4.6 Article

PRMT1 negatively regulates activation-induced cell death in macrophages by arginine methylation of GAPDH

Journal

EXPERIMENTAL CELL RESEARCH
Volume 368, Issue 1, Pages 50-58

Publisher

ELSEVIER INC
DOI: 10.1016/j.yexcr.2018.04.012

Keywords

Arginine methylation/GAPDH/macrophage/nitric oxide/PRMT1

Funding

  1. National Research Foundation grant [NRF-2017R1A2B2008193]
  2. BRL grant - Ministry of Science and ICT of Korea [NRF-2015R1A4A1041919]
  3. Korea University grant

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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is implicated in cell death in addition to a role as a glycolytic enzyme. In particular, when cells are exposed to cellular stressors involving nitric oxide (NO) production, GAPDH can undergo NO -induced S-nitrosylation and S-nitrosylated GAPDH has been shown to elicit apoptosis. However, the mechanism underlying the regulation of the pro-apoptotic function of GAPDH remains unclear. Here, we found that protein arginine methyltransferase 1 (PRMT1) mediated arginine methylation of GAPDH in primary bone marrow-derived macrophages in a NO-dependent manner. Moreover, PRMT1 inhibited S-nitrosylation of GAPDH as well as its binding to STAHl, thereby reducing the nuclear translocation of GAPDH in lipopolysaccharide (LPS)/interferon (IFN)-gamma-activated macrophages. Furthermore, depletion of PRMT1 expression by RNA interference potentiated LPS/IFN-gamma-induced apoptosis in macrophages. Taken together, our results suggest that PRMT1 has a previously unrecognized function to inhibit activation-induced cell death of macrophages through arginine methylation of GAPDH.

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