ArticleCell communication and signaling : CCS2026
A non-classical necroptosis pathway mediated by caspases.
Article in Cell communication and signaling : CCS, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
backgroundNecroptosis is a regulated form of cell death mediated by the RIPK1/RIPK3-MLKL pathway. In humans, caspase (CASP) 8 negatively regulates the necroptotic pathway by inactivating RIPK1 and RIPK3. In teleosts and other non-mammalian vertebrates, the role of caspase in necroptosis remains to be explored. By using large yellow croaker Larimichthys crocea as a representative teleost species, this work investigated caspase-mediated regulation on teleost necroptosis.
methodsNecroptosis was investigated with microscopy and biochemical assays. Caspase cleavages were analyzed via immunoblotting. Protein-protein interactions were examined by co-immunoprecipitation. Evolutionary conservations were assessed through sequence alignment and WebLogo analysis.
resultsThe three core necroptotic machinery components (RIPK1, RIPK3, and MLKL) were identified from L. crocea and named LcRIPK1, LcRIPK3, and LcMLKL, respectively. Cellular transfection studies showed that LcRIPK3 complexed with LcRIPK1 and recruited LcMLKL. The recruited LcMLKL was subsequently activated by LcRIPK3. LcMLKL possessed two conserved phosphorylation sites essential to LcMLKL activation, and mimetic phosphorylation of these sites induced strong necroptosis. The activities of LcRIPK1, LcRIPK3, and LcMLKL were all subjected to caspase regulation. L. crocea CASP (LcCASP) 3 and 6 inactivated LcRIPK1 by preferentially cleaving at
conclusionsThis study revealed a non-canonical necroptotic pathway mediated by integrated caspase regulation networks in teleosts and provided a strong hypothesis for the existence of a conserved CASPs-MLKL pathway in other vertebrate lineages. These findings added new insights into the complex regulation mechanisms of necroptosis in Vertebrata.
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