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

Jun Ho Cho, Rana Lee, Eunju Kim, Yea Eun Choi, Eui Ju Choi

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1 Citation (Scopus)

Abstract

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 SIAH1, thereby reducing the nuclear translocation of GAPDH in lipopolysaccharide (LPS)/interferon (IFN)-γ-activated macrophages. Furthermore, depletion of PRMT1 expression by RNA interference potentiated LPS/IFN-γ-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.

Original languageEnglish
JournalExperimental Cell Research
DOIs
Publication statusAccepted/In press - 2018 Jan 1

Keywords

  • Arginine methylation/GAPDH/ macrophage/nitric oxide/PRMT1

ASJC Scopus subject areas

  • Cell Biology

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