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From trash collectors to guardians of cell signaling and immune homeostasis

Ubiquitination, the covalent attachment of ubiquitin molecules to target proteins, occurs rapidly and often reversibly, and regulates a vast array of protein-protein interactions that underlie cellular immune responses (1). Ubiquitination is best known for mediating protein interactions with degradative proteasomes, thereby dictating protein stability. This critical function was recognized by the Nobel Prize in Chemistry in 2004. Recent studies indicate that ubiquitination also mediates a broad array of non-proteolytic interactions between proteins that regulate protein trafficking, transcription factor complexes, and signal transduction (2). In this volume, the review articles utilize the lens of individual ubiquitin ligase enzymes that regulate ubiquitination of signaling proteins in immune cells.