Viral M45 and necroptosis-associated proteins form heteromeric amyloid assemblies.
Amyloid
/ chemistry
Amyloidosis
/ etiology
Animals
Carrier Proteins
/ chemistry
Cell Line
Humans
Mice
Models, Molecular
Necroptosis
Protein Aggregation, Pathological
/ metabolism
Protein Binding
Protein Multimerization
Receptor-Interacting Protein Serine-Threonine Kinases
/ metabolism
Ribonucleotide Reductases
/ chemistry
Structure-Activity Relationship
Viral Proteins
/ chemistry
M45
RIP homotypic interaction motif
RIPK3
amyloid
necroptosis
Journal
EMBO reports
ISSN: 1469-3178
Titre abrégé: EMBO Rep
Pays: England
ID NLM: 100963049
Informations de publication
Date de publication:
02 2019
02 2019
Historique:
received:
31
05
2018
revised:
05
11
2018
accepted:
07
11
2018
pubmed:
1
12
2018
medline:
21
4
2020
entrez:
1
12
2018
Statut:
ppublish
Résumé
The murine cytomegalovirus protein M45 protects infected mouse cells from necroptotic death and, when heterologously expressed, can protect human cells from necroptosis induced by tumour necrosis factor receptor (TNFR) activation. Here, we show that the N-terminal 90 residues of the M45 protein, which contain a RIP homotypic interaction motif (RHIM), are sufficient to confer protection against TNFR-induced necroptosis. This N-terminal region of M45 drives rapid self-assembly into homo-oligomeric amyloid fibrils and interacts with the RHIMs of the human kinases RIPK1 and RIPK3, and the Z-DNA binding protein 1 (ZBP1), to form heteromeric amyloid fibrils
Identifiants
pubmed: 30498077
pii: embr.201846518
doi: 10.15252/embr.201846518
pmc: PMC6362354
pii:
doi:
Substances chimiques
Amyloid
0
Carrier Proteins
0
Viral Proteins
0
Ribonucleotide Reductases
EC 1.17.4.-
m45 protein, Mouse cytomegalovirus 1
EC 1.17.4.-
RIPK1 protein, human
EC 2.7.11.1
RIPK3 protein, human
EC 2.7.11.1
Receptor-Interacting Protein Serine-Threonine Kinases
EC 2.7.11.1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Commentaires et corrections
Type : CommentIn
Informations de copyright
© 2018 The Authors.
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