The aryl hydrocarbon receptor as a model PAS sensor. (2022)

• Record Type: Journal Article
• Authors: Vazquez-Rivera, Emmanuel; Rojas, Brenda L.; Parrott, Jessica C.; Shen, Anna L.; Xing, Yongna; Carney, Patrick R.; Bradfield, Christopher A.
• Is Part Of: Toxicology reports. Volume 9(2022)
• Page Start: 1
• Page End: 11
• Publication Date: 2022
• Subjects: Aryl hydrocarbon receptor -- PAS proteins -- Environmental sensors; Toxicology -- Periodicals; Clinical toxicology -- Periodicals; Drug-Related Side Effects and Adverse Reactions; Hazardous Substances; Poisoning; Toxicology; Electronic journals; Periodicals; Periodicals; 571.9505
• DOI: 10.1016/j.toxrep.2021.11.017
• Languages: English
• ISSNs: 2214-7500

Abstract

Graphical abstract: Abstract: Proteins containing P ER-A RNT-S IM (PAS) domains are commonly associated with environmental adaptation in a variety of organisms. The PAS domain is found in proteins throughout Archaea, Bacteria, and Eukarya and often binds small-molecules, supports protein-protein interactions, and transduces input signals to mediate an adaptive physiological response. Signaling events mediated by PAS sensors can occur through induced phosphorelays or genomic events that are often dependent upon PAS domain interactions. In this perspective, we briefly discuss the diversity of PAS domain containing proteins, with particular emphasis on the prototype member, the aryl hydrocarbon receptor (AHR). This ligand-activated transcription factor acts as a sensor of the chemical environment in humans and many chordates. We conclude with the idea that since mammalian PAS proteins often act through PAS-PAS dimers, undocumented interactions of this type may link biological processes that we currently think of as independent. To support this idea, we present a framework to guide future experiments aimed at fully elucidating the spectrum of PAS-PAS interactions with an eye towards understanding how they might influence environmental sensing in human and wildlife populations.