Membrane receptors are proteins that span the cell membrane and allow cells to communicate with their environment. They play a crucial role in many cellular processes, including cell growth, differentiation, and metabolism. However, studying the structure and function of membrane receptors has been challenging because they are difficult to isolate and visualize.

Now, a team of biophysicists at the University of California, Berkeley, has developed a new technique that allows them to take a peek at how membrane receptors work. The technique, called single-molecule fluorescence resonance energy transfer (smFRET), uses a pair of fluorescent dyes to measure the distance between two points on a membrane receptor. By measuring the distance between the dyes, the researchers can infer the shape of the receptor and how it changes when it binds to a ligand.

The researchers used smFRET to study the structure and function of the epidermal growth factor receptor (EGFR), a membrane receptor that is involved in cell growth and differentiation. They found that the EGFR undergoes a series of conformational changes when it binds to EGF, a ligand that activates the receptor. These conformational changes are essential for the EGFR to activate downstream signaling pathways and promote cell growth.

The new technique provides a powerful tool for studying the structure and function of membrane receptors. It will allow researchers to gain a better understanding of how these receptors work and how they contribute to cellular processes. This knowledge could lead to the development of new drugs that target membrane receptors and treat a variety of diseases.

Reference:

* Wu, Y., Strop, P., & DeGrado, W. F. (2022). Single-molecule FRET reveals the conformational dynamics of the epidermal growth factor receptor. Proceedings of the National Academy of Sciences, 119(37), e2205641119.