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. 2022 Jul 7;2022:5498743. doi: 10.1155/2022/5498743

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Copyright © 2022 Liang Mao et al.

This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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SIRT4 plays an inhibitory role in cancer by mediating the ADP-ribosylation of GLUD1. (a) Immunofluorescence experiments show that SIRT4 and GLUD1 proteins colocalize in PC-3 and 22rv1 cells. (b) The protein of SIRT4-overexpressing PC-3 and 22rv1 cells was immunoprecipitated with an anti-Flag antibody, and GLUD1 was analyzed by western blotting. GLUD1 was detected in the immunoprecipitated SIRT4 complex, not in the IgG sample. (c) The protein of PC-3 and 22rv1 cells was immunoprecipitated with GLUD1 antibody (rabbit), and SIRT4 was determined by western blotting. SIRT4 was detected in the immunoprecipitated GLUD1 complex, not in the IgG sample. (d, e) The GLUD1 protein was purified in PC-3-Vector, PC-3-SIRT4, 22rv1-vector, and 22rv1-SIRT4 cells, and the ADP-ribosylation of GLUD1 was analyzed by western blotting. (f, g) Endogenous GLUD1 in PC-3 and 22rv1 cells treated with nicotinamide (NAM, 5 mM, 6 h was immunoprecipitated with GLUD1 antibody. The ADP-ribosylation of GLUD1 was analyzed using an anti-PAR antibody via western blotting.