Extracellular proximal interaction profiling by cell surface–targeted TurboID reveals LDLR as a partner of liganded EGFR

细胞外 仿形(计算机编程) 化学 细胞生物学 受体 癌症研究 生物 生物物理学 生物化学 计算机科学 操作系统
作者
Rasha Al Mismar,Payman Samavarchi‐Tehrani,Brendon Seale,Vesal Kasmaeifar,Claire E. Martin,Anne‐Claude Gingras
出处
期刊:Science Signaling [American Association for the Advancement of Science (AAAS)]
卷期号:17 (861)
标识
DOI:10.1126/scisignal.adl6164
摘要

Plasma membrane proteins play pivotal roles in receiving and transducing signals from other cells and from the environment and are vital for cellular functionality. Enzyme-based, proximity-dependent approaches, such as biotin identification (BioID), combined with mass spectrometry have begun to illuminate the landscape of proximal protein interactions within intracellular compartments. To extend the potential of these approaches to study the extracellular environment, we developed extracellular TurboID (ecTurboID), a method designed to profile the interactions between proteins on the surfaces of living cells over short timescales using the fast-acting biotin ligase TurboID. After optimizing our experimental and data analysis strategies to capture extracellular proximity interactions, we used ecTurboID to reveal the proximal interactomes of several plasma membrane proteins, including the epidermal growth factor receptor (EGFR). We found that EGF stimulation induced an association between EGFR and the low-density lipoprotein receptor (LDLR) and changed the interactome of LDLR by increasing its proximity with proteins that regulate EGFR signaling. The identification of this interaction between two well-studied and clinically relevant receptors illustrates the utility of our modified proximity labeling methodology for identifying dynamic extracellular associations between plasma membrane proteins.
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