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Cell Signal. 2011 Feb;23(2):317-23. doi: 10.1016/j.cellsig.2010.08.003. Epub 2010 Aug 19.

The diverse functions of GAPDH: views from different subcellular compartments.

Author information

1
Department of Psychiatry, Johns Hopkins University School of Medicine, Baltimore, MD 21287, USA.

Abstract

Multiple roles for glyceraldehyde-3-phosphate dehydrogenase (GAPDH) have been recently appreciated. In addition to the cytoplasm where the majority of GAPDH is located under the basal condition, GAPDH is also found in the particulate fractions, such as the nucleus, the mitochondria, and the small vesicular fractions. When cells are exposed to various stressors, dynamic subcellular re-distribution of GAPDH occurs. Here we review these multifunctional properties of GAPDH, especially linking them to its oligomerization, posttranslational modification, and subcellular localization. This includes mechanistic descriptions of how S-nitrosylation of GAPDH under oxidative stress may lead to cell death/dysfunction via nuclear translocation of GAPDH, which is counteracted by a cytosolic GOSPEL. GAPDH is also involved in various diseases, especially neurodegenerative disorders and cancers. Therapeutic strategies to these conditions based on molecular understanding of GAPDH are discussed.

PMID:
20727968
PMCID:
PMC3084531
DOI:
10.1016/j.cellsig.2010.08.003
[Indexed for MEDLINE]
Free PMC Article

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