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Nuclear localization signal-independent and importin/karyopherin-independent nuclear import of β-catenin
Open accessAbstract
Background Control of the nuclear localization of specific proteins is an important mechanism for regulating many signal transduction pathways. Upon activation of the Wnt signaling pathway, beta-catenin localizes into the nucleus and interacts with TCF/LEF-1 (T-cell factor/lymphocyte enhancer factor-1) transcription factors, triggering activation of downstream genes. The role of regulated nuclear localization in beta-catenin signaling is still unclear. Beta-catenin has no nuclear localization sequence (NLS). Although it has been reported that beta-catenin can piggyback into the nucleus by binding to TCF/LEF-1, there is evidence that its import is independent of TCF/LEF-1 in vivo. Therefore, the mechanism for beta-catenin nuclear localization remains to be established.Results We have analyzed beta-catenin nuclear import in an in vitro assay using permeabilized cells. Beta-catenin docks specifically onto the nuclear envelope in the absence of other cytosolic factors. Docking is not inhibited by an NLS peptide and does not require importins/karyopherins, the receptors for classical NLS substrates. Rather, docking is specifically competed by importin-beta/beta-karyopherin, indicating that beta-catenin and importin-beta/beta-karyopherin both interact with common nuclear pore components. Nuclear translocation of beta-catenin is energy dependent and is inhibited by nonhydrolyzable GTP analogs and by a dominant-negative mutant form of the Ran GTPase. Cytosol preparations contain inhibitory activities for beta-catenin import that are distinct from the competition by importin-beta/beta-karyopherin and may be involved in the physiological regulation of the pathway.Conclusions Beta-catenin is imported into the nucleus by binding directly to the nuclear pore machinery, similar to importin-beta/beta-karyopherin or other importin-beta-like import factors, such as transportin. These findings provide an explanation for how beta-catenin localizes to the nucleus without an NLS and independently of its interaction with TCF/LEF-1. This is a new and unusual mechanism for the nuclear import of a signal transduction protein. The lack of beta-catenin import activity in the presence of normal cytosol suggests that its import may be regulated by upstream events in the Wnt signaling pathway.
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“β-catenin itself has no nuclear localization sequence (NLS), nor does its entry into the nucleus appear to require the function of the importin proteins or the Ran-mediated nuclear import.43”
From Wnt signal transduction pathways (2008) · cites this paper as [43]
Citations
Cites
Functional interaction of β-catenin with the transcription factor LEF-1
Behrens, J., von Kries, J. P., Kühl, M., Bruhn, L., Wedlich, D., Grosschedl, R., & Birchmeier, W. (1996) · Nature · doi:10.1038/382638a0 · Cited by 2,912
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
CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals
Fornerod, M. W. J., Ohno, M., Yoshida, M., & Mattaj, I. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80371-2 · Cited by 2,086
Nuclear targeting sequences — a consensus?
Dingwall, C., & Laskey, R. A. (1991) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(91)90184-w · Cited by 1,871
XTcf-3 Transcription Factor Mediates β-Catenin-Induced Axis Formation in Xenopus Embryos
Molenaar, M., van de Wetering, M., Oosterwegel, M., Peterson-Maduro, J., Godsave, S., Korinek, V., Roose, J., Destrée, O., & Clevers, H. (1996) · Cell · doi:10.1016/s0092-8674(00)80112-9 · Cited by 1,824
Rel/NF-kappa B/I kappa B family: intimate tales of association and dissociation.Preprint
Verma, I. M., Stevenson, J. K., Schwarz, E. M., Antwerp, D. V., & Miyamoto, S. (1995) · Genes & Development · doi:10.1101/gad.9.22.2723 · Cited by 1,696
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
Wetering, M. L. V. D., Cavallo, R. A., Dooijes, D., van Beest, M., van Es, J. V., Loureiro, J., Ypma, A., Hursh, D., Jones, T. L., Bejsovec, A., et al. (1997) · Cell · doi:10.1016/s0092-8674(00)81925-x · Cited by 1,347
Yost, C., Torres, M., Miller, J., Huang, E., Kimelman, D., & Moon, R. T. (1996) · Genes & Development · doi:10.1101/gad.10.12.1443 · Cited by 1,167
Exportin 1 (Crm1p) Is an Essential Nuclear Export Factor
Stade, K., Ford, C. S., Guthrie, C., & Weis, K. (1997) · Cell · doi:10.1016/s0092-8674(00)80370-0 · Cited by 1,145
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Rongish, B. J., & Kinsey, W. H. (2000) · The Anatomical Record · doi:10.1002/1097-0185(20001001)260:2 · Cited by 19
Langer, T. (2000) · Histochemistry and Cell Biology · doi:10.1007/s004180000147 · Cited by 19
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Scully, C. M., Sebastián, J. V. B., Black, M., Carrozzo, M., Eisen, D., Escudier, M., Farthing, P. M., Küffer, R., Muzio, L. L., Mignogna, M. D., et al. (2005) · Oral Diseases · doi:10.1111/j.1601-0825.2004.01078.x · Cited by 18
Yen, Y., Roberts, P. M., & Johnson, R. C. (2001) · Traffic · doi:10.1034/j.1600-0854.2001.20703.x · Cited by 18
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Introducing STRaNDs: shuttling transcriptional regulators that are non-DNA binding
Lu, M. M., Muers, M. R., & Lü, X. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.41 · Cited by 18
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Hwang, W. Y., Kostiuk, V., González, D. P., Lusk, C. P., & Khokha, M. K. (2022) · eLife · doi:10.7554/elife.70495 · Cited by 17
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Lever, M. B., Karpova, A., & Kreutz, M. R. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00033 · Cited by 17
Roles of cytoskeletal and junctional plaque proteins in nuclear signaling
Hubner, S. E., Jans, D. A., & Drenckhahn, D. (2001) · International review of cytology · doi:10.1016/s0074-7696(01)08005-6 · Cited by 17
Baulida, J., Batlle, E., & de Herreros, A. G. (1999) · Biochemical Journal · doi:10.1042/bj3440565 · Cited by 17
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Vuong, L. T., & Mlodzik, M. (2023) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2023.09.002 · Cited by 18
Nucleo-cytoplasmic shuttling of APC can maximize β‐catenin/TCF concentration
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Peluso, J. J., Pappalardo, A., & Hess, S. A. (2000) · Endocrine · doi:10.1385/endo:12:3:295 · Cited by 16
Li, S., Paterno, G. D., & Gillespie, L. L. (2013) · PLoS ONE · doi:10.1371/journal.pone.0084046 · Cited by 15
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Shi, X., Zhao, Y., Ding, C., Wang, Z., Ji, A., Li, Z., Feng, D., Li, Y., Gao, D., Zhou, J., et al. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.04.036 · Cited by 15
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Rudt, F., & Pieler, T. (2001) · European Journal of Cell Biology · doi:10.1078/0171-9335-00212 · Cited by 15
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Mayr, J., Wang, H.-R., Nederlof, P. M., & Baumeister, W. P. (1999) · Biological Chemistry · doi:10.1515/bc.1999.150 · Cited by 14
Edwards, J., Kolman, K., Lamar, P. C., Chandar, N., Fay, M. J., & Prozialeck, W. C. (2012) · BioMetals · doi:10.1007/s10534-012-9592-0 · Cited by 14
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Parker, D. S., Blauwkamp, T. A., & Cadigan, K. M. (2007) · Advances in developmental biology · doi:10.1016/s1574-3349(06)17001-5 · Cited by 14
Steinert, G., Oancea, C., Roos, J., Hagemeyer, H., Maier, T. J., Ruthardt, M., & Puccetti, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022540 · Cited by 13
Custos controls β-catenin to regulate head development during vertebrate embryogenesis
Komiya, Y., Mandrekar, N., Sato, A., Dawid, I. B., & Habas, R. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1414437111 · Cited by 13
Somorjai, I., & Martínez-Arias, A. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002893 · Cited by 13
Epithelial proliferation induces novel changes in APC expression
Umar, S., Wang, Y., & Sellin, J. H. (2005) · Oncogene · doi:10.1038/sj.onc.1208820 · Cited by 12
Self-regulation of functional pathways by motifs inside the disordered tails of beta-catenin
Zhao, B., & Xue, B. (2016) · BMC Genomics · doi:10.1186/s12864-016-2825-9 · Cited by 12
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Gassen, G. V., Jonghe, C. D., Nishimura, M., Yu, G., Kuhn, S., George‐Hyslop, P. S., & Broeckhoven, C. V. (2000) · Molecular Medicine · doi:10.1007/bf03401795 · Cited by 12
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Kaffman, A., & O’Shea, E. K. (1999) · Cited by 12
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Takata, T., & Matsumura, M. (2022) · Results and problems in cell differentiation · doi:10.1007/978-3-031-06573-6_11 · Cited by 11
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Scully, C. M. (2005) · Oral Diseases · doi:10.1111/j.1601-0825.2005.01107.x · Cited by 11
Tomaso, M. V. D., Alberdi, L. V., Olsson, D., Cancela, S., Fernández, A. S., Rosillo, J. C., Reyes-Ábalos, A. L., Álvarez-Zabaleta, M., Calero, M., & Kun, A. (2022) · Biomolecules · doi:10.3390/biom12030456 · Cited by 10
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Huang, J., & Fisher, R. A. (2009) · Progress in molecular biology and translational science · doi:10.1016/s1877-1173(09)86005-5 · Cited by 9
Kwok, J. C., Perdomo, J., & Chong, B. H. (2007) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21264 · Cited by 9
Mitra, P., Gupta, E. D., Sahar, T., Pandey, A. K., Dangi, P., Reddy, K. S., Chauhan, V. S., & Gaur, D. (2016) · PLoS ONE · doi:10.1371/journal.pone.0148446 · Cited by 8
Chu, C., Chang, L.-C., Hsu, H., Wei, S., Liu, H.-W., Lee, Y. Z., Kuo, C.-C., Indra, D., Chen, C., Ong, S.-J., et al. (2011) · Eukaryotic Cell · doi:10.1128/ec.05177-11 · Cited by 8
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Liu, Y., Sun, Y., Huang, Y., Cheng, K., Xu, Y., Tian, Q., & Zhang, S. (2021) · Cell Death Discovery · doi:10.1038/s41420-020-00394-9 · Cited by 8
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Cho, G., Kim, M.-H., Kim, S. H., Ha, S.-A., Kim, H. K., Kim, J. W., & Kim, J. W. (2009) · BMC Molecular Biology · doi:10.1186/1471-2199-10-42 · Cited by 7
Ki, H., Jung, H., Park, J. H., Kim, J., Lee, K. Y., Kim, T. S., & Kim, K. (2005) · Cell Biology International · doi:10.1016/j.cellbi.2005.11.005 · Cited by 7
Zhi, J., Feng, M., Feng, X., Niu, X., Chen, W., Jiang, X., & Bai, R. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c02108 · Cited by 8
Schmidt, A., Pfeiffer, M., & Sdelci, S. (2026) · npj Metabolic Health and Disease · doi:10.1038/s44324-025-00097-8 · Cited by 7
Regulatory role of miRNAs in Wnt signaling pathway linked with cardiovascular diseases
Behera, J. K., Bhattacharya, M., Mishra, P. K., Mishra, A., Dash, A. A., Kar, N. B., Behera, B., & Patra, B. C. (2022) · Current Research in Pharmacology and Drug Discovery · doi:10.1016/j.crphar.2022.100133 · Cited by 6
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Guo, L., Glover, J. S., Risner, A., Wang, C. E., Fulmer, D. B., Moore, K. S., Gensemer, C., Rumph, M. K., Moore, R. A., Beck, T. C., et al. (2020) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd7030031 · Cited by 6
Ilyas, M. (2007) · Wiley eBooks · doi:10.1002/9780470025079.chap14.pub2 · Cited by 6
Fuerer, C., Homicskó, K., Lukashev, A. N., Pittet, A.-L., & Iggo, R. D. (2006) · BMC Cancer · doi:10.1186/1471-2407-6-236 · Cited by 5
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(2002) · Springer eBooks · doi:10.1007/978-1-4615-0129-9 · Cited by 5
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Ishida, A., Iwabuchi, S., Li, Y.-Y., Murai, K., Shirasaki, T., Kuroki, K., Shimakami, T., Nio, K., Kawaguchi, K., Imafuku, T., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26146942 · Cited by 4
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Tartakoff, A. M., Matera, A. G., Pimplikar, S. W., & Weimbs, T. (2004) · European Journal of Cell Biology · doi:10.1078/0171-9335-00386 · Cited by 4
Elbaum, M. (2007) · Springer eBooks · doi:10.1007/0-387-27747-1_1 · Cited by 4
Ha, S., Oh, J., Kim, Y., & Ham, S. W. (2017) · Journal of Chromatography B · doi:10.1016/j.jchromb.2017.05.037 · Cited by 4
Bagheri, M., Sarabi, P. Z., & Mondanizadeh, M. (2022) · Journal of Cellular Physiology · doi:10.1002/jcp.30720 · Cited by 4
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Klymkowsky, M. W. (2007) · Springer eBooks · doi:10.1007/0-387-28671-3_18 · Cited by 4
Górka, J., & Miękus, K. (2025) · Discover Oncology · doi:10.1007/s12672-025-02228-5 · Cited by 4
Nekooie‐Marnany, N., Dady, A., Duband‐Goulet, I., Relaix, F., Motterlini, R., Foresti, R., Dufour, S., & Duband, J. (2025) · Nature Communications · doi:10.1038/s41467-025-58573-0 · Cited by 3
Nuclear β-catenin: molecular regulation, challenges and therapeutic opportunities
Xie, B., Cao, Y., Li, W., Chen, R., Zhou, Q., & Xie, X. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02600-6 · Cited by 4
Largent, E. A., & Morain, S. R. (2020) · Journal of Medical Ethics · doi:10.1136/medethics-2020-106184 · Cited by 3
Molecular Crowing in Nuclear Pore
Kumeta, M. (2025) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-032-03370-3_12 · Cited by 2
Yang, H., Wu, H., Zhou, H., Liu, S., Xu, M., Wu, D., Jin, Y., Xing, R., Zhang, H., Wang, G., et al. (2026) · Genes & Diseases · doi:10.1016/j.gendis.2026.102065 · Cited by 2
The Role of E-Cadherin-Catenin Complex in Prostate Cancer Progression
Anuradha, K., & James, S. (2013) · InTech eBooks · doi:10.5772/52751 · Cited by 2
Rashidiani, S., Gebeyehu, G. M., Farkas, B., Szabadi, A., Farkas, B., Uszkai, V., Császár, A., Brandt, B., Kovács, K. A., Pap, M., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042223 · Cited by 2
Dorsoventral compartmentalization of mesoderm in heart-forming area of chick embryo
Kärner, M., Krinka, D., Padari, K., Kärner, J., & Raid, R. (2000) · Anatomy and Embryology · doi:10.1007/s004290050337 · Cited by 2
How Many Pathways Are Available for Nuclear Protein Import in Cells.
Yoneda, Y., Kametaka, A., & Sekimoto, T. (2002) · ACTA HISTOCHEMICA ET CYTOCHEMICA · doi:10.1267/ahc.35.435 · Cited by 2
de Man, S. M. A., Zwanenburg, G., van der Wal, T., Hink, M. A., & van Amerongen, R. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.28.120543 · Cited by 2
A Backdoor to the Nucleus that Runs in the Family?
Raveh, B. (2014) · Structure · doi:10.1016/j.str.2014.11.005 · Cited by 1
Desmin’s conformational modulation by hydrophobicity
Mangıt, E. K., Cevheroğlu, O., & Dinçer, P. (2024) · Turkish Journal of Biochemistry · doi:10.1515/tjb-2023-0220 · Cited by 1
The Wnt signaling network in cancer
Apfel-Starke, J., Parikh, J. R., Reischmann, P., Ewing, R. M., Müller, O. J., Xia, Y., & Dominguez, I. M. (2015) · Cambridge University Press eBooks · doi:10.1017/cbo9780511979811.016 · Cited by 2
Developmental Signaling Networks
Bommer, G. T., & Fearon, E. R. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382026-6.00009-9 · Cited by 2
Bozorgmehr, J. H. (2011) · Biosystems · doi:10.1016/j.biosystems.2011.04.006 · Cited by 1
A High-Content Imaging Screen for Cellular Regulators of β-Catenin Protein Abundance
Zeng, X., Montoute, M. N., Bee, W. T., Lin, H., Kallal, L. A., Liu, Y., Agarwal, P., Wang, D., Lu, Q., Morrow, D. M., et al. (2015) · SLAS DISCOVERY · doi:10.1177/1087057115620169 · Cited by 1
Hassan, S. A., Shabaan, A. A. A., Ahmed, A. R., Issa, Y. A., Fadel, S. H., & Elsabaa, B. M. (2023) · Journal of Histotechnology · doi:10.1080/01478885.2023.2193526 · Cited by 1
Wolf, A. K.-L., Adams-Phillips, L. C., Adams, A. N. D., Erives, A. J., & Phillips, B. T. (2021) · Cells and Development · doi:10.1016/j.cdev.2025.204013 · Cited by 1
A gust of WNT: analysis of the canonical WNT pathway.
Giunta, S. (2009) · Acta bio-medica dell'Ateneo parmense/Acta biomedica · Cited by 1
Regulating β-Catenin Nuclear Import with the Small GTPase Rap
Imamoto, N. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.01.004 · Cited by 1
Prasad, M., Ghosh, M., Kumar, R., Buragohain, L., Kumari, A., & Prasad, G. (2022) · Springer eBooks · doi:10.1007/978-981-15-9411-3_81 · Cited by 1
Liu, C., Régimbald‐Dumas, Y., Zhang, X., & He, X. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.30008-6 · Cited by 1
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Barish, G. D., & Williams, B. O. (2000) · Humana Press eBooks · doi:10.1007/978-1-59259-218-0_4 · Cited by 1
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Simos, G. (2002) · Springer eBooks · doi:10.1007/978-1-4615-0129-9_7 · Cited by 1
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Schmierer, B., & Hill, C. S. (2007) · Springer eBooks · doi:10.1007/1-4020-4709-6_10 · Cited by 1
Human TUBA1B short open reading frame product regulates cancer cell growth via importin βPreprint
Tao, Y., Bai, X., Zhou, Y., Zhao, Y., Yang, L., Zhang, S., Liu, H., Huang, X., Schneider, E., Zampetaki, A., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.08.26.554759 · Cited by 1
Nuclear force transmission drives cancer-associated fibroblast activation under BRAF inhibitionPreprint
Wang, J., Soley, B. D. S., Xiao, Y., Siegfried, L. G., Zhou, L., Xu, M., Millar, S. E., Andl, T., & Zhang, Y. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.07.19.665630 · Cited by 1
Sattar, S. (2011) · Open University of Cape Town (University of Cape Town)
Functional networks of events that modulate phenotypic manifestation of cancer
Thiagalingam, S. (2015) · Cambridge University Press eBooks · doi:10.1017/cbo9780511979811.012
Dedifferentiation and Redifferentiation in Epithelial Repair
Hallman, M. A., & Schnellmann, R. G. (2010) · Elsevier eBooks · doi:10.1016/b978-0-08-046884-6.00807-1
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Packham, S. (2015) · Figshare
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Das, U. N. (2010) · Wiley eBooks · doi:10.1002/9780813820637.ch18
IKK and Beta-Catenin in Breast Cancer
Teo, M. (2002) · Defense Technical Information Center (DTIC) · doi:10.21236/ada407807
Therapeutic Targets in Colorectal Cancer
Ettarh, R. R., Calamai, A., & Culle, A. (2012) · InTech eBooks · doi:10.5772/29610
Ultrastructural nuclear import assay
Zhong, H., Shio, H., & Yaseen, N. R. (2006) · Methods · doi:10.1016/j.ymeth.2006.07.012
Alexander, N. R. (2005) · UA Campus Repository (The University of Arizona)
Non-phosphorylated b-catenin in Wnt signaling
van Noort, M. (2002) · Utrecht University Repository (Utrecht University)
Metadata
- Authors
- Fagotto, F., Glück, U., & Gumbiner, B. M.
- Affiliations
- Memorial Sloan Kettering Cancer Center (US)
- Corresponding author
- Gumbiner, Barry M.
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 1998-02
- Volume
- 8
- Issue
- 4
- Pages
- 181-190
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W1993496373
- Cited by
- 434
- References
- 60
- Citations by year
- 2026: 4 · 2025: 7 · 2024: 8 · 2023: 6 · 2022: 11 · 2021: 11 · 2020: 6 · 2019: 7 · 2018: 11 · 2017: 13 · 2016: 10 · 2015: 16 · 2014: 15 · 2013: 12 · 2012: 14
- FWCI
- 13.79
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Current Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (P30CA008748)
- National Institute of General Medical Sciences (GM37432)
- 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 › Nuclear Structure and Function
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- β-catenin, nuclear import, Wnt signaling, nuclear localization signal, importin beta, nuclear pore complex, Ran GTPase, signal transduction regulation
- MeSH terms
- Animals, Binding, Competitive, Biological Transport, Cell Nucleus, Cytoskeletal Proteins, Cytosol, Nuclear Proteins, Recombinant Proteins, Xenopus, Trans-Activators, Nuclear Localization Signals, Karyopherins, alpha Karyopherins, Xenopus Proteins, beta Catenin
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