The DOI matches its Crossref record; 87 of the 87 references it cites were found in a registry or an index.
The diverse functions of GAPDH: Views from different subcellular compartments
Open accessAbstract
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Redox changes may also affect posttranslational modifications of GAPDH, altering its binding to mRNA, metabolites, as well as its localization within the cell (113, 114).”
From Fueling Immunity: Insights into Metabolism and Lymphocyte Function (2013) · cites this paper as [114]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Protein S-nitrosylation: a physiological signal for neuronal nitric oxide
Jaffrey, S. R., Erdjument‐Bromage, H., Ferris, C. D., Tempst, P., & Snyder, S. H. (2001) · Nature Cell Biology · doi:10.1038/35055104 · Cited by 1,402
S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
Hara, M. R., Agrawal, N., Kim, S. F., Cascio, M. B., Fujimuro, M., Ozeki, Y., Takahashi, M., Cheah, J. H., Tankou, S. K., Hester, L. D., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1268 · Cited by 1,079
Self-citationDu, X., Matsumura, T., Edelstein, D., Rossetti, L., Zsengellér, Z. K., Szabó, C., & Brownlee, M. (2003) · Journal of Clinical Investigation · doi:10.1172/jci18127 · Cited by 843
Protein S-nitrosylation in health and disease: a current perspective
Foster, M. W., Hess, D. T., & Stamler, J. S. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.06.007 · Cited by 752
Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress
Ralser, M., Wamelink, M. M. C., Kowald, A., Gerisch, B., Heeren, G., Struys, E. A., Klipp, E., Jakobs, C., Breitenbach, M., Lehrach, H. R., et al. (2007) · Journal of Biology · doi:10.1186/jbiol61 · Cited by 627
Zheng, L., Roeder, R. G., & Luo, Y. (2003) · Cell · doi:10.1016/s0092-8674(03)00552-x · Cited by 534
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
Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation
Choi, Y., Tenneti, L., Le, D. A., Ortiz, J., Bai, G., Chen, H.-S. V., & Lipton, S. A. (2000) · Nature Neuroscience · doi:10.1038/71090 · Cited by 426
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
Cited by
Sorted by citations
Posttranscriptional Control of T Cell Effector Function by Aerobic Glycolysis
Chang, C.-H., Curtis, J. D., Maggi, L. B., Faubert, B., Villarino, A. V., O’Sullivan, D., Huang, S. C.-C., van der Windt, G. J. W., Blagih, J., Qiu, J., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.016 · Cited by 2,204
A brave new world of RNA-binding proteins
Hentze, M. W., Castello, A., Schwarzl, T., & Preiss, T. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.130 · Cited by 1,821
Fueling Immunity: Insights into Metabolism and Lymphocyte Function
Pearce, E. L., Poffenberger, M. C., Chang, C.-H., & Jones, R. G. (2013) · Science · doi:10.1126/science.1242454 · Cited by 1,363
Brain Glucose Metabolism: Integration of Energetics with Function
Dienel, G. A. (2018) · Physiological Reviews · doi:10.1152/physrev.00062.2017 · Cited by 911
Metabolic Regulation of Epigenetics
Lu, C., & Thompson, C. B. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.06.001 · Cited by 699
Metadata
- Authors
- Tristan, C., Shahani, N., Sedlak, T. W., & Sawa, A.
- Affiliations
- Johns Hopkins University (US)
- Corresponding author
- Sawa, Akira
- Venue
- Cellular Signalling
- Publisher
- Elsevier BV
- Published
- 2011-02
- Volume
- 23
- Issue
- 2
- Pages
- 317-323
- ISSN
- 0898-6568 (ISSN-L)
- 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
- 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
