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GSK3 takes centre stage more than 20 years after its discovery
Open accessAbstract
Identified originally as a regulator of glycogen metabolism, glycogen synthase kinase-3 (GSK3) is now a well-established component of the Wnt signalling pathway, which is essential for setting up the entire body pattern during embryonic development. It may also play important roles in protein synthesis, cell proliferation, cell differentiation, microtubule dynamics and cell motility by phosphorylating initiation factors, components of the cell-division cycle, transcription factors and proteins involved in microtubule function and cell adhesion. Generation of the mouse knockout of GSK3β, as well as studies in neurons, also suggest an important role in apoptosis. The substrate specificity of GSK3 is unusual in that efficient phosphorylation of many of its substrates requires the presence of another phosphorylated residue optimally located four amino acids C-terminal to the site of GSK3 phosphorylation. Recent experiments, including the elucidation of its three-dimensional structure, have enhanced our understanding of the molecular basis for the unique substrate specificity of GSK3. Insulin and growth factors inhibit GSK3 by triggering its phosphorylation, turning the N-terminus into a pseudosubstrate inhibitor that competes for binding with the ‘priming phosphate’ of substrates. In contrast, Wnt proteins inhibit GSK3 in a completely different way, by disrupting a multiprotein complex comprising GSK3 and its substrates in the Wnt signalling pathway, which do not appear to require a ‘priming phosphate’. These latest findings have generated an enormous amount of interest in the development of drugs that inhibit GSK3 and which may have therapeutic potential for the treatment of diabetes, stroke and Alzheimer's disease.
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Glycogen synthase is the key insulin-regulated enzyme controlling the rate of muscle glycogen synthesis.
“Glycogen synthase is the key insulin-regulated enzyme that controls the rate of muscle glycogen synthesis [148, 150, 200, 212–214].”
From Pathogenesis of insulin resistance in skeletal muscle (2010) · cites this paper as [213]
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2 retracted
Prevention of Chemotherapy-Induced Alopecia in Rats by CDK Inhibitors
Davis, S. T., Benson, B. G., Bramson, H. N., Chapman, D. E., Dickerson, S. H., Dold, K. M., Eberwein, D. J., EDELSTEIN, M. P., Frye, S. V., Gampe, R. T., et al. (2001) · Science · doi:10.1126/science.291.5501.134 · Cited by 166
RetractedRuel, L., Stambolic, V., Ali, A., Manoukian, A. S., & Woodgett, J. R. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.31.21790 · Cited by 84
RetractedAmyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
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
Self-citationSpecificity and mechanism of action of some commonly used protein kinase inhibitors
DAVIES, S. P., Reddy, H., Caivano, M., & Cohen, P. (2000) · Biochemical Journal · doi:10.1042/0264-6021:3510095 · Cited by 4,366
Self-citationPolakis, P. (2000) · Genes & Development · doi:10.1101/gad.14.15.1837 · Cited by 3,183
β‐catenin is a target for the ubiquitin–proteasome pathway
Aberle, H., Bauer, A., Stappert, J., Kispert, A., & Kemler, R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.13.3797 · Cited by 2,586
Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480
The cyclin D1 gene is a target of the β-catenin/LEF-1 pathway
Shtutman, M., Zhurinsky, J., Simcha, I., Albanese, C., D’Amico, M., Pestell, R., & Ben-Ze’ev, A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5522 · Cited by 2,230
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
Apoptosis in neurodegenerative disorders
Mattson, M. P. (2000) · Nature Reviews Molecular Cell Biology · doi:10.1038/35040009 · Cited by 1,605
Linking Colorectal Cancer to Wnt Signaling
Bienz, M., & Clevers, H. C. (2000) · Cell · doi:10.1016/s0092-8674(00)00122-7 · Cited by 1,518
Binding of GSK3β to the APC-β-Catenin Complex and Regulation of Complex Assembly
Rubinfeld, B., Albert, I., Porfiri, E., Fiol, C. J., Munemitsu, S. M., & Polakis, P. G. (1996) · Science · doi:10.1126/science.272.5264.1023 · Cited by 1,420
Multiple Ras-dependent phosphorylation pathways regulate Myc protein stabilityPreprint
Sears, R. C., Nuckolls, F., Haura, E. B., Taya, Y., Tamai, K., & Nevins, J. R. (2000) · Genes & Development · doi:10.1101/gad.836800 · Cited by 1,411
Requirement for glycogen synthase kinase-3β in cell survival and NF-κB activation
Hoeflich, K. P., Luo, J., Rubie, E. A., Tsao, M., Jin, O., & Woodgett, J. R. (2000) · Nature · doi:10.1038/35017574 · Cited by 1,401
Molecular cloning and expression of glycogen synthase kinase‐3/factor A.
Woodgett, J. R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07419.x · Cited by 1,362
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
Functional Interaction of an Axin Homolog, Conductin, with β-Catenin, APC, and GSK3β
Behrens, J., Jerchow, B., Würtele, M., Grimm, J., Asbrand, C., Wirtz, R. M., Kühl, M., Wedlich, D., & Birchmeier, W. (1998) · Science · doi:10.1126/science.280.5363.596 · Cited by 1,255
Ikeda, S., Kishida, S., Yamamoto, H., Murai, H., Koyama, S., & Kikuchi, A. (1998) · The EMBO Journal · doi:10.1093/emboj/17.5.1371 · Cited by 1,248
Intestinal polyposis in mice with a dominant stable mutation of the β‐catenin gene
Harada, N., Tamai, Y., Ishikawa, T., Sauer, B., Takaku, K., Oshima, M., & Taketo, M. M. (1999) · The EMBO Journal · doi:10.1093/emboj/18.21.5931 · Cited by 1,212
Role of Glycogen Synthase Kinase-3 in the Phosphatidylinositol 3-Kinase/Akt Cell Survival Pathway
Pap, M., & Cooper, G. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.19929 · Cited by 1,046
Boyle, W. J., Smeal, T., Defize, L. H. K., Angel, P. E., Woodgett, J. R., Karin, M., & Hunter, T. R. (1991) · Cell · doi:10.1016/0092-8674(91)90241-p · Cited by 1,039
Deák, M., Clifton, A. D., Lucocq, J. M., & Alessi, D. R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.15.4426 · Cited by 1,004
DasGupta, R., & Fuchs, E. V. (1999) · Development · doi:10.1242/dev.126.20.4557 · Cited by 995
Embi, N., Rylatt, D. B., & Cohen, P. (1980) · PubMed · Cited by 911
Self-citationCoghlan, M. P., Culbert, A. A., Cross, D. A. E., Corcoran, S. L., Yates, J. W., Pearce, N. J., Rausch, O., Murphy, G. J., Carter, P. S., Cox, L. R., et al. (2000) · Chemistry & Biology · doi:10.1016/s1074-5521(00)00025-9 · Cited by 906
Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90057-x · Cited by 903
Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A
Fang, X., Yu, S. X., Lu, Y., Bast, R. C., Woodgett, J. R., & Mills, G. B. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220413597 · Cited by 852
Hart, M. J., Santos, R. D. L., Albert, I., Rubinfeld, B., & Polakis, P. G. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70226-x · Cited by 850
Nuclear Export of NF-ATc Enhanced by Glycogen Synthase Kinase-3
Beals, C. R., Sheridan, C. M., Turck, C. W., Gardner, P. I., & Crabtree, G. R. (1997) · Science · doi:10.1126/science.275.5308.1930 · Cited by 759
Hanger, D. P., Hughes, K., Woodgett, J. R., Brion, J.-P., & Anderton, B. H. (1992) · Neuroscience Letters · doi:10.1016/0304-3940(92)90774-2 · Cited by 737
Leclerc, S., Garnier, M., Hoessel, R., Marko, D., Bibb, J. A., Snyder, G. L., Greengard, P., Biernat, J., Wu, Y., Mandelkow, E., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m002466200 · Cited by 736
Frame, S., Cohen, P., & Biondi, R. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00253-2 · Cited by 724
Self-citationControl of p70 S6 kinase by kinase activity of FRAP in vivo
Brown, E. J., Beal, P. A., Keith, C. T., Chen, J., Shin, T. B., & Schreiber, S. L. (1995) · Nature · doi:10.1038/377441a0 · Cited by 705
Crystal Structure of Glycogen Synthase Kinase 3β
Dajani, R., Fraser, E., Roe, S. M., Young, N., Good, V. M., Dale, T. C., & Pearl, L. H. (2001) · Cell · doi:10.1016/s0092-8674(01)00374-9 · Cited by 680
Hart, M. J., Concordet, J., Lassot, I., Albert, I., Santos, R., Durand, H., Perret, C., Rubinfeld, B., Margottin-Goguet, F., Bénarous, R., et al. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80091-8 · Cited by 670
Activation of the Wnt Signaling Pathway: A Molecular Mechanism for Lithium Action
Hedgepeth, C. M., Conrad, L. J., Zhang, J., Huang, H., Lee, V. M.-Y., & Klein, P. S. (1997) · Developmental Biology · doi:10.1006/dbio.1997.8552 · Cited by 644
Modulation of the glycogen synthase kinase‐3 family by tyrosine phosphorylation.
Hughes, K., Nikolakaki, E., Plyte, S. E., Totty, N. F., & Woodgett, J. R. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05715.x · Cited by 630
Matsuzawa, S.-I., & Reed, J. C. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00242-8 · Cited by 587
Alt, J. R., Cleveland, J. L., Hannink, M., & Diehl, J. A. (2000) · Genes & Development · doi:10.1101/gad.854900 · Cited by 535
Glycogen synthase kinase‐3 and the Alzheimer‐like state of microtubule‐associated protein tau
Mandelkow, E.-M., Drewes, G., Biernat, J., Gustke, N., Van Lint, J., Vandenheede, J. R., & Mandelkow, E. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81496-9 · Cited by 515
Kishida, S., Yamamoto, H., Ikeda, S., Kishida, M., Sakamoto, I., Koyama, S., & Kikuchi, A. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.18.10823 · Cited by 491
Glycogen synthase kinase-3 and dorsoventral patterning in Xenopus embryos
He, X., Saint‐Jeannet, J., Woodgett, J. R., VARMUS, H. E., & Dawid, I. B. (1995) · Nature · doi:10.1038/374617a0 · Cited by 484
Cross, D. A. E., Alessi, D. R., Vandenheede, J. R., McDowell, H. E., Hundal, H. S., & Cohen, P. (1994) · Biochemical Journal · doi:10.1042/bj3030021 · Cited by 480
Self-citationWilliams, M. R., Arthur, J. S. C., Balendran, A., KAAY, J. V. D., Poli, V., Cohen, P., & Alessi, D. R. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00441-3 · Cited by 479
Self-citationRas Enhances Myc Protein Stability
Sears, R. C., Leone, G. W., DeGregori, J. V., & Nevins, J. R. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80308-1 · Cited by 463
Casein kinase I transduces Wnt signals
Peters, J. M., McKay, R. M., McKay, J. P., & Graff, J. M. (1999) · Nature · doi:10.1038/43830 · Cited by 447
Role of Glycogen Synthase Kinase-3β in Neuronal Apoptosis Induced by Trophic Withdrawal
Hetman, M., Cavanaugh, J. E., Kimelman, D., & Xia, Z. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-07-02567.2000 · Cited by 442
Zumbrunn, J., Kinoshita, K., Hyman, A. A., & Näthke, I. S. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00002-1 · Cited by 438
Cell adhesion and the integrin-linked kinase regulate the LEF-1 and β-catenin signaling pathways
Novak, A., Hsu, S.-C., Leung-Hagesteijn, C., Radeva, G., Papkoff, J., Montesano, R., Roskelley, C. D., Grosschedl, R., & Dedhar, S. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.8.4374 · Cited by 434
Differential Regulation of Glycogen Synthase Kinase 3β by Insulin and Wnt Signaling
Ding, V. W., Chen, R., & McCormick, F. P. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005342200 · Cited by 429
Siegfried, E., Chou, T.-B., & Perrimon, N. (1992) · Cell · doi:10.1016/s0092-8674(05)80065-0 · Cited by 423
Liu, J., Stevens, J., Rote, C. A., Yost, H. J., Hu, Y., Neufeld, K. L., White, R. L., & Matsunami, N. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00241-6 · Cited by 422
Axin and Frat1 interact with Dvl and GSK, bridging Dvl to GSK in Wnt‐mediated regulation of LEF‐1
Li, L., Yuan, H., Weaver, C. D., Mao, J., Farr, G. H., Sussman, D. J., Jonkers, J., Kimelman, D., & Wu, D. (1999) · The EMBO Journal · doi:10.1093/emboj/18.15.4233 · Cited by 403
Welsh, G. I., & Proud, C. G. (1993) · Biochemical Journal · doi:10.1042/bj2940625 · Cited by 397
WNT-1 Signaling Inhibits Apoptosis by Activating β-Catenin/T Cell Factor–Mediated Transcription
Chen, S., Guttridge, D. C., You, Z., Zhang, Z., Fribley, A. M., Mayo, M. W., Kitajewski, J., & Wang, C. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.152.1.87 · Cited by 397
Structure of GSK3beta reveals a primed phosphorylation mechanism.
ter Haar, E., Coll, J. T., Austen, D. A., Hsiao, H.-M., Swenson, L. L., & Jain, J. (2001) · Nature Structural Biology · doi:10.1038/89624 · Cited by 394
Chu, B., Soncin, F., Price, B. D., Stevenson, M. A., & Calderwood, S. K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30847 · Cited by 382
Bhat, R. V., Shanley, J. R., Correll, M. P., Fieles, W. E., Keith, R. A., Scott, C. W., & Lee, C. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.190297597 · Cited by 379
Cross, D. A. E., Culbert, A. A., Chalmers, K. A., Facci, L., Skaper, S. D., & Reith, A. D. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.t01-1-00251.x · Cited by 376
Fiol, C. J., Mahrenholz, A. M., Wang, Y., Roeske, R. W., & Roach, P. J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47901-x · Cited by 367
Estrogen induction of the cyclin D1 promoter: Involvement of a cAMP response-like element
Sabbah, M., Courilleau, D., Mešter, J., & Redeuilh, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11217 · Cited by 367
Yamamoto, H., Kishida, S., Kishida, M., Ikeda, S., Takada, S., & Kikuchi, A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.10681 · Cited by 364
Cyclic AMP Promotes Neuronal Survival by Phosphorylation of Glycogen Synthase Kinase 3β
Li, M., Wang, X., Meintzer, M. K., Laessig, T. A., Birnbaum, M. J., & Heidenreich, K. A. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.24.9356-9363.2000 · Cited by 362
Woods, Y. L., Cohen, P., Becker, W. B., Jakes, R., Goedert, M., Wang, X., & Proud, C. G. (2001) · Biochemical Journal · doi:10.1042/bj3550609 · Cited by 343
Self-citationOrsulic, S., & Peifer, M. (1996) · Journal of Cell Biology · doi:10.1083/jcb.134.5.1283 · Cited by 342
Lithium inhibits Alzheimer's disease‐like tau protein phosphorylation in neurons
Muñoz-Montaño, J. R., Moreno, F. J., Ávila, J., & Díaz‐Nido, J. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00688-1 · Cited by 322
Desbois-Mouthon, C., Cadoret, A., Blivet-Van Eggelpoël, M.-J., Bertrand, F., Cherqui, G., Perret, C., & Capeau, J. (2001) · Oncogene · doi:10.1038/sj.onc.1204064 · Cited by 321
Phosphorylation of insulin receptor substrate 1 by glycogen synthase kinase 3 impairs insulin action
Eldar-Finkelman, H., & Krebs, E. G. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9660 · Cited by 319
Fagotto, F., Funayama, N., Glück, U., & Gumbiner, B. M. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.132.6.1105 · Cited by 317
Dominguez, I. M., Itoh, K., & Sokol, S. Y. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8498 · Cited by 316
Eyers, P. A., Craxton, M., Morricel, N., Cohen, P., & Goedert, M. (1998) · Chemistry & Biology · doi:10.1016/s1074-5521(98)90170-3 · Cited by 310
Self-citationLucas, F. R., Goold, R., Gordon‐Weeks, P. R., & Salinas, P. C. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.10.1351 · Cited by 307
Glycogen Synthase Kinase-3β Facilitates Staurosporine- and Heat Shock-induced Apoptosis
Bijur, G. N., Sarno, P. D., & Jope, R. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7583 · Cited by 301
Welsh, G. I., Miller, C. M., Loughlin, A. J., & Price, N. T. (1998) · FEBS Letters · doi:10.1016/s0014-5793(97)01548-2 · Cited by 298
Parker, P. J., Caudwell, F. B., & Cohen, P. (1983) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1983.tb07140.x · Cited by 298
Self-citationBhatia, K., Huppi, K. E., Spangler, G., Siwarski, D. F., Iyer, R., & Magrath, I. T. (1993) · Nature Genetics · doi:10.1038/ng0993-56 · Cited by 285
Rimm, D. L., Caca, K., Hu, G., Harrison, F. B., & Fearon, E. R. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65278-9 · Cited by 283
Playford, M. P., Bicknell, D., Bodmer, W. F., & Macaulay, V. M. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.210394297 · Cited by 281
Goold, R., Owen, R., & Gordon‐Weeks, P. R. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.19.3373 · Cited by 281
Fiol, C. J., Williams, J. S., Chou, C. H., Wang, Q. M., Roach, P. J., & ANDRISANI, O. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31619-3 · Cited by 279
Orford, K. W., Orford, C. C., & Byers, S. W. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.4.855 · Cited by 276
Park, D. S., Morris, E. J., Greene, L. A., & Geller, H. M. (1997) · Journal of Neuroscience · doi:10.1523/jneurosci.17-04-01256.1997 · Cited by 270
Biochemical interactions in the wnt pathway
Seidensticker, M. J., & Behrens, J. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(99)00158-5 · Cited by 260
Itoh, K., Krupnik, V. E., & Sokol, S. Y. (1998) · Current Biology · doi:10.1016/s0960-9822(98)70229-5 · Cited by 257
Increased glycogen synthase kinase-3 activity in diabetes- and obesity-prone C57BL/6J mice.
Eldar-Finkelman, H., Schreyer, S. A., Shinohara, M. M., LeBoeuf, R. C., & Krebs, E. G. (1999) · Diabetes · doi:10.2337/diabetes.48.8.1662 · Cited by 252
Casein kinase 2 associates with and phosphorylates Dishevelled
Willert, K., Brink, M., Wodarz, A., Varmus, H., & Nusse, R. (1997) · The EMBO Journal · doi:10.1093/emboj/16.11.3089 · Cited by 249
Lithium-induced respecification of pattern in Xenopus laevis embryos
Kao, K. R., Masui, Y., & Elinson, R. P. (1986) · Nature · doi:10.1038/322371a0 · Cited by 248
PDK1, one of the missing links in insulin signal transduction?1
Cohen, P., Alessi, D. R., & Cross, D. A. E. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00490-0 · Cited by 246
Self-citationLi, Y., Bharti, A. K., Chen, D., Gong, J., & Kufe, D. W. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.12.7216 · Cited by 241
Zhu, A. J., & Watt, F. M. (1999) · Development · doi:10.1242/dev.126.10.2285 · Cited by 240
Yoshida, H., & Ihara, Y. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03642.x · Cited by 236
Thomas, G. M., Frame, S., Goedert, M., Näthke, I. S., Polakis, P. G., & Cohen, P. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01161-8 · Cited by 234
Self-citationShaw, M., Cohen, P., & Alessi, D. R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)01235-0 · Cited by 231
Self-citationSite-specific modulation of c-Myc cotransformation by residues phosphorylated in vivo.
Pulverer, B., Fisher, C., Vousden, K. H., Littlewood, T. D., Evan, G. I., & Woodgett, J. R. (1994) · PubMed · Cited by 228
Regulation of Spemann organizer formation by the intracellular kinase Xgsk-3
Pierce, S. B., & Kimelman, D. (1995) · Development · doi:10.1242/dev.121.3.755 · Cited by 227
Cross, D. A. E., Watt, P., Shaw, M., KAAY, J. V. D., Downes, C. P., Holder, J. C., & Cohen, P. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00240-8 · Cited by 221
Self-citationLochhead, P. A., Coghlan, M., Rice, S. Q. J., & Sutherland, C. (2001) · Diabetes · doi:10.2337/diabetes.50.5.937 · Cited by 219
The Role of Glycogen Synthase Kinase 3β in Insulin-stimulated Glucose Metabolism
Summers, S. A., Kao, A. W., Kohn, A. D., Backus, G. S., Roth, R. A., Pessin, J. E., & Birnbaum, M. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17934 · Cited by 218
GSK3, a master switch regulating cell-fate specification and tumorigenesis
Kim, L., & Kimmel, A. R. (2000) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00120-9 · Cited by 218
Multisite phosphorylation of glycogen synthase
Woodgett, J. R., & Cohen, P. (1984) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(84)90047-5 · Cited by 216
Self-citationCasein kinase Iɛ in the Wnt pathway: Regulation of β-catenin function
Sakanaka, C., Leong, P. C., Xu, L., Harrison, S. D., & Williams, L. T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.22.12548 · Cited by 213
Ruel, L., Bourouis, M., Heitzler, P., Pantesco, V., & Simpson, P. (1993) · Nature · doi:10.1038/362557a0 · Cited by 202
Li, J., DeFea, K., & Roth, R. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9351 · Cited by 196
New approaches in the treatment of type 2 diabetes
Zhang, B. B., & Moller, D. E. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00103-4 · Cited by 196
Glycogen Synthase Kinase 3 Is an Insulin-Regulated C/EBPα Kinase
Ross, S. E., Erickson, R. L., Hemati, N., & MacDougald, O. A. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.12.8433 · Cited by 193
MSK1 is required for CREB phosphorylation in response to mitogens in mouse embryonic stem cells
Arthur, J. S. C., & Cohen, P. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02031-7 · Cited by 191
Self-citationNewgard, C. B., Brady, M. J., O'Doherty, R. M., & Saltiel, A. R. (2000) · Diabetes · doi:10.2337/diabetes.49.12.1967 · Cited by 189
Nikolakaki, E., Coffer, P. J., Hemelsoet, R., Woodgett, J. R., & Defize, L. H. K. (1993) · PubMed · Cited by 188
The development and therapeutic potential of protein kinase inhibitors.
Cohen, P. R. (1999) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)80067-2 · Cited by 178
Self-citationShimamura, K., Hirano, S., McMahon, A. P., & Takeichi, M. (1994) · Development · doi:10.1242/dev.120.8.2225 · Cited by 176
Chu, B., Zhong, R., Soncin, F., Stevenson, M. A., & Calderwood, S. K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.29.18640 · Cited by 170
Takeda, K. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.1.125 · Cited by 168
Glycogen Synthase Kinase-3 Inhibits the DNA Binding Activity of NFATc
Neal, J. W., & Clipstone, N. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004888200 · Cited by 167
Curbing the nuclear activities of β‐catenin
Hecht, A., & Kemler, R. (2000) · EMBO Reports · doi:10.1093/embo-reports/kvd012 · Cited by 163
Interaction among Gsk-3, Gbp, Axin, and APC in Xenopus Axis Specification
Farr, G. H., Ferkey, D. M., Yost, C., Pierce, S. B., Weaver, C. I., & Kimelman, D. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.4.691 · Cited by 161
The Novel Tyrosine Kinase ZAK1 Activates GSK3 to Direct Cell Fate Specification
Kim, L., Liu, J., & Kimmel, A. R. (1999) · Cell · doi:10.1016/s0092-8674(00)81526-3 · Cited by 161
Suzuki, Y., Lannér, C., Kim, J., Vilardo, P. G., Zhang, H., Yang, J., Cooper, L. D., Steele, M., Kennedy, A., Bock, C. B., et al. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.8.2683-2694.2001 · Cited by 160
Xavier, I. J., Mercier, P. A., McLoughlin, C., Ali, A., Woodgett, J. R., & Ovsenek, N. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002169200 · Cited by 155
A Versatile Transcriptional Effector of Wingless Signaling
Nusse, R. (1997) · Cell · doi:10.1016/s0092-8674(00)80210-x · Cited by 151
Hartigan, J. A., & Johnson, G. V. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.21395 · Cited by 141
[48] cDNA cloning and properties of glycogen synthase kinase-3
Robertwoodgett, J. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)00172-s · Cited by 132
de Groot, R. P., Auwerx, J. H., Bourouis, M., & Sassone‐Corsi, P. (1993) · PubMed · Cited by 128
Activation of a novel proto‐oncogene, Frat1, contributes to progression of mouse T‐cell lymphomas
Jonkers, J., Korswagen, H. C., Acton, D., Breuer, M. L., & Berns, A. J. M. (1997) · The EMBO Journal · doi:10.1093/emboj/16.3.441 · Cited by 126
Regulation of Glycogen Synthesis by Amino Acids in Cultured Human Muscle Cells
Armstrong, J. L., Bonavaud, S. M., Toole, B. J., & Yeaman, S. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m004812200 · Cited by 123
Hughes, K., Ramakrishna, S., Benjamin, W. B., & Woodgett, J. R. (1992) · Biochemical Journal · doi:10.1042/bj2880309 · Cited by 113
Orena, S., Torchia, A. J., & Garofalo, R. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m910002199 · Cited by 111
Piwien‐Pilipuk, G., Mater, D. V., Ross, S. E., MacDougald, O. A., & Schwartz, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010193200 · Cited by 104
Glycogen Synthase Kinase-3β Regulates Presenilin 1 C-terminal Fragment Levels
Kirschenbaum, F., Hsu, S.-C., Cordell, B., & McCarthy, J. V. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102849200 · Cited by 100
Wnt signalling: pathway or network?
Arias, A. M., Browntand, A. M., & Brennan, K. R. (1999) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(99)80068-9 · Cited by 97
Jho, E., Lomvardas, S., & Costantini, F. D. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1760 · Cited by 95
Ashcroft, M. A., Stephens, R. M., Hallberg, B., Downward, J., & Kaplan, D. R. (1999) · Oncogene · doi:10.1038/sj.onc.1202814 · Cited by 90
Shaw, M., & Cohen, P. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01434-9 · Cited by 87
Self-citationCommon Pathway for the Ubiquitination of IκBα, IκBβ, and IκBε Mediated by the F-Box Protein FWD1
Shirane, M., Hatakeyama, S., Hattori, K., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.40.28169 · Cited by 86
The significance of tau and α-synuclein inclusions in neurodegenerative diseases
Goedert, M. (2001) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00200-8 · Cited by 86
Shao, J., Sheng, H., DuBois, R. N., & Beauchamp, R. D. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002235200 · Cited by 81
Modulation of Wnt signaling by Axin and Axil
Kikuchi, A. (1999) · Cytokine & Growth Factor Reviews · doi:10.1016/s1359-6101(99)00017-9 · Cited by 79
Palmieri, S., Kahn, P., & Graf, T. (1983) · The EMBO Journal · doi:10.1002/j.1460-2075.1983.tb01750.x · Cited by 78
Mutations in the coding region of c-MYC in AIDS-associated and other aggressive lymphomas.
Clark, H. M., Yano, T., Otsuki, T., et al. (1994) · PubMed · Cited by 72
Maas, J. W., Horstmann, S., Borasio, G. D., et al. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.70041401.x · Cited by 55
Sequence curiosity in v-myc oncogene
Papas, T. S., & Lautenberger, J. A. (1985) · Nature · doi:10.1038/318237a0 · Cited by 54
Freeman, M., & Bienz, M. (2001) · EMBO Reports · doi:10.1093/embo-reports/kve019 · Cited by 52
Walker, K. S., Watt, P., & Cohen, P. (2000) · FEBS Letters · doi:10.1016/s0014-5793(99)01771-8 · Cited by 47
Self-citationHow does insulin stimulate glycogen synthesis?
Cohen, P., Nimmo, H. G., & Proud, C. G. (1978) · PubMed · Cited by 46
Self-citationTurner, N. C., & Clapham, J. C. (1998) · Birkhäuser Basel eBooks · doi:10.1007/978-3-0348-8845-5_2 · Cited by 46
Benjamin, W. B., Pentyala, S., Woodgett, J. R., Hod, Y., & Marshak, D. R. (1994) · Biochemical Journal · doi:10.1042/bj3000477 · Cited by 38
Markus, M. A., Kahle, P. J., Winkler, A., Horstmann, S., Anneser, J. M. H., & Borasio, G. D. (1997) · Neurobiology of Disease · doi:10.1006/nbdi.1997.0140 · Cited by 29
Chen, X., McMahon, E. G., & Gulve, E. A. (1998) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.1998.275.2.e272 · Cited by 28
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Taniguchi, C. M., Emanuelli, B., & Kahn, C. R. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1837 · Cited by 2,760
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Day, T. F., Guo, X., Garrett-Beal, L., & Yang, Y. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.03.016 · Cited by 1,616
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DeFronzo, R. A. (2004) · Medical Clinics of North America · doi:10.1016/j.mcna.2004.04.013 · Cited by 1,342
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Pearce, L. R., Komander, D., & Alessi, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2822 · Cited by 1,294
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Metadata
- Authors
- FRAME, S., & COHEN, P.
- Affiliations
- University of Dundee (GB)
- Corresponding author
- FRAME, Sheelagh
- COHEN, Philip
- ORCID
- COHEN, Philip
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2001-09-24
- Volume
- 359
- Issue
- 1
- Pages
- 1-16
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- PMC
- PMC1222116
- OpenAlex
- W1964631519
- Cited by
- 1,433
- References
- 148
- Citations by year
- 2026: 13 · 2025: 29 · 2024: 22 · 2023: 32 · 2022: 37 · 2021: 24 · 2020: 38 · 2019: 45 · 2018: 46 · 2017: 42 · 2016: 43 · 2015: 47 · 2014: 75 · 2013: 83 · 2012: 86
- FWCI
- 3.99
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Biochemical Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Wnt/β-catenin signaling in development and cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- glycogen synthase kinase-3, GSK3β, Wnt signalling pathway, glycogen metabolism, substrate specificity, protein phosphorylation, apoptosis, growth factor inhibition, GSK-3 inhibitors, Alzheimer's disease, diabetes mellitus, stroke, embryonic development, microtubule dynamics, cell motility
- MeSH terms
- Animals, Humans, Glycogen Synthase Kinase 3
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