Cited by 663Redox biology and oxidative stressCell death mechanisms and regulationGlutathione Transferases and Polymorphisms

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The diverse functions of GAPDH: Views from different subcellular compartments

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Tristan, Carlos, Shahani, Neelam, Sedlak, Thomas W., Sawa, Akira·2011·Cellular Signalling

DOI 10.1016/j.cellsig.2010.08.003PMC PMC3084531

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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.

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Colell, A., Ricci, J.-E., Tait, S., Milasta, S., Maurer, U., Bouchier-Hayes, L., Fitzgerald, P., Guio-Carrion, A., Waterhouse, N. J., Li, C. W., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.045 · Cited by 516
Sequence-Specific Binding of Transfer RNA by Glyceraldehyde-3-Phosphate Dehydrogenase
Singh, R., & Green, M. R. (1993) · Science · doi:10.1126/science.8420004 · Cited by 481
Huntingtin and DRPLA proteins selectively interact with the enzyme GAPDH
Burke, J. R., Enghild, J. J., Martin, M. E., Jou, Y., Myers, R., Roses, A. D., Vance, J. M., & Strittmatter, W. J. (1996) · Nature Medicine · doi:10.1038/nm0396-347 · Cited by 430
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Flagged first, then by citations

Show all 86 references

Research works printed but not linked: 4

Brune, 1995, Genet. Eng. (N Y), 17, 149
Reiss, 1996, Biochem. Mol. Biol. Int., 40, 1191
Kusner, 2004, Invest. Ophthalmol. Vis. Sci., 45, 1553
Waldmeier, 2000, J. Neural Transm. Suppl., 197

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Authors: Tristan, C., Shahani, N., Sedlak, T. W., & Sawa, A.
Affiliations: Johns Hopkins University (US)
Corresponding author: Sawa, Akira
ORCID: Tristan, Carlos
Shahani, Neelam
Sedlak, Thomas W.
Sawa, Akira
Venue: Cellular Signalling
Publisher: Elsevier BV
Published: 2011-02
Volume: 23
Issue: 2
Pages: 317-323
ISSN: 0898-6568 (ISSN-L)
DOI: 10.1016/j.cellsig.2010.08.003
PMC: PMC3084531
OpenAlex: W2139503567
Cited by: 663
References: 86
Citations by year: 2026: 43 · 2025: 49 · 2024: 34 · 2023: 42 · 2022: 47 · 2021: 67 · 2020: 53 · 2019: 37 · 2018: 38 · 2017: 49 · 2016: 40 · 2015: 37 · 2014: 37 · 2013: 37 · 2012: 37
FWCI: 2.52
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Cellular Signalling (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: USPHS (MH-084018, MH-069853, MH-085226, MH-088753)
Stanley
CHDI
HighQ
RUSK
NARSAD
NINDS
S-R
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
Keywords: glyceraldehyde-3-phosphate dehydrogenase, nuclear translocation, S-nitrosylation, oxidative stress, post-translational modification, protein oligomerization, Gospels, neurodegenerative diseases, cancer, cell death
MeSH terms: Animals, Cell Nucleus, Cytoplasm, Cytoskeleton, Glyceraldehyde-3-Phosphate Dehydrogenases, Humans, Mitochondria, Vesicular Transport Proteins

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