Format

Send to

Choose Destination
J Biol Chem. 2014 Feb 7;289(6):3775-85. doi: 10.1074/jbc.M113.531640. Epub 2013 Dec 21.

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

Author information

1
From the Key Laboratory of Molecular Medicine, Ministry of Education, and Department of Biochemistry and Molecular Biology, Fudan University Shanghai Medical College, Shanghai 200032, China.

Abstract

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.

KEYWORDS:

Acetylation; Cell Growth; GAPDH; Glycolysis; HDAC5; Histone Deacetylase; Lung Cancer; Metabolism; PCAF; Tumorigenesis

PMID:
24362262
PMCID:
PMC3916574
DOI:
10.1074/jbc.M113.531640
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center