The RasGAP N-terminal fragment generated by caspase cleavage protects cells in a Ras/PI3K/Akt-dependent manner that does not rely on NFkappa B activation.

Détails

ID Serval
serval:BIB_3D81ED52D7E2
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
The RasGAP N-terminal fragment generated by caspase cleavage protects cells in a Ras/PI3K/Akt-dependent manner that does not rely on NFkappa B activation.
Périodique
Journal of Biological Chemistry
Auteur(s)
Yang J.Y., Widmann C.
ISSN
0021-9258
Statut éditorial
Publié
Date de publication
04/2002
Peer-reviewed
Oui
Volume
277
Numéro
17
Pages
14641-14646
Langue
anglais
Résumé
RasGAP, a regulator of Ras GTPase family members, is cleaved at low levels of caspase activity into an N-terminal fragment (fragment N) that generates potent anti-apoptotic signals. At higher levels of caspase activity, fragment N is further cleaved into two fragments that strongly potentiate apoptosis. RasGAP could thus function as a sensor of caspase activity to determine whether a cell should survive or not. Here we show that fragment N protects cells by activating the Ras-PI3K-Akt pathway. Surprisingly, even though nuclear factor kappaB (NFkappaB) can be activated by Akt, it plays no role in the anti-apoptotic functions of fragment N. This indicates that Akt effectors are differentially regulated when fragment N is generated.
Mots-clé
1-Phosphatidylinositol 3-Kinase/metabolism, Apoptosis, Caspases/metabolism, Hela Cells, Humans, Hydrolysis, NF-kappa B/metabolism, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins/metabolism, Proto-Oncogene Proteins c-akt, Signal Transduction, ras GTPase-Activating Proteins/chemistry, ras GTPase-Activating Proteins/metabolism, ras Proteins/metabolism
Pubmed
Web of science
Open Access
Oui
Création de la notice
24/01/2008 15:43
Dernière modification de la notice
20/08/2019 14:33
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