Specialized biological processes occur in different regions and organelles of the cell. Additionally, the function of proteins correlate greatly with their interactions and subcellular localization. Understanding the mechanism underlying the specialized functions of cellular structures therefore requires a detailed identification of proteins within spatially defined domains of the cell. Furthermore, the identification of interacting proteins is also crucial for the elucidation of the underlying mechanism of complex cellular processes. Mass spectrometry methods have been utilized systematically for the characterization of the proteome of isolated organelles and protein interactors purified through affinity pull-down or following crosslinking. However, the available methods of purification have limited these approaches, as it is difficult to derive intact organelles of high purity in many circumstances. Furthermore, contamination that leads to the identification of false positive is widespread even when purification is possible. Here, we present a highlight of the BioID proximity labeling approach which has been used to effectively characterize the proteomic composition of several cellular compartments. In addition, an observed limitation of this method based on proteomic spatiotemporal dynamics, was also discussed.

中文翻译：

---

细胞内蛋白质组划分：一种基于生物素连接酶的邻近标记方法

特殊的生物过程发生在细胞的不同区域和细胞器中。此外，蛋白质的功能与它们的相互作用和亚细胞定位密切相关。因此，了解细胞结构特殊功能的潜在机制需要详细鉴定细胞空间定义域内的蛋白质。此外，相互作用蛋白的鉴定对于阐明复杂细胞过程的潜在机制也至关重要。质谱法已被系统地用于表征分离的细胞器和通过亲和下拉或交联后纯化的蛋白质相互作用物的蛋白质组。然而，可用的纯化方法限制了这些方法，因为在许多情况下很难获得高纯度的完整细胞器。此外，即使可以进行纯化，导致识别假阳性的污染也很普遍。在这里，我们展示了 BioID 邻近标记方法的一个亮点，该方法已被用于有效表征几个细胞隔室的蛋白质组学组成。此外，还讨论了基于蛋白质组学时空动力学的这种方法的观察局限性。我们展示了 BioID 邻近标记方法的一个亮点，该方法已用于有效表征几个细胞区室的蛋白质组学组成。此外，还讨论了基于蛋白质组学时空动力学的这种方法的观察局限性。我们展示了 BioID 邻近标记方法的一个亮点，该方法已用于有效表征几个细胞区室的蛋白质组学组成。此外，还讨论了基于蛋白质组学时空动力学的这种方法的观察局限性。