Cullin-4B E3 ubiquitin ligase mediates Apaf-1 ubiquitination to regulate caspase-9 activity.
Journal
PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081
Informations de publication
Date de publication:
2019
2019
Historique:
received:
24
01
2019
accepted:
01
07
2019
entrez:
23
7
2019
pubmed:
23
7
2019
medline:
28
2
2020
Statut:
epublish
Résumé
Apoptotic protease-activating factor 1 (Apaf-1) is a component of apoptosome, which regulates caspase-9 activity. In addition to apoptosis, Apaf-1 plays critical roles in the intra-S-phase checkpoint; therefore, impaired expression of Apaf-1 has been demonstrated in chemotherapy-resistant malignant melanoma and nuclear translocation of Apaf-1 has represented a favorable prognosis of patients with non-small cell lung cancer. In contrast, increased levels of Apaf-1 protein are observed in the brain in Huntington's disease. The regulation of Apaf-1 protein is not yet fully understood. In this study, we show that etoposide triggers the interaction of Apaf-1 with Cullin-4B, resulting in enhanced Apaf-1 ubiquitination. Ubiquitinated Apaf-1, which was degraded in healthy cells, binds p62 and forms aggregates in the cytosol. This complex of ubiquitinated Apaf-1 and p62 induces caspase-9 activation following MG132 treatment of HEK293T cells that stably express bcl-xl. These results show that ubiquitinated Apaf-1 may activate caspase-9 under conditions of proteasome impairment.
Identifiants
pubmed: 31329620
doi: 10.1371/journal.pone.0219782
pii: PONE-D-19-02233
pmc: PMC6645535
doi:
Substances chimiques
APAF1 protein, human
0
Apoptotic Protease-Activating Factor 1
0
CUL4B protein, human
0
Cullin Proteins
0
Leupeptins
0
bcl-X Protein
0
Etoposide
6PLQ3CP4P3
Caspase 9
EC 3.4.22.-
benzyloxycarbonylleucyl-leucyl-leucine aldehyde
RF1P63GW3K
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0219782Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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