Immunoblot Analysis of the Regulation of TNF Receptor Family-Induced NF-κB Signaling by c-IAP Proteins.
IAP
IAP antagonist
Inhibitor of apoptosis
NF-kB
NIK
Proteasomal degradation
RING domain
RIP1
TNF
TRAF2
Ubiquitin
c-IAP1/2
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2021
2021
Historique:
entrez:
8
7
2021
pubmed:
9
7
2021
medline:
13
1
2022
Statut:
ppublish
Résumé
Proper maintenance of organismal homeostasis, development, and immune defense requires precise regulation of survival and signaling pathways. Inhibitor of apoptosis (IAP) proteins are evolutionarily conserved regulators of cell death and immune signaling that impact numerous cellular processes. Although initially characterized as inhibitors of apoptosis, the ubiquitin ligase activity of IAP proteins is critical for modulating various signaling pathways (e.g., NF-κB, MAPK) and cell survival. Cellular IAP1 and 2 regulate the pro-survival canonical NF-κB pathway by ubiquitinating RIP1 and themselves thus enabling recruitment of kinase (IKK) and E3 ligase (LUBAC) complexes. On the other hand, c-IAP1 and c-IAP2 are negative regulators of noncanonical NF-κB signaling by promoting ubiquitination and consequent proteasomal degradation of the NF-κB-inducing kinase NIK. Here we describe the involvement of c-IAP1 and c-IAP2 in NF-κB signaling and provide detailed methodology for examining functional roles of c-IAPs in these pathways.
Identifiants
pubmed: 34236635
doi: 10.1007/978-1-0716-1669-7_7
doi:
Substances chimiques
Inhibitor of Apoptosis Proteins
0
NF-kappa B
0
Receptors, Tumor Necrosis Factor
0
Tumor Necrosis Factor-alpha
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
109-123Références
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