The caspase-generated cleavage product of ...
Type de document :
Article dans une revue scientifique
PMID :
URL permanente :
Titre :
The caspase-generated cleavage product of Ets-1 p51 and Ets-1 p27, Cp17, induces apoptosis
Auteur(s) :
Choul-Li, Souhaila [Auteur]
Université Chouaib Doukkali [UCD]
Tulasne, David [Auteur]
Mécanismes de la Tumorigénèse et Thérapies Ciblées (M3T) - UMR 8161
Mécanismes de la Tumorigénèse et Thérapies Ciblées - UMR 8161 [M3T]
Aumercier, Marc [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Université Chouaib Doukkali [UCD]
Tulasne, David [Auteur]
Mécanismes de la Tumorigénèse et Thérapies Ciblées (M3T) - UMR 8161
Mécanismes de la Tumorigénèse et Thérapies Ciblées - UMR 8161 [M3T]
Aumercier, Marc [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Titre de la revue :
Biochemical and biophysical research communications
Nom court de la revue :
Biochem. Biophys. Res. Commun.
Numéro :
480
Pagination :
1-7
Date de publication :
2016-11-04
ISSN :
1090-2104
Mot(s)-clé(s) en anglais :
Peptide Fragments
Exons
Humans
Caspase
Ets-1
Recombinant Proteins
Animals
Protein Isoforms
HEK293 Cells
Dogs
Madin Darby Canine Kidney Cells
Caspase 3
Proto-Oncogene Protein c-ets-1
Cp17 fragment
Apoptosis
Exons
Humans
Caspase
Ets-1
Recombinant Proteins
Animals
Protein Isoforms
HEK293 Cells
Dogs
Madin Darby Canine Kidney Cells
Caspase 3
Proto-Oncogene Protein c-ets-1
Cp17 fragment
Apoptosis
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
The transcription factor Ets-1 is involved in various physiological processes and invasive pathologies. Human Ets-1 exists under three isoforms: p51, the predominant full-length isoform, p42 and p27, shorter alternatively ...
Lire la suite >The transcription factor Ets-1 is involved in various physiological processes and invasive pathologies. Human Ets-1 exists under three isoforms: p51, the predominant full-length isoform, p42 and p27, shorter alternatively spliced isoforms. We have previously demonstrated that Ets-1 p51, but not the spliced variant Ets-1 p42, is processed by caspases in vitro and during apoptosis. However, the caspase cleavage of the second spliced variant Ets-1 p27 remains to investigate. In the present study, we demonstrate that Ets-1 p27 is a cleavage substrate of caspases. We show that Ets-1 p27 is processed in vitro by caspase-3, resulting in three C-terminal fragments Cp20, Cp17 and Cp14. Similarly, Ets-1 p27 was cleaved during apoptotic cell death induced by anisomycin, producing fragments consistent with those observed in in vitro cleavage assay. These fragments are generated by cleavage at three sites located in the exon VII-encoded region of Ets-1 p27. As a functional consequences, Cp17 fragment, the major cleavage product generated during apoptosis, induced itself apoptosis when transfected into cells. Our results show that Ets-1 p27 is cleaved in the same manner as Ets-1 p51 within the exon VII-encoded region, thus generating a stable C-terminal fragment that induces cell death by initiating apoptosis.Lire moins >
Lire la suite >The transcription factor Ets-1 is involved in various physiological processes and invasive pathologies. Human Ets-1 exists under three isoforms: p51, the predominant full-length isoform, p42 and p27, shorter alternatively spliced isoforms. We have previously demonstrated that Ets-1 p51, but not the spliced variant Ets-1 p42, is processed by caspases in vitro and during apoptosis. However, the caspase cleavage of the second spliced variant Ets-1 p27 remains to investigate. In the present study, we demonstrate that Ets-1 p27 is a cleavage substrate of caspases. We show that Ets-1 p27 is processed in vitro by caspase-3, resulting in three C-terminal fragments Cp20, Cp17 and Cp14. Similarly, Ets-1 p27 was cleaved during apoptotic cell death induced by anisomycin, producing fragments consistent with those observed in in vitro cleavage assay. These fragments are generated by cleavage at three sites located in the exon VII-encoded region of Ets-1 p27. As a functional consequences, Cp17 fragment, the major cleavage product generated during apoptosis, induced itself apoptosis when transfected into cells. Our results show that Ets-1 p27 is cleaved in the same manner as Ets-1 p51 within the exon VII-encoded region, thus generating a stable C-terminal fragment that induces cell death by initiating apoptosis.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Collections :
Équipe(s) de recherche :
Biologie structurale et intégrative
Date de dépôt :
2020-02-12T15:11:30Z
2021-03-26T09:28:57Z
2021-03-26T09:28:57Z