Moonlighting glyceraldehyde-3-phosphate dehydrogenase: posttranslational modification, protein and nucleic acid interactions in normal cells and in human pathology

Abstract

Moonlighting glyceraldehyde-3-phosphate dehydrogenase (GAPDH) exhibits multiple functions separate and distinct from its historic role in energy production. Further, it exhibits dynamic changes in its subcellular localization which is an a priori requirement for its multiple activities. Separately, moonlighting GAPDH may function in the pathology of human disease, involved in tumorigenesis, diabetes, and age-related neurodegenerative disorders. It is suggested that moonlighting GAPDH function may be related to specific modifications of its protein structure as well as the formation of GAPDH protein: protein or GAPDH protein: nucleic acid complexes.

Keywords:

• Glyceraldehyde-3-phosphate dehydrogenase
• moonlighting protein
• posttranslational modification
• mRNA stability
• DNA structure

Disclosure statement

No potential conflict of interest was reported by the author(s).

Notes

* There is some variability in GAPDH sequence with some species having two additional amino acids.

Additional information

Funding

Studies in the author’s laboratory were funded by the National Institutes of Health, the National Science Foundation and the W.W. Charitable Trust.