Proteolytic activation of executioner caspase-3 and -7 regulates different physiological processes

The uploaded lipidomics dataset contains Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS) data associated to a publication of Noëlle Sieg et al. from the laboratory of Hamid Kashkar. The title of the publication is: Proteolytic activation of executioner caspase-3 and -7 regulates different physiological processes This article will be published in the EMBO Journal. Article Abstract Caspase-3 (CASP3) and caspase-7 (CASP7) represent the two major executioner caspases that are proteolytically activated by upstreat initiator caspases. They possess almost indistinguishable activity toward synthetic substrates which has led to the overall view that these caspases provide functionally redundant roles. Here, we generated knock-in mice that express cleavage-resistant CASP3(D175A) or CASP7(D198A). Our data showed that the proteolytic activation of CASP3 and CASP7 is decisive for their activation in vivo and controls redundant processes during embryonic development, likely by ensuring apoptosis. In adult mice, however, activation of CASP3 and CASP7 controlled different processes in different tissues. Whereas CASP7 activation was required for male fertility by controlling spermatogenesis without involving apoptosis, CASP3 activation appeared crucial for lymphoid tissue development by regulating interferon (IFN) signaling. Our data shed light on emerging roles of caspases in non-apoptotic processes and provides impetus for reconsidering the involvement of caspases in physiologic and pathologic conditions.