MMP7 cleavage of amino-terminal CD95 death receptor switches signaling toward non-apoptotic pathways.
Journal
Cell death & disease
ISSN: 2041-4889
Titre abrégé: Cell Death Dis
Pays: England
ID NLM: 101524092
Informations de publication
Date de publication:
23 10 2022
23 10 2022
Historique:
received:
25
07
2022
accepted:
14
10
2022
revised:
12
10
2022
entrez:
23
10
2022
pubmed:
24
10
2022
medline:
26
10
2022
Statut:
epublish
Résumé
CD95 is a death receptor that can promote oncogenesis through molecular mechanisms that are not fully elucidated. Although the mature CD95 membrane receptor is considered to start with the arginine at position 17 after elimination of the signal peptide, this receptor can also be cleaved by MMP7 upstream of its leucine at position 37. This post-translational modification occurs in cancer cells but also in normal cells such as peripheral blood leukocytes. The non-cleaved CD95 amino-terminal region consists in a disordered domain and its in silico reconstitution suggests that it might contribute to receptor aggregation and thereby, regulate the downstream death signaling pathways. In agreement with this molecular modeling analysis, the comparison of CD95-deficient cells reconstituted with full-length or N-terminally truncated CD95 reveals that the loss of the amino-terminal region of CD95 impairs the initial steps of the apoptotic signal while favoring the induction of pro-survival signals, including the PI3K and MAPK pathways.
Identifiants
pubmed: 36274061
doi: 10.1038/s41419-022-05352-0
pii: 10.1038/s41419-022-05352-0
pmc: PMC9588774
doi:
Substances chimiques
fas Receptor
0
Matrix Metalloproteinase 7
EC 3.4.24.23
Leucine
GMW67QNF9C
Phosphatidylinositol 3-Kinases
EC 2.7.1.-
Protein Sorting Signals
0
Arginine
94ZLA3W45F
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
895Informations de copyright
© 2022. The Author(s).
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