Controlling Cell Death through Post-translational Modifications of DED Proteins.
DED proteins
SUMOylation
apoptosis
nitrosylation
phosphorylation
ubiquitylation
Journal
Trends in cell biology
ISSN: 1879-3088
Titre abrégé: Trends Cell Biol
Pays: England
ID NLM: 9200566
Informations de publication
Date de publication:
05 2020
05 2020
Historique:
received:
13
11
2019
revised:
12
02
2020
accepted:
19
02
2020
entrez:
18
4
2020
pubmed:
18
4
2020
medline:
25
6
2021
Statut:
ppublish
Résumé
Apoptosis is a form of programmed cell death, deregulation of which occurs in multiple disorders, including neurodegenerative and autoimmune diseases as well as cancer. The formation of a death-inducing signaling complex (DISC) and death effector domain (DED) filaments are critical for initiation of the extrinsic apoptotic pathway. Post-translational modifications (PTMs) of DED-containing DISC components such as FADD, procaspase-8, and c-FLIP comprise an additional level of apoptosis regulation, which is necessary to overcome the threshold for apoptosis induction. In this review we discuss the influence of PTMs of FADD, procaspase-8, and c-FLIP on DED filament assembly and cell death induction, with a focus on the 3D organization of the DED filament.
Identifiants
pubmed: 32302548
pii: S0962-8924(20)30041-6
doi: 10.1016/j.tcb.2020.02.006
pii:
doi:
Substances chimiques
Death Domain Receptor Signaling Adaptor Proteins
0
Caspase 8
EC 3.4.22.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
354-369Informations de copyright
Copyright © 2020 The Authors. Published by Elsevier Ltd.. All rights reserved.