AI Article Synopsis

  • - The study investigates how oxidative stress affects the mobility and function of B-cell lymphoma (BCL-2-interacting cell death suppressor, BIS) through phosphorylation by extracellular signaling-regulated kinase (ERK).
  • - Key amino acids Thr285 and Ser289 in BIS are identified as phosphorylation sites, and their deletion partially reduces the protein's mobility shift under oxidative stress, increasing cell death sensitivity in A172 cells.
  • - The findings suggest that the phosphorylation of BIS by ERK influences the nuclear translocation of heat shock transcription factor (HSF1) and the expression of heat shock protein (HSP) 70, affecting how cells respond to oxidative stress.

Article Abstract

B-cell lymphoma (BCL)-2-interacting cell death suppressor (BIS) has diverse cellular functions depending on its binding partners. However, little is known about the effects of biochemical modification of BIS on its various activities under oxidative stress conditions. In this study, we showed that HO reduced BIS mobility on SDS-polyacrylamide gels in a time-dependent manner via the activation of extracellular signaling-regulated kinase (ERK). The combined results of mass spectroscopy and computational prediction identified Thr285 and Ser289 in BIS as candidate residues for phosphorylation by ERK under oxidative stress conditions. Deletion of these sites resulted in a partial reduction in the HO-induced mobility shift relative to that of the wild-type BIS protein; overexpression of the deletion mutant sensitized A172 cells to HO-induced cell death without increasing the level of intracellular reactive oxygen species. Expression of the BIS deletion mutant decreased the level of heat shock protein (HSP) 70 mRNA following HO treatment, which was accompanied by impaired nuclear translocation of heat shock transcription factor (HSF) 1. Co-immunoprecipitation assays revealed that the binding of wild-type BIS to HSF1 was decreased by oxidative stress, while the binding of the BIS deletion mutant to HSF1 was not affected. These results indicate that ERK-dependent phosphorylation of BIS has a role in the regulation of nuclear translocation of HSF1 likely through modulation of its interaction affinity with HSF1, which affects HSP70 expression and sensitivity to oxidative stress.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5050300PMC
http://dx.doi.org/10.1038/emm.2016.84DOI Listing

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