Bergmann, Andreas2022-08-232022-08-232018-08-032018-10-04<p>Oncotarget. 2018 Aug 3;9(60):31566-31567. doi: 10.18632/oncotarget.25796. eCollection 2018 Aug 3. <a href="https://doi.org/10.18632/oncotarget.25796">Link to article on publisher's site</a></p>1949-2553 (Linking)10.18632/oncotarget.2579630167077https://hdl.handle.net/20.500.14038/40757Critical mediators of apoptotic cell death are caspases, a highly specialized class of Cys-proteases that cleave substrates after Asp residues. Under normal conditions, caspases are cytosolic proteins. After their activation, they cleave a large number of cytosolic proteins and execute apoptosis (Figure 1, left). However, in addition to their well-studied role in apoptosis, caspases also have many non-apoptotic functions [1, 2]. It is not very well understood how cells escape the potential harmful action of caspases when they perform nonapoptotic functions. In our recent work, we now show that epithelial cells may prevent apoptosis by sequestration of caspases at the plasma membrane, specifically the basal side of the plasma membrane, for non-apoptotic functions [3].en-USCopyright: Bergmann et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License 3.0 (CC BY 3.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.http://creativecommons.org/licenses/by/3.0/apoptosis-induced proliferationundead cellscaspaseMyo1Dplasma membraneAmino Acids, Peptides, and ProteinsCell BiologyCellsCellular and Molecular PhysiologyEnzymes and CoenzymesEditorialhttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=4573&amp;context=oapubs&amp;unstamped=1https://escholarship.umassmed.edu/oapubs/356113014897oapubs/3561