Neddylation steers the fate of cellular receptors

Abstract

Cellular receptors regulate physiological responses by interacting with ligands, thus playing a crucial role in intercellular communication. Receptors are categorized on the basis of their location and engage in diverse biochemical mechanisms, which include posttranslational modifications (PTMs). Considering the broad impact and diversity of PTMs on cellular functions, we focus narrowly on neddylation, a modification closely resembling ubiquitination. We systematically organize its canonical and noncanonical roles in modulating proteins associated with cellular receptors with the goal of providing a more detailed perspective on the intricacies of both intracellular and cell-surface receptors. Proteins undergo posttranslational modifications (PTMs) to maintain physiological balance. Neddylation, a type of PTM, involves attaching a small ubiquitin-like molecule, NEDD8, to target proteins. In this study, J.B.P. and colleagues explore the role of neddylation role in cellular receptors. The researchers conducted a review to understand how neddylation affects different types of receptors, including membrane and intracellular receptors. They examined both canonical (cullin-dependent) and noncanonical pathways regulated by neddylation. The study systematically analyzes the impact of neddylation on receptor stability, signaling, and function. This summary was initially drafted using artificial intelligence, then revised and fact-checked by the author.