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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.

  • Yang JY Institut de Biologie Cellulaire et de Morphologie, Université de Lausanne, 1005 Lausanne, Switzerland.
  • Widmann C
  • 2002-02-16
Published in:
  • The Journal of biological chemistry. - 2002
Apoptosis
Caspases
HeLa Cells
Humans
Hydrolysis
NF-kappa B
Phosphatidylinositol 3-Kinases
Protein-Serine-Threonine Kinases
Proto-Oncogene Proteins
Proto-Oncogene Proteins c-akt
Signal Transduction
ras GTPase-Activating Proteins
ras Proteins
English 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.
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  • English
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bronze
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https://sonar.ch/global/documents/139131
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