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Glyceraldehyde-3-phosphate dehydrogenase is activated by lysine 254 acetylation in response to glucose signal.

J. Biol. Chem.. 2014; 
LiTingting,LiuMengxi,FengXu,WangZhen,DasIndrani,XuYanping,ZhouXin,SunYiping,GuanKun-Liang,XiongYue,LeiQun-
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Catalog Antibody … Antibodies to FLAG (catalogue no. A00170 from GenScript or catalogue no. A2220 from Sigma), GAPDH (used for IP, 5632-1, Epitomics; 1:100), GAPDH (6C5) (SC32233, Santa Cruz Biotechnology), HA (F7) (SC7392, Santa Cruz Biotechnology), and β-actin (13E5) (no … Get A Quote

摘要

The altered metabolism in most tumor cells consists of elevated glucose uptake and increased glycolysis even in the presence of high oxygen tension. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an obligatory enzyme in glycolysis. Here, we report that acetylation at lysine 254 (K254) increases GAPDH activity in response to glucose. Furthermore, acetylation of GAPDH (K254) is reversibly regulated by the acetyltransferase PCAF and the deacetylase HDAC5. Substitution of K254 to glutamine compromises the ability of GAPDH to support cell proliferation and tumor growth. Our study reveals a mechanism of GAPDH enzyme activity regulation by acetylation and its critical role in cellular regulation.

关键词

Acetylation,Cell Growth,GAPDH,Glycolysis,HDAC5,Histone Deacetylase,Lung Cancer,Metabolism,PCAF,Tumorigen