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Abstract：
Protein-protein interactions are of paramount importance in regulating normal cardiac physiology. Methodologies to elucidate these interactions in vivo have been limited. Recently, proximity-dependent biotinylation, with the use of BioID, TurboID, and ascorbate peroxidase, has been developed to uncover cellular neighborhoods and novel protein-protein interactions. These cutting-edge techniques have enabled the identification of subcellular localizations of specific proteins and the neighbors or interacting proteins within these subcellular regions. In contrast to classic methods such as affinity purification and subcellular fractionation, these techniques add covalently bound tags in living cells, such that spatial relationships and interaction networks are not disrupted. Recently, these methodologies have been used to identify novel protein-protein interactions relevant to the cardiovascular system. In this review, we discuss the development and current use of proximity biotin-labeling for cardiovascular research.
摘要：
蛋白质-蛋白质相互作用在调节正常心脏生理学中至关重要。在体内阐明这些相互作用的方法是有限的。最近,接近依赖性生物素化，使用BioID，TurboID,和抗坏血酸过氧化物酶，已被开发用于揭示细胞邻域和新型蛋白质-蛋白质相互作用。这些尖端技术使得能够识别特定蛋白质和这些亚细胞区域内的邻居或相互作用蛋白质的亚细胞定位。与经典方法如亲和纯化和亚细胞分级分离相反，这些技术在活细胞中添加共价结合的标签，这样空间关系和交互网络就不会中断。最近,这些方法已被用于鉴定与心血管系统相关的新型蛋白质-蛋白质相互作用.在这次审查中,我们讨论了邻近生物素标记在心血管研究中的发展和当前应用。
