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Article Abstract
To investigate Livin-mediated regulation of H2A.X phosphorylation via a novel kinase activity and its effect on autophagy in colon cancer cells. The interaction between Livin and H2A.X was tested by immunoprecipitation. H2A.X-/- HCT116 cells were transfected with human influenza hemagglutinin (HA)-tagged WT or Y142F phospho-dead mutantH2A.X plasmids. GST-tagged recombinant Livin protein was used to perform pull-down experiment and kinase assay. H2A.X-/-Livin+/+ SW480 cells were co-transfected with H2A.X/H2A.X plasmid and LC3 EGFP-tagged plasmid to explore whether H2A.X was involved in Livin-mediated autophagy induced by starvation in colon cancer cells. Co-immunoprecipitation studies confirmed that Livin interacted with H2A.X and that it was phosphorylation dependent. kinase assay confirmed that Livin could phosphorylate H2A.X. Knockdown of Livin (Livin-/-) in SW480 cells or HCT116 cells canceled the starvation-induced autophagy in colon cancer cells; H2A.X-/-Livin+/+ SW480 cells transfected with H2A.X activated autophagy induced by starvation while cells transfected with H2A.X had no significant difference; Livin-H2A.X axis activated autophagy in colon cancer cells through transcriptionally regulating and . Livin promotes autophagy in colon cancer cells via regulating the phosphorylation of H2A.X.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6868062 | PMC |
| http://dx.doi.org/10.3389/fonc.2019.01233 | DOI Listing |
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