Category: Database

MLKL is the terminal effector of necroptosis. After phosphorylation by RIPK3, MLKL oligomerises and inserts into the plasma membrane, causing membrane rupture and release of inflammatory DAMPs. MLKL is essential for regulated necrotic cell death and immune activation.

PERK is a central ER stress sensor that phosphorylates eIF2α, reduces protein synthesis and activates ATF4‑dependent transcription. Through adaptive and apoptotic signalling, PERK coordinates unfolded protein response pathways that restore proteostasis or eliminate irreparably damaged cells.

IRE1 is the most conserved ER stress sensor, activating XBP1 splicing and RIDD to restore proteostasis. Through its kinase and RNase activities, IRE1 detects misfolded proteins, initiates adaptive signalling and coordinates the unfolded protein response during ER stress.

Aurora C kinase is a germ‑cell‑enriched member of the Chromosomal Passenger Complex that safeguards meiotic chromosome segregation. By regulating kinetochore–microtubule interactions and cytokinesis, Aurora C ensures gamete quality and genomic stability. Its dysregulation contributes to infertility and tumour progression.

Aurora A kinase is a key regulator of centrosome maturation and spindle assembly. By controlling microtubule dynamics, centrosome separation and chromosome alignment, Aurora A ensures accurate mitotic progression. Its frequent overexpression in cancer highlights its importance in genomic stability and tumour development.

Aurora B kinase is the catalytic core of the Chromosomal Passenger Complex, ensuring accurate chromosome segregation, correcting kinetochore–microtubule attachment errors and coordinating cytokinesis. Its central role in mitotic fidelity and frequent dysregulation in cancer make Aurora B a major therapeutic target.

Borealin (CDCA8) is the structural stabiliser of the Chromosomal Passenger Complex. By anchoring Aurora B, INCENP and Survivin to centromeres and guiding CPC relocation to the spindle midzone, Borealin ensures accurate chromosome segregation and successful cytokinesis.

INCENP is the structural and regulatory scaffold of the Chromosomal Passenger Complex. By activating Aurora B kinase, binding microtubules and directing CPC movement from centromeres to the spindle midzone, INCENP ensures accurate chromosome segregation and successful cytokinesis.

TRIM5α is a specialised antiviral ubiquitin ligase that recognises retroviral capsids, assembles K63‑linked ubiquitin chains and promotes autophagic degradation. Its tripartite motif and SPRY domain enable potent restriction of retroviruses, making TRIM5α a key factor in innate antiviral immunity and retroviral defence.

RIG‑I is a cytosolic pattern‑recognition receptor that detects viral RNA and activates innate immunity. Its CARD domains become exposed and ubiquitinated by TRIM25, enabling RIG‑I to bind MAVS and trigger interferon production. Through this pathway, RIG‑I converts viral RNA detection into a strong antiviral response.

MDA5 is a cytosolic receptor that detects long viral double‑stranded RNA and activates MAVS‑dependent interferon signalling. Its ATP‑driven filament formation enables precise recognition of replicating RNA viruses, while LGP2 stabilises MDA5 filaments to ensure accurate antiviral responses.

LGP2 is a regulatory RNA sensor that modulates the activity of RIG‑I and MDA5 rather than directly activating antiviral signalling. By stabilising MDA5 filaments and fine‑tuning RIG‑I responses, LGP2 ensures precise detection of viral RNA and prevents harmful immune overactivation.

The IAP family consists of intracellular proteins that regulate apoptosis, ubiquitination and immune signalling. Through their BIR domains and RING ligase activity, IAPs control caspase inhibition, NF‑κB activation, inflammasome signalling and tumour cell survival, making them central players in cell biology and cancer research.

Survivin (BIRC5) is a tumour‑specific IAP that integrates apoptosis suppression with essential mitotic functions. As part of the chromosomal passenger complex, Survivin ensures proper chromosome segregation while stabilising anti‑apoptotic pathways, making it a central driver of tumour progression and therapy resistance.

NAIP is a pattern‑recognition receptor that detects bacterial ligands such as flagellin and type III secretion system proteins. By recruiting NLRC4 to form the NAIP–NLRC4 inflammasome, NAIP activates caspase‑1, triggers pyroptosis and drives early innate immune defence against intracellular pathogens.