The diverse functions of GAPDH: Views from different subcellular compartments

Carlos Tristan, Neelam Shahani, Thomas W. Sedlak, Akira Sawa

Research output: Contribution to journalReview articlepeer-review

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.

Original languageEnglish (US)
Pages (from-to)317-323
Number of pages7
JournalCellular Signalling
Volume23
Issue number2
DOIs
StatePublished - Feb 1 2011

Keywords

  • Cytoplasm
  • Cytoskeleton
  • GAPDH
  • GOSPEL
  • Glyceraldehyde 3-phosphate dehydrogenase
  • Microtubules
  • Mitochondria
  • Nucleus
  • Oxidative stress
  • S-nitrosylation
  • Siah
  • Stress signaling
  • Vesicular trafficking

ASJC Scopus subject areas

  • Cell Biology

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