<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Yang JY</submitter><funding>Swiss National Science Foundation</funding><pagination>10425-36</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC529026</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>24(23)</volume><pubmed_abstract>Tight control of apoptosis is required for proper development and maintenance of homeostasis in multicellular organisms. Cells can protect themselves from potentially lethal stimuli by expressing antiapoptotic factors, such as inhibitors of apoptosis, FLICE (caspase 8)-inhibitory proteins, and members of the Bcl2 family. Here, we describe a mechanism that allows cells to survive once executioner caspases have been activated. This mechanism relies on the partial cleavage of RasGAP by caspase 3 into an amino-terminal fragment called fragment N. Generation of this fragment leads to the activation of the antiapoptotic Akt kinase, preventing further amplification of caspase activity. Partial cleavage of RasGAP is required for cell survival under stress conditions because cells expressing an unc</pubmed_abstract><journal>Molecular and cellular biology</journal><pubmed_title>Partial cleavage of RasGAP by caspases is required for cell survival in mild stress conditions.</pubmed_title><pmcid>PMC529026</pmcid><funding_grant_id>066797</funding_grant_id><pubmed_authors>Yang JY</pubmed_authors><pubmed_authors>Murphy BM</pubmed_authors><pubmed_authors>Walicki J</pubmed_authors><pubmed_authors>Kasibhatla S</pubmed_authors><pubmed_authors>Martin SJ</pubmed_authors><pubmed_authors>Michod D</pubmed_authors><pubmed_authors>Widmann C</pubmed_authors></additional><is_claimable>false</is_claimable><name>Partial cleavage of RasGAP by caspases is required for cell survival in mild stress conditions.</name><description>Tight control of apoptosis is required for proper development and maintenance of homeostasis in multicellular organisms. Cells can protect themselves from potentially lethal stimuli by expressing antiapoptotic factors, such as inhibitors of apoptosis, FLICE (caspase 8)-inhibitory proteins, and members of the Bcl2 family. Here, we describe a mechanism that allows cells to survive once executioner caspases have been activated. This mechanism relies on the partial cleavage of RasGAP by caspase 3 into an amino-terminal fragment called fragment N. Generation of this fragment leads to the activation of the antiapoptotic Akt kinase, preventing further amplification of caspase activity. Partial cleavage of RasGAP is required for cell survival under stress conditions because cells expressing an unc</description><dates><release>2004-01-01T00:00:00Z</release><publication>2004 Dec</publication><modification>2025-04-05T10:01:11.924Z</modification><creation>2019-03-27T01:08:21Z</creation></dates><accession>S-EPMC529026</accession><cross_references><pubmed>15542850</pubmed><doi>10.1128/MCB.24.23.10425-10436.2004</doi><doi>10.1128/mcb.24.23.10425-10436.2004</doi></cross_references></HashMap>