Tag: NF‑κB signalling
cIAP2
cIAP2 is a ubiquitin ligase that regulates TNF receptor signalling, non‑canonical NF‑κB activation and NOD2‑mediated immune responses. By controlling RIPK1, RIPK2 and NIK stability, cIAP2 determines whether cells activate survival pathways or transition into apoptosis, making it essential in inflammation and cancer biology.
cIAP1
cIAP1 is a ubiquitin ligase that regulates TNF receptor signalling and determines whether cells activate NF‑κB survival pathways or switch into apoptosis or necroptosis. By controlling RIPK1 ubiquitination and cooperating with TRAF2, cIAP1 plays essential roles in inflammation, immunity and cancer biology.
K63‑Linked Ubiquitination
K63‑linked ubiquitination is a non‑degradative signalling modification that assembles scaffold‑like ubiquitin chains regulating DNA repair, NF‑κB activation, receptor endocytosis and autophagy. Built by UBE2N/UBE2V1 and specialised E3 ligases, K63 chains coordinate dynamic cellular responses without targeting proteins for proteasomal degradation.
RBR Ubiquitin Ligase
RBR ubiquitin ligases are hybrid E3 enzymes that combine RING‑type E2 binding with HECT‑like catalytic ubiquitin transfer. Through key members such as Parkin, HHARI and HOIP, the RBR family regulates mitophagy, protein‑quality control and M1‑linked ubiquitination in immune signalling, making them central to cellular stress responses and disease mechanisms.
cIAP2
cIAP2 is a ubiquitin ligase that regulates TNF receptor signalling, non‑canonical NF‑κB activation and NOD2‑mediated immune responses. By controlling RIPK1, RIPK2 and NIK stability, cIAP2 determines whether cells activate survival pathways or transition into apoptosis, making it essential in inflammation and cancer biology.
cIAP1
cIAP1 is a ubiquitin ligase that regulates TNF receptor signalling and determines whether cells activate NF‑κB survival pathways or switch into apoptosis or necroptosis. By controlling RIPK1 ubiquitination and cooperating with TRAF2, cIAP1 plays essential roles in inflammation, immunity and cancer biology.
K63‑Linked Ubiquitination
K63‑linked ubiquitination is a non‑degradative signalling modification that assembles scaffold‑like ubiquitin chains regulating DNA repair, NF‑κB activation, receptor endocytosis and autophagy. Built by UBE2N/UBE2V1 and specialised E3 ligases, K63 chains coordinate dynamic cellular responses without targeting proteins for proteasomal degradation.
RBR Ubiquitin Ligase
RBR ubiquitin ligases are hybrid E3 enzymes that combine RING‑type E2 binding with HECT‑like catalytic ubiquitin transfer. Through key members such as Parkin, HHARI and HOIP, the RBR family regulates mitophagy, protein‑quality control and M1‑linked ubiquitination in immune signalling, making them central to cellular stress responses and disease mechanisms.