Pellino E3 ubiquitin protein ligase family member 2 (PELI2)

Pellino E3 ubiquitin protein ligase family member 2 (PELI2) is an enzyme in the RING-type E3 ubiquitin ligase family, characterized by its role in catalyzing the covalent attachment of ubiquitin to substrate proteins in innate immune pathways[1][4][6]. PELI2 is a central regulator of signaling downstream of the Toll-like and IL-1 receptors, especially through the ubiquitination of IRAK1 and the modulation of MAPK and NF-κB cascades[1][2][6]. Uniquely, PELI2 is essential for the priming and activation of the NLRP3 inflammasome, which mediates maturation of pro-inflammatory cytokines such as IL-1β and IL-18, linking PELI2 directly to inflammation and anti-pathogen responses[4]. Through these activities, PELI2 plays a critical role in orchestrating host innate immunity and inflammatory signaling. Targets of PELI2 include IRAK1 and possibly NLRP3 (directly or indirectly), but no approved modulatory drugs or established biomarker indications are reported for clinical use as of now[4][6].

Other names

E3 ubiquitin-protein ligase pellino homolog 2Pellino-2RING-type E3 ubiquitin transferase pellino homolog 2Protein pellino homolog 2

Modulation of ubiquitination status of key signaling proteins (e.g., IRAK1, NLRP3) and regulation of downstream signal transduction in innate immune pathways.