛋白质，专门位于光感受器外节，并参与感光体外段圆盘的形成。PRCD的突变与人类的视网膜变性有关，老鼠,还有狗.这项工作的目的是鉴定视网膜中的PRCD结合蛋白。在实施Ras募集系统(RRS)时，确定了PRCD蛋白质-蛋白质相互作用，基于细胞质的酵母双杂交系统，在牛视网膜cDNA文库上。鉴定了PRCD与管状样蛋白1（TULP1）之间的相互作用。转染的哺乳动物细胞中的免疫共沉淀证实PRCD与TULP1及其同源物相互作用，浴缸.这些相互作用由TULP1和TUB高度保守的C末端tubby结构域介导。PRCD定位在TULP1-和TUB缺陷小鼠的视网膜中改变。这些结果表明，TULP1和TUB，它们参与了几种感光蛋白从内段到外段的囊泡运输，还需要PRCD独家定位到感光器外段光盘。
