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- Title
The role of posttranslational modification in moonlighting glyceraldehyde-3-phosphate dehydrogenase structure and function.
- Authors
Sirover, Michael A.
- Abstract
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a moonlighting protein exhibiting distinct activities apart from its classical role in glycolysis. Regulation of its moonlighting functions and its subcellular localization may be dependent on its posttranslational modification (PTM). The latter include its phosphorylation, which is required for its role in intermembrane trafficking, synaptic transmission and cancer survival; nitrosylation, which is required for its function in apoptosis, heme metabolism and the immune response; acetylation which is necessary for its modulation of apoptotic gene regulation; and N-acetylglucosamine modification which may induce changes in GAPDH oligomeric structure. These findings suggest a structure function relationship between GAPDH posttranslational modification and its diverse moonlighting activities.
- Subjects
GENETIC regulation; NEURAL transmission; N-acetylglucosamine; NITROSYLATION; HEME
- Publication
Amino Acids, 2021, Vol 53, Issue 4, p507
- ISSN
0939-4451
- Publication type
Article
- DOI
10.1007/s00726-021-02959-z