PRMT1 negatively regulates activation-induced cell death in macrophages by arginine methylation of GAPDH
- Authors
- Cho, Jun-Ho; Lee, Rana; Kim, Eunju; Choi, Yea Eun; Choi, Eui-Ju
- Issue Date
- 1-7월-2018
- Publisher
- ELSEVIER INC
- Keywords
- Arginine methylation/GAPDH/macrophage/nitric oxide/PRMT1
- Citation
- EXPERIMENTAL CELL RESEARCH, v.368, no.1, pp.50 - 58
- Indexed
- SCIE
SCOPUS
- Journal Title
- EXPERIMENTAL CELL RESEARCH
- Volume
- 368
- Number
- 1
- Start Page
- 50
- End Page
- 58
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/74386
- DOI
- 10.1016/j.yexcr.2018.04.012
- ISSN
- 0014-4827
- 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 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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