The caspase-generated cleavage product of ...
Document type :
Article dans une revue scientifique
PMID :
Permalink :
Title :
The caspase-generated cleavage product of Ets-1 p51 and Ets-1 p27, Cp17, induces apoptosis
Author(s) :
Choul-Li, Souhaila [Auteur]
Université Chouaib Doukkali [UCD]
Tulasne, David [Auteur]
Mécanismes de la Tumorigénèse et Thérapies Ciblées - UMR 8161 [M3T]
Aumercier, Marc [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Université Chouaib Doukkali [UCD]
Tulasne, David [Auteur]

Mécanismes de la Tumorigénèse et Thérapies Ciblées - UMR 8161 [M3T]
Aumercier, Marc [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Journal title :
Biochemical and biophysical research communications
Abbreviated title :
Biochem. Biophys. Res. Commun.
Volume number :
480
Pages :
1-7
Publication date :
2016-11-04
ISSN :
1090-2104
English keyword(s) :
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
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Collections :
Research team(s) :
Biologie structurale et intégrative
Submission date :
2020-02-12T15:11:30Z
2021-03-26T09:28:57Z
2021-03-26T09:28:57Z