Intrinsically disordered regions are poised to act as sensors of cellular chemistry

Trends Biochem Sci. 2023 Aug 30:S0968-0004(23)00204-9. doi: 10.1016/j.tibs.2023.08.001. Online ahead of print.ABSTRACTIntrinsically disordered proteins and protein regions (IDRs) are abundant in eukaryotic proteomes and play a wide variety of essential roles. Instead of folding into a stable structure, IDRs exist in an ensemble of interconverting conformations whose structure is biased by sequence-dependent interactions. The absence of a stable 3D structure, combined with high solvent accessibility, means that IDR conformational biases are inherently sensitive to changes in their environment. Here, we argue that IDRs are ideally poised to act as sensors and actuators of cellular physicochemistry. We review the physical principles that underlie IDR sensitivity, the molecular mechanisms that translate this sensitivity to function, and recent studies where environmental sensing by IDRs may play a key role in their downstream function.PMID:37657994 | DOI:10.1016/j.tibs.2023.08.001
Source: Trends in Biochemical Sciences - Category: Biochemistry Authors: Source Type: research