836-Genetic Architecture of an Allosteric Hormone Receptor

This article introduces GluePCA, a high-throughput method used to map how thousands of mutations affect the PYL1 hormone receptor, a molecular switch in plants. By analyzing over 40,000 measurements, the researchers discovered that nearly 90% of mutations alter the receptor’s response to chemicals, primarily through changes in protein stability. The study reveals a modular genetic architecture where different regions of the protein independently control sensitivity and activity levels. Notably, specific rare mutations were found to create innovative signaling behaviors, such as inverted or "band-stop" responses. Ultimately, the data illustrates the evolutionary flexibility of allosteric proteins and provides a scalable framework for engineering future biosensors.

References:

• Stammnitz M R, Lehner B. The genetic architecture of an allosteric hormone receptor[J]. bioRxiv, 2025: 2025.05. 30.656975.