The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Nuclear Export of NF-ATc Enhanced by Glycogen Synthase Kinase-3
Abstract
The transcription factor NF-AT responds to Ca 2+ -calcineurin signals by translocating to the nucleus, where it participates in the activation of early immune response genes. Calcineurin dephosphorylates conserved serine residues in the amino terminus of NF-AT, resulting in nuclear import. Purification of the NF-AT kinase revealed that it is composed of a priming kinase activity and glycogen synthase kinase-3 (GSK-3). GSK-3 phosphorylates conserved serines necessary for nuclear export, promotes nuclear exit, and thereby opposes Ca 2+ -calcineurin signaling. Because GSK-3 responds to signals initiated by Wnt and other ligands, NF-AT family members could be effectors of these pathways.
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.
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
Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
Cross, D. A. E., Alessi, D. R., Cohen, P., Andjelkovich, M., & Hemmings, B. A. (1995) · Nature · doi:10.1038/378785a0 · Cited by 5,244
Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes
Liu, J., Farmer, J. D., Lane, W. S., Friedman, J., Weissman, I., & Schreiber, S. L. (1991) · Cell · doi:10.1016/0092-8674(91)90124-h · Cited by 4,116
Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells
Stambolic, V., Ruel, L., & Woodgett, J. R. (1996) · Current Biology · doi:10.1016/s0960-9822(02)70790-2 · Cited by 1,321
Cited by
Smith-Garvin, J. E., Koretzky, G. A., & Jordan, M. S. (2009) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132706 · Cited by 2,144
Glycogen synthase kinase-3β regulates cyclin D1 proteolysis and subcellular localization
Diehl, J. A., Cheng, M., Roussel, M. F., & Sherr, C. J. (1998) · Genes & Development · doi:10.1101/gad.12.22.3499 · Cited by 2,130
GSK-3: tricks of the trade for a multi-tasking kinase
Doble, B. W., & Woodgett, J. R. (2003) · Journal of Cell Science · doi:10.1242/jcs.00384 · Cited by 2,084
Transcriptional regulation by calcium, calcineurin, and NFAT
Hogan, P. G., Chen, L., Nardone, J., & Rao, A. (2003) · Genes & Development · doi:10.1101/gad.1102703 · Cited by 1,991
Zhou, B. P., Deng, J., Xia, W., Xu, J., Li, Y. M., Gunduz, M., & Hung, M.-C. (2004) · Nature Cell Biology · doi:10.1038/ncb1173 · Cited by 1,581
Crabtree, G. R., & Olson, E. N. (2002) · Cell · doi:10.1016/s0092-8674(02)00699-2 · Cited by 1,323
Self-citationGSK3 takes centre stage more than 20 years after its discovery
FRAME, S., & COHEN, P. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3590001 · Cited by 1,433
Skeletal muscle hypertrophy and atrophy signaling pathways
Glass, D. J. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.04.018 · Cited by 1,106
CD28-mediated co-stimulation: a quantitative support for TCR signalling.
Acuto, O., & Michel, F. (2003) · Nature Reviews Immunology · doi:10.1038/nri1248 · Cited by 775
NFAT dysregulation by increased dosage of DSCR1 and DYRK1A on chromosome 21
Arron, J. R., Winslow, M. M., Polleri, A., Chang, C.-P., Wu, H., Gao, X., Neilson, J. R., Chen, L., Heit, J. J., Kim, S. K., et al. (2006) · Nature · doi:10.1038/nature04678 · Cited by 698
Self-citationBentzinger, C. F., Romanino, K., Cloëtta, D., Lin, S., Mascarenhas, J. B., Oliveri, F., Xia, J., Casanova, E., Costa, C. F., Brink, M., et al. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2008.10.002 · Cited by 640
Regulation of NFATc1 in Osteoclast Differentiation
Kim, J. H., & Kim, N. (2014) · Journal of Bone Metabolism · doi:10.11005/jbm.2014.21.4.233 · Cited by 570
“Several kinases such as glycogen synthase kinase 3 (GSK3), casein kinase 1 (CK1), p38, and JNK phosphorylate the various serine-rich motifs in NFAT proteins, thereby preventing translocation into the nucleus or promoting nuclear export of NFAT proteins.[59-63] A recent study has reported that the ectopic expression of…”
BackgroundGraef, I. A., Wang, F., Charron, F., Chen, L., Neilson, J., Tessier-Lavigne, M., & Crabtree, G. R. (2003) · Cell · doi:10.1016/s0092-8674(03)00390-8 · Cited by 379
Self-citationNuclear Accumulation of NFAT4 Opposed by the JNK Signal Transduction Pathway
Chow, C.-W., Rincón, M., Cavanagh, J., Dickens, M., & Davis, R. J. (1997) · Science · doi:10.1126/science.278.5343.1638 · Cited by 357
Calcineurin signaling in Saccharomyces cerevisiae: how yeast go crazy in response to stress.
Cyert, M. S. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01552-3 · Cited by 333
The Wnt/calcium pathway activates NF-AT and promotes ventral cell fate in Xenopus embryos
Saneyoshi, T., Kume, S., Amasaki, Y., & Mikoshiba, K. (2002) · Nature · doi:10.1038/417295a · Cited by 322
Signaling pathways in Th2 development
Mowen, K. A., & Glimcher, L. H. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.00209.x · Cited by 255
Calcineurin: Structure, function, and inhibition
Hemenway, C. S., & Heitman, J. (1999) · Cell Biochemistry and Biophysics · doi:10.1007/bf02737887 · Cited by 227
Lochhead, P. A., Coghlan, M., Rice, S. Q. J., & Sutherland, C. (2001) · Diabetes · doi:10.2337/diabetes.50.5.937 · Cited by 219
NFAT control of immune function: New Frontiers for an Abiding Trooper
Vaeth, M., & Feske, S. (2018) · F1000Research · doi:10.12688/f1000research.13426.1 · Cited by 191
Increasingly complex: New players enter the Wnt signaling network
Pandur, P., Maurus, D., & Kühl, M. (2002) · BioEssays · doi:10.1002/bies.10164 · Cited by 188
Calcium signaling in vertebrate embryonic patterning and morphogenesis
Slusarski, D. C., & Pelegri, F. (2007) · Developmental Biology · doi:10.1016/j.ydbio.2007.04.043 · Cited by 178
Basheer, N., Smolek, T., Hassan, I., Liu, F., Iqbal, K., Zilka, N., & Novak, P. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02113-z · Cited by 159
Neurogenesis impairment: An early developmental defect in Down syndrome
Stagni, F., Giacomini, A., Emili, M., Guidi, S., & Bartesaghi, R. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.07.026 · Cited by 120
Active Akt signaling triggers CLL toward Richter transformation via overactivation of Notch1
Kohlhaas, V., Blakemore, S. J., Al-Maarri, M., Nickel, N., Pal, M., Roth, A., Hövelmeyer, N., Schäfer, S. C., Knittel, G., Lohneis, P., et al. (2021) · Blood · doi:10.1182/blood.2020005734 · Cited by 87
RSK2 mediates muscle cell differentiation through regulation of NFAT3
Cho, Y.-Y., Yao, K., Bode, A. M., Bergen, H. R., Madden, B. J., Oh, S.-M., Ermakova, S., Kang, B. S., Choi, H. S., Shim, J.-H., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m611322200 · Cited by 85
β-Catenin/TCF-1 Pathway in T Cell Development and Differentiation
Ma, J., Wang, R., Fang, X., & Sun, Z. (2012) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-012-9367-y · Cited by 83
Tsika, R. W., Schramm, C., Simmer, G., Fitzsimons, D. P., Moss, R. L., & Ji, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807461200 · Cited by 65
Porciello, N., & Tuosto, L. (2016) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2016.02.004 · Cited by 61
Calcineurin phosphatase in signal transduction: lessons from fission yeast
Sugiura, R., Sio, S. O., Shuntoh, H., & Kuno, T. (2002) · Genes to Cells · doi:10.1046/j.1365-2443.2002.00557.x · Cited by 58
Liu, W., Youn, H.-D., Zhou, X. Z., Lu, K. P., & Liu, J. O. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02411-5 · Cited by 52
Zawawi, M. S. F., Dharmapatni, A. A. S. S. K., Cantley, M. D., McHugh, K. P., Haynes, D. R., & Crotti, T. N. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.09.077 · Cited by 29
Metadata
- Authors
- Beals, C. R., Sheridan, C. M., Turck, C. W., Gardner, P., & Crabtree, G. R.
- Venue
- Science
- Published
- 1997-03-28
- Volume
- 275
- Issue
- 5308
- Pages
- 1930-1933
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2039842713
- Cited by
- 754
- References
- 3
- FWCI
- 12.15
- Type
- journal article
- Language
- en
- Open access
- closed
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
