Tumor suppression by the Fbw7 ubiquitin ligase: mechanisms and opportunities
Open accessAbstract
Tumor suppressors with widespread impact on carcinogenesis control broad spectra of oncogenic pathways. Protein degradation is an emerging mechanism by which tumor suppressors regulate a diversity of pathways and is exemplified by the SCF(Fbw7) ubiquitin ligase. Rapidly accumulating data indicate that SCF(Fbw7) regulates a network of crucial oncoproteins. Importantly, the FBXW7 gene, which encodes Fbw7, is one of the most frequently mutated genes in human cancers. These studies are yielding important new insights into tumorigenesis and may soon enable therapies targeting the Fbw7 pathway. Here, we focus on the mechanisms and consequences of Fbw7 deregulation in cancers and discuss possible therapeutic approaches.
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GSK3β drives protein destruction majorly through E3 ubiquitin ligase FBW7.
“GSK3b drives protein destruction majorly through E3 ubiquitin ligase FBW7 (also called FBXW7, hCDC4, and SEL-10; ref. 14).”
From FBW7 Inhibits Myeloid Differentiation in Acute Myeloid Leukemia via GSK3-Dependent Ubiquitination of PU.1 (2021) · cites this paper as [14]
The section “Substrate phosphorylation stimulates Fbw7 binding” (page not supplied) says GSK3 phosphorylates many Fbw7-recognized degrons, linking its activity to Fbw7-mediated degradation. It does not establish that GSK3β drives protein destruction *mainly* through FBW7; it notes that most substrates have multiple turnover pathways. (LLM, conf=0.86)
Experimental — accuracy not yet measuredFbw7 dimerization increases cyclin E binding: both Fbw7 protomers have one cyclin E binding site, and through dimerization both binding sites become simultaneously accessible to cyclin E, leading to increased affinity of Fbw7-cyclin E interaction.
“In Fbw7 dimer interface, both Fbw7 protomers have one cyclin E binding site, and through dimerization both binding sites become simultaneously accessible to cyclin E, thus leading to increased affinity of Fbw7 -cyclin E interaction [39].”
From Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56 (2017) · cites this paper as [39]
Split into 2 atoms — 1 confirmed, 1 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredFBW7 is the substrate recognition motif of multimeric E3 ligase SCF-FBW7 which binds to substrates by recognizing phosphorylated motifs via its WD40 repeat regions.
“F-box protein FBW7 is the substrate recognition motif of multimeric E3 ligase SCF-FBW7 (SKP-cullin-Fbox) which binds to substrates by recognizing phosphorylated motifs (phosphodegron motif) via its WD40 repeat regions (14,15).”
From FBW7 Inhibits Myeloid Differentiation in Acute Myeloid Leukemia via GSK3-Dependent Ubiquitination of PU.1 (2021) · cites this paper as [14]
FBXW7 recognizes a conserved S/TxxxS/T motif.
“FBXW7 is known to recognize a conserved S/TxxxS/T motif59,60”
From Targeting Msx2 as a brake in the fusion fate of osteoclasts and an anabolic therapy in pre-clinical models of osteoporosis (2025) · cites this paper as [60]
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Cites
Cerami, E., Gao, J., Dogrusoz, U., Gross, B. E., Sumer, S. O., Aksoy, B. A., Jacobsen, A., Byrne, C. J., Heuer, M. L., Larsson, E., et al. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0095 · Cited by 17,455 · see citing works
Integrative Analysis of Complex Cancer Genomics and Clinical Profiles Using the cBioPortal
Gao, J., Aksoy, B. A., Dogrusoz, U., Dresdner, G., Gross, B., Sumer, S. O., Sun, Y., Jacobsen, A., Sinha, R., Larsson, E., et al. (2013) · Science Signaling · doi:10.1126/scisignal.2004088 · Cited by 15,160 · see citing works
Hershko, A., & Ciechanover, A. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.425 · Cited by 8,840 · see citing works
Comprehensive molecular characterization of human colon and rectal cancer
The Cancer Genome Atlas Network (2012) · Nature · doi:10.1038/nature11252 · Cited by 8,499 · see citing works
Integrated genomic characterization of endometrial carcinoma
The Cancer Genome Atlas Research Network, & Levine, D. A. (2013) · Nature · doi:10.1038/nature12113 · Cited by 5,784 · see citing works
Mutational landscape and significance across 12 major cancer types
Kandoth, C., McLellan, M. D., Vandin, F., Ye, K., Niu, B., Lu, C., Xie, M., Zhang, Q., McMichael, J. F., Wyczalkowski, M. A., et al. (2013) · Nature · doi:10.1038/nature12634 · Cited by 4,419 · see citing works
Activating Mutations of NOTCH1 in Human T Cell Acute Lymphoblastic Leukemia
Weng, A. P., Ferrando, A. A., Lee, W., Morris, J. P., Silverman, L. B., Sanchez-Irizarry, C., Blacklow, S. C., Look, A. T., & Aster, J. C. (2004) · Science · doi:10.1126/science.1102160 · Cited by 2,706 · see citing works
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679 · see citing works
Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome
Finley, D. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.081507.101607 · Cited by 1,764 · see citing works
Mechanism of auxin perception by the TIR1 ubiquitin ligase
Tan, X., Calderon-Villalobos, L. I. A., Sharon, M., Zheng, C., Robinson, C. V., Estelle, M., & Zheng, N. (2007) · Nature · doi:10.1038/nature05731 · Cited by 1,688 · see citing works
Ubiquitin ligases: cell-cycle control and cancer
Nakayama, K. I., & Nakayama, K. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1881 · Cited by 1,441 · see citing works
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 1,379 · see citing works
Welcker, M., & Clurman, B. E. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2290 · Cited by 1,084 · see citing works
Self-citationWelcker, M., Orian, A., Jin, J., Grim, J. A., Harper, J. W., Eisenman, R. N., & Clurman, B. E. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0402770101 · Cited by 942 · see citing works
Self-citationPhosphorylation‐dependent degradation of c‐Myc is mediated by the F‐box protein Fbw7
Yada, M., Hatakeyama, S., Kamura, T., Nishiyama, M., Tsunematsu, R., Imaki, H., Ishida, N., Okumura, F., Nakayama, K., & Nakayama, K. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600217 · Cited by 810 · see citing works
Sensitivity to antitubulin chemotherapeutics is regulated by MCL1 and FBW7
Wertz, I. E., Kusam, S., Lam, C., Okamoto, T., Sandoval, W. N., Anderson, D. J., Helgason, E., Ernst, J. A., Eby, M., Liu, J., et al. (2011) · Nature · doi:10.1038/nature09779 · Cited by 784 · see citing works
Phosphorylation-Dependent Ubiquitination of Cyclin E by the SCF Fbw7 Ubiquitin Ligase
Koepp, D. M., Schaefer, L. K., Ye, X., Keyomarsi, K., Chu, C., Harper, J. W., & Elledge, S. J. (2001) · Science · doi:10.1126/science.1065203 · Cited by 764 · see citing works
Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication
Nash, P., Tang, X., Orlicky, S. M., Chen, Q., Gertler, F. B., Mendenhall, M. D., Sicheri, F., Pawson, T. J., & Tyers, M. (2001) · Nature · doi:10.1038/35107009 · Cited by 761 · see citing works
Deregulated cyclin E induces chromosome instability
Spruck, C., Won, K., & Reed, S. I. (1999) · Nature · doi:10.1038/45836 · Cited by 692 · see citing works
Mechanisms and function of substrate recruitment by F-box proteins
Skaar, J. R., Pagan, J. K., & Pagano, M. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3582 · Cited by 671 · see citing works
O’Neil, J., Grim, J. A., Strack, P. R., Rao, S. S., Tibbitts, D., Winter, C. G., Hardwick, J. S., Welcker, M., Meijerink, J. P. P., Pieters, R., et al. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070876 · Cited by 662 · see citing works
Self-citationSCFFBW7 regulates cellular apoptosis by targeting MCL1 for ubiquitylation and destruction
Inuzuka, H., Shaik, S., Onoyama, I., Gao, D., Tseng, A., Maser, R. S., Zhai, B., Wan, L., Gutiérrez, A., Lau, A. W., et al. (2011) · Nature · doi:10.1038/nature09732 · Cited by 635 · see citing works
Mastermind Recruits CycC:CDK8 to Phosphorylate the Notch ICD and Coordinate Activation with Turnover
Fryer, C. J., White, B., & Jones, K. A. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.014 · Cited by 627 · see citing works
Strohmaier, H. M., Spruck, C., Kaiser, P., Won, K., Sangfelt, O., & Reed, S. I. (2001) · Nature · doi:10.1038/35095076 · Cited by 584 · see citing works
Inactivation of hCDC4 can cause chromosomal instability
Rajagopalan, H., Jallepalli, P. V., Rago, C., Velculescu, V. E., Kinzler, K. W., Vogelstein, B., & Christoph Lengauer, C. (2004) · Nature · doi:10.1038/nature02313 · Cited by 552 · see citing works
Orlicky, S. M., Tang, X., Willems, A. R., Tyers, M., & Sicheri, F. (2003) · Cell · doi:10.1016/s0092-8674(03)00034-5 · Cited by 510 · see citing works
FBXW7/hCDC4 Is a General Tumor Suppressor in Human Cancer
Akhoondi, S., Sun, D., von der Lehr, N., Apostolidou, S., Klotz, K., Malyukova, A., Cepeda, D., Fiegl, H., Dafou, D., Marth, C., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1320 · Cited by 507 · see citing works
Clurman, B. E., Sheaff, R. J., Thress, K. S., Groudine, M. T., & Roberts, J. M. (1996) · Genes & Development · doi:10.1101/gad.10.16.1979 · Cited by 488 · see citing works
Self-citationThe SCFFBW7 ubiquitin ligase complex as a tumor suppressor in T cell leukemia
Thompson, B. J., Buonamici, S., Sulis, M. L., Palomero, T., Vilimas, T., Basso, G., Ferrando, A. A., & Aifantis, I. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20070872 · Cited by 479 · see citing works
Phosphorylation by Glycogen Synthase Kinase-3 Controls c-Myc Proteolysis and Subnuclear Localization
Gregory, M. A., Qi, Y., & Hann, S. R. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m310722200 · Cited by 476 · see citing works
Hao, B., Oehlmann, S., Sowa, M. E., Harper, J. W., & Pavletich, N. P. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.02.022 · Cited by 464 · see citing works
Öberg, C., Li, J., Pauley, A. M., Wolf, E., Gurney, M. E., & Lendahl, U. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103992200 · Cited by 412 · see citing works
Wei, W., Jin, J., Schlisio, S., Harper, J. W., & Kaelin, W. G. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.06.005 · Cited by 403 · see citing works
Gupta-Rossi, N., Bail, O. L., Gonen, H., Brou, C., Logeat, F., Six, E. M., Ciechanover, A. J., & Israël, A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101343200 · Cited by 379 · see citing works
Chromosomally unstable mouse tumours have genomic alterations similar to diverse human cancers
Maser, R. S., Choudhury, B., Campbell, P. J., Feng, B., Wong, K.-K., Protopopov, A., O’Neil, J., Gutierrez, A., Ivanova, E., Perna, I., et al. (2007) · Nature · doi:10.1038/nature05886 · Cited by 377 · see citing works
Multisite Phosphorylation by Cdk2 and GSK3 Controls Cyclin E Degradation
Welcker, M., Singer, J. D., Loeb, K. R., Grim, J. A., Bloecher, A., Gurian-West, M., Clurman, B. E., & Roberts, J. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00287-9 · Cited by 364 · see citing works
Self-citationWon, K. A., & Reed, S. I. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00793.x · Cited by 360 · see citing works
The Ubiquitin Ligase FBXW7 Modulates Leukemia-Initiating Cell Activity by Regulating MYC Stability
King, B., Trimarchi, T., Reavie, L. B., Xu, L., Mullenders, J., Ntziachristos, P., Aranda-Orgillés, B., Pérez-García, A., Shi, J., Vakoc, C. R., et al. (2013) · Cell · doi:10.1016/j.cell.2013.05.041 · Cited by 347 · see citing works
The Ubiquitin Ligase SCF Fbw7 Antagonizes Apoptotic JNK Signaling
Nateri, A. S., Riera-Sans, L., Costa, C. D., & Behrens, A. (2004) · Science · doi:10.1126/science.1092880 · Cited by 339 · see citing works
Wu, G., Lyapina, S., Das, I., Li, J., Gurney, M. E., Pauley, A. M., Chui, I., Deshaies, R. J., & Kitajewski, J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.21.7403-7415.2001 · Cited by 338 · see citing works
A Nucleolar Isoform of the Fbw7 Ubiquitin Ligase Regulates c-Myc and Cell Size
Welcker, M., Orian, A., Grim, J. A., Eisenman, R. N., & Clurman, B. E. (2004) · Current Biology · doi:10.1016/j.cub.2004.09.083 · Cited by 311 · see citing works
Self-citationBrockmann, M., Poon, E., Berry, T., Carstensen, A., Deubzer, H. E., Rycak, L., Jamin, Y., Thway, K., Robinson, S. P., Roels, F., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.05.005 · Cited by 300 · see citing works
Deregulation of cyclin E in human cells interferes with prereplication complex assembly
Ekholm‐Reed, S., Méndez, J., Tedesco, D., Zetterberg, A., Stillman, B., & Reed, S. I. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200404092 · Cited by 296 · see citing works
Bhatia, 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 · see citing works
Bahram, F., von der Lehr, N., Cetinkaya, C., & Larsson, L. (2000) · Blood · doi:10.1182/blood.v95.6.2104 · Cited by 283 · see citing works
Mouse Fbw7/Sel-10/Cdc4 Is Required for Notch Degradation during Vascular Development
Tsunematsu, R., Nakayama, K., Oike, Y., Nishiyama, M., Ishida, N., Hatakeyama, S., Bessho, Y., Kageyama, R., Suda, T., & Nakayama, K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312337200 · Cited by 276 · see citing works
hCDC4 gene mutations in endometrial cancer.
Spruck, C., Strohmaier, H. M., Sangfelt, O., Müller, H. M., Hubalek, M., Müller‐Holzner, E., Marth, C., Widschwendter, M., & Reed, S. I. (2002) · PubMed · Cited by 268 · see citing works
Tetzlaff, M. T., Yu, W., Li, M. Z., Zhang, P., Finegold, M. J., Mahon, K., Harper, J. W., Schwartz, R. J., & Elledge, S. J. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307875101 · Cited by 250 · see citing works
Tang, X., Orlicky, S., Lin, Z., Willems, A., Neculai, D., Ceccarelli, D., Mercurio, F., Shilton, B. H., Sicheri, F., & Tyers, M. (2007) · Cell · doi:10.1016/j.cell.2007.04.042 · Cited by 209 · see citing works
Malyukova, A., Dohda, T., von der Lehr, N., Akhoondi, S., Corcoran, M., Heyman, M. M., Spruck, C., Grandér, D., Lendahl, U., & Sangfelt, O. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4381 · Cited by 197 · see citing works
Olson, B. L., Hock, M. B., Ekholm‐Reed, S., Wohlschlegel, J. A., Dev, K. K., Kralli, A., & Reed, S. I. (2008) · Genes & Development · doi:10.1101/gad.1624208 · Cited by 185 · see citing works
Matsuoka, S., Oike, Y., Onoyama, I., Iwama, A., Arai, F., Takubo, K., Mashimo, Y., Oguro, H., Nitta, E., Ito, K., et al. (2008) · Genes & Development · doi:10.1101/gad.1621808 · Cited by 183 · see citing works
Onoyama, I., Tsunematsu, R., Matsumoto, A., Kimura, T., de Alborán, I. M., Nakayama, K., & Nakayama, K. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20062299 · Cited by 183 · see citing works
Ablation of Fbxw7 Eliminates Leukemia-Initiating Cells by Preventing Quiescence
Takeishi, S., Matsumoto, A., Onoyama, I., Naka, K., Hirao, A., & Nakayama, K. I. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.01.026 · Cited by 177 · see citing works
Babaei‐Jadidi, R., Li, N., Saadeddin, A., Spencer‐Dene, B., Jandke, A., Muhammad, B. A., Ibrahim, E. E., Muraleedharan, R., Abuzinadah, M. F., Belnoue-Davis, H. L., et al. (2011) · The Journal of Experimental Medicine · doi:10.1084/jem.20100830 · Cited by 172 · see citing works
Control of hematopoietic stem cell quiescence by the E3 ubiquitin ligase Fbw7
Thompson, B. J., Janković, V., Gao, J., Buonamici, S., Vest, A., Lee, J. M., Zavadil, J., Nimer, S. D., & Aifantis, I. (2008) · The Journal of Experimental Medicine · doi:10.1084/jem.20080277 · Cited by 171 · see citing works
Fbw7 controls neural stem cell differentiation and progenitor apoptosis via Notch and c-Jun
Hoeck, J. D., Jandke, A., Blake, S. M., Nye, E. L., Spencer‐Dene, B., Brandner, S., & Behrens, A. (2010) · Nature Neuroscience · doi:10.1038/nn.2644 · Cited by 168 · see citing works
Fbxw7α- and GSK3-mediated degradation of p100 is a pro-survival mechanism in multiple myeloma
Busino, L., Millman, S. E., Scotto, L., Kyratsous, C. A., Basrur, V., O’Connor, O. A., Hoffmann, A., Elenitoba‐Johnson, K. S. J., & Pagano, M. (2012) · Nature Cell Biology · doi:10.1038/ncb2463 · Cited by 165 · see citing works
Tumor suppressor functions of FBW7 in cancer development and progression
Wang, Z. P., Inuzuka, H., Zhong, J., Wan, L., Fukushima, H., Sarkar, F. H., & Wei, W. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.03.017 · Cited by 152 · see citing works
An allosteric inhibitor of substrate recognition by the SCFCdc4 ubiquitin ligase
Orlicky, S. M., Tang, X., Neduva, V., Elowe, N. H., Brown, E. D., Sicheri, F., & Tyers, M. (2010) · Nature Biotechnology · doi:10.1038/nbt.1646 · Cited by 150 · see citing works
Zhao, D. H., Zheng, H., Zhou, Z., & Chen, C. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-0040 · Cited by 150 · see citing works
Min, S. H., Lau, A. W., Lee, T. H., Inuzuka, H., Wei, S., Huang, P., Shaik, S., Lee, D. Y., Finn, G., Balaštík, M., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.04.012 · Cited by 146 · see citing works
Sancho, R., Jandke, A., Belnoue-Davis, H. L., Diefenbacher, M. E., Tomlinson, I. P. M., & Behrens, A. (2010) · Gastroenterology · doi:10.1053/j.gastro.2010.05.078 · Cited by 136 · see citing works
Nucleophosmin and its AML-associated mutant regulate c-Myc turnover through Fbw7γ
Bonetti, P., Davoli, T., Sironi, C., Amati, B. B., Pelicci, P. G., & Colombo, E. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200711040 · Cited by 134 · see citing works
Regulation of c-Myc Ubiquitination Controls Chronic Myelogenous Leukemia Initiation and Progression
Reavie, L. B., Buckley, S. M., Loizou, E., Takeishi, S., Aranda-Orgillés, B., Ndiaye‐Lobry, D., Abdel-Wahab, O. I., Ibrahim, S., Nakayama, K. I., & Aifantis, I. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.01.025 · Cited by 130 · see citing works
Loss of Fbw7 Reprograms Adult Pancreatic Ductal Cells into α, δ, and β Cells
Sancho, R., Gruber, R., Gu, G., & Behrens, A. (2014) · Cell stem cell · doi:10.1016/j.stem.2014.06.019 · Cited by 130 · see citing works
hCDC4b, a regulator of cyclin E, as a direct transcriptional target of p53
Kimura, T., Gotoh, M., Nakamura, Y., & Arakawa, H. (2003) · Cancer Science · doi:10.1111/j.1349-7006.2003.tb01460.x · Cited by 127 · see citing works
Regulation of hematopoietic stem cell differentiation by a single ubiquitin ligase–substrate complex
Reavie, L. B., Gatta, G. D., Moran-Crusio, K., Aranda-Orgillés, B., Buckley, S. M., Thompson, B. J., Lee, E., Gao, J., Bredemeyer, A. L., Helmink, B. A., et al. (2010) · Nature Immunology · doi:10.1038/ni.1839 · Cited by 123 · see citing works
Isoform- and cell cycle–dependent substrate degradation by the Fbw7 ubiquitin ligase
Grim, J. E., Gustafson, M. P., Hirata, R. K., Hagar, A., Swanger, J., Welcker, M., Hwang, H. C., Ericsson, J., Russell, D. W., & Clurman, B. E. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200802076 · Cited by 119 · see citing works
Self-citationFbxw7 regulates lipid metabolism and cell fate decisions in the mouse liver
Onoyama, I., Suzuki, A., Matsumoto, A., Tomita, K., Katagiri, H., Oike, Y., Nakayama, K., & Nakayama, K. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40725 · Cited by 118 · see citing works
p53 and p21 Form an Inducible Barrier that Protects Cells against Cyclin E-cdk2 Deregulation
Minella, A. C., Swanger, J., Bryant, E. M., Welcker, M., Hwang, H. C., & Clurman, B. E. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01225-3 · Cited by 117 · see citing works
Self-citationFbw7/hCDC4 dimerization regulates its substrate interactions.
Welcker, M., & Clurman, B. E. (2007) · Cell Division · doi:10.1186/1747-1028-2-7 · Cited by 115 · see citing works
Self-citationLiu, N., Li, H., Li, S., Shen, M., Xiao, N., Chen, Y., Wang, Y., Wang, W., Wang, R., Wang, Q., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.099440 · Cited by 115 · see citing works
van Drogen, F., Sangfelt, O., Malyukova, A., Matskova, L. V., Yeh, E. S., Means, A. R., & Reed, S. I. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.020 · Cited by 112 · see citing works
Davis, M. A., Larimore, E. A., Fissel, B. M., Swanger, J., Taatjes, D. J., & Clurman, B. E. (2013) · Genes & Development · doi:10.1101/gad.207720.112 · Cited by 112 · see citing works
Self-citationThe ubiquitous nature of cancer: the role of the SCFFbw7 complex in development and transformation
Moran-Crusio, K., King, B., Reavie, L. B., & Aifantis, I. (2010) · Oncogene · doi:10.1038/onc.2010.222 · Cited by 111 · see citing works
A mouse model for cyclin E-dependent genetic instability and tumorigenesis
Loeb, K. R., Kostner, H., Firpo, E. J., Norwood, T. H., Tsuchiya, K. D., Clurman, B. E., & Roberts, J. M. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.06.010 · Cited by 107 · see citing works
Self-citationCyclin E overexpression impairs progression through mitosis by inhibiting APCCdh1
Keck, J. M., Summers, M. K., Tedesco, D., Ekholm‐Reed, S., Chuang, L.-C., Jackson, P. K., & Reed, S. I. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200703202 · Cited by 103 · see citing works
FBXW7α attenuates inflammatory signalling by downregulating C/EBPδ and its target gene Tlr4
Balamurugan, K., Sharan, S., Klarmann, K. D., Zhang, Y., Coppola, V., Summers, G. H., Roger, T., Morrison, D. K., Keller, J. R., & Sterneck, E. (2013) · Nature Communications · doi:10.1038/ncomms2677 · Cited by 98 · see citing works
Fbw7 and p53 Cooperatively Suppress Advanced and Chromosomally Unstable Intestinal Cancer
Grim, J. E., Knoblaugh, S. E., Guthrie, K. A., Hagar, A., Swanger, J., Hespelt, J., Delrow, J. J., Small, T., Grady, W. M., Nakayama, K. I., et al. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00305-12 · Cited by 97 · see citing works
Self-citationFbw7 dimerization determines the specificity and robustness of substrate degradationPreprint
Welcker, M., Larimore, E. A., Swanger, J., Bengoechea-Alonso, M. T., Grim, J. E., Ericsson, J., Zheng, N., & Clurman, B. E. (2013) · Genes & Development · doi:10.1101/gad.229195.113 · Cited by 91 · see citing works
Self-citationMinella, A. C., Loeb, K. R., Knecht, A., Welcker, M., Varnum‐Finney, B., Bernstein, I. D., Roberts, J. M., & Clurman, B. E. (2008) · Genes & Development · doi:10.1101/gad.1650208 · Cited by 90 · see citing works
Self-citationAberrant regulation of FBW7 in cancer
Wang, L., Ye, X., Liu, Y., Wei, W., & Wang, Z. P. (2014) · Oncotarget · doi:10.18632/oncotarget.1859 · Cited by 89 · see citing works
Akhoondi, S., Lindström, L. S., Widschwendter, M., Corcoran, M., Bergh, J. C. S., Spruck, C., Grandér, D., & Sangfelt, O. (2010) · Breast Cancer Research · doi:10.1186/bcr2788 · Cited by 84 · see citing works
Kanatsu‐Shinohara, M., Onoyama, I., Nakayama, K. I., & Shinohara, T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1401837111 · Cited by 82 · see citing works
A component of the mir-17-92 polycistronic oncomir promotes oncogene-dependent apoptosis
Olive, V., Sabio, E. Y., Bennett, M. J., Jong, C. S. D., Biton, A., McGann, J. C., Greaney, S. K., Sodir, N. M., Zhou, A. Y., Balakrishnan, A., et al. (2013) · eLife · doi:10.7554/elife.00822 · Cited by 80 · see citing works
The ubiquitin ligase Fbxw7 controls adipocyte differentiation by targeting C/EBPα for degradation
Bengoechea-Alonso, M. T., & Ericsson, J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0913367107 · Cited by 80 · see citing works
Belnoue-Davis, H. L., Lewis, A., Behrens, A., & Tomlinson, I. P. M. (2013) · Gut · doi:10.1136/gutjnl-2013-304719 · Cited by 75 · see citing works
Pten Regulates Aurora-A and Cooperates with Fbxw7 in Modulating Radiation-Induced Tumor Development
Kwon, Y.-W., Kim, I.-J., Wu, D., Lü, J., Stock, W. A., Liu, Y., Huang, Y., Kang, H. C., Delrosario, R., Jen, K., et al. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0025 · Cited by 73 · see citing works
Fbw7 Isoform Interaction Contributes to Cyclin E Proteolysis
Zhang, W., & Koepp, D. M. (2006) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0253 · Cited by 67 · see citing works
Sancho, R., Blake, S. M., Tendeng, C., Clurman, B. E., Lewis, J. H., & Behrens, A. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001586 · Cited by 66 · see citing works
Self-citationEkholm‐Reed, S., Goldberg, M. S., Schlossmacher, M. G., & Reed, S. I. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00535-13 · Cited by 65 · see citing works
Lee, E. K., & Diehl, J. A. (2013) · Oncogene · doi:10.1038/onc.2013.144 · Cited by 62 · see citing works
p53 and SCFFbw7 cooperatively restrain cyclin E-associated genome instability
Minella, A. C., Grim, J., Welcker, M., & Clurman, B. E. (2007) · Oncogene · doi:10.1038/sj.onc.1210518 · Cited by 60 · see citing works
Self-citationTumor suppressor Fbxw7 regulates TGFβ signaling by targeting TGIF1 for degradation
Bengoechea-Alonso, M. T., & Ericsson, J. (2010) · Oncogene · doi:10.1038/onc.2010.278 · Cited by 46 · see citing works
Bialkowska, A. B., Liu, Y., Nandan, M. O., & Yang, V. W. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.508549 · Cited by 39 · see citing works
Fbxw7β resides in the endoplasmic reticulum membrane and protects cells from oxidative stress
Matsumoto, A., Tateishi, Y., Onoyama, I., Okita, Y., Nakayama, K., & Nakayama, K. (2011) · Cancer Science · doi:10.1111/j.1349-7006.2011.01851.x · Cited by 32 · see citing works
Prognostic Significance of Fbw7 in Human Melanoma and Its Role in Cell Migration
Cheng, Y., Chen, G., Martinka, M., Ho, V., & Li, G. (2013) · Journal of Investigative Dermatology · doi:10.1038/jid.2013.58 · Cited by 29 · see citing works
Siu, K. T., Xu, Y., Swartz, K. L., Bhattacharyya, M., Gurbuxani, S. K., Hua, Y., & Minella, A. C. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01528-13 · Cited by 25 · see citing works
CDC4/FBXW7 and the ‘just enough’ model of tumourigenesis
Belnoue-Davis, H. L., & Tomlinson, I. P. M. (2012) · The Journal of Pathology · doi:10.1002/path.4004 · Cited by 21 · see citing works
The methylation status of FBXW7 β-form correlates with histological subtype in human thymoma
Gu, Z., Mitsui, H., Inomata, K., Honda, M., Endo, C., Sakurada, A., Sato, M., Okada, Y., Kondo, T., & Horii, A. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.047 · Cited by 14 · see citing works
Gu, Z., Inomata, K., Mitsui, H., & Horii, A. (2008) · Genes & Genetic Systems · doi:10.1266/ggs.83.347 · Cited by 10 · see citing works
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Mackay, A., Burford, A., Carvalho, D., Izquierdo, E., Fazal-Salom, J., Taylor, K. R., Bjerke, L., Clarke, M., Vinci, M., Nandhabalan, M., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.08.017 · Cited by 1,212 · see citing works
FBXW7: a critical tumor suppressor of human cancers
Yeh, C., Bellon, M., & Nicot, C. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0857-2 · Cited by 513 · see citing works
Ubiquitination and deubiquitination in cancer: from mechanisms to novel therapeutic approaches
Liu, F., Chen, J., Li, K., Li, H., Zhu, Y., Zhai, Y., Lu, B., Fan, Y., Liu, Z., Chen, X., et al. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02046-3 · Cited by 352 · see citing works
WD40 repeat domain proteins: a novel target class?
Schapira, M., Tyers, M., Torrent, M., & Arrowsmith, C. H. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.179 · Cited by 335 · see citing works
Zhang, G., Li, S., Lu, J., Ge, Y., Wang, Q., Ma, G., Zhao, Q., Wu, D., Gong, W., Du, M., et al. (2018) · Molecular Cancer · doi:10.1186/s12943-018-0829-6 · Cited by 270 · see citing works
FBW7-NRA41-SCD1 axis synchronously regulates apoptosis and ferroptosis in pancreatic cancer cells
Zeng, Y., Zhuo, Q., Hu, Q., Xu, X., Liu, M., Zhang, Z., Xu, W., Liu, W., Fan, G., Qin, Y., et al. (2020) · Redox Biology · doi:10.1016/j.redox.2020.101807 · Cited by 271 · see citing works
Human papillomavirus and the landscape of secondary genetic alterations in oral cancersPreprint
Gillison, M. L., Akagi, K., Xiao, W., Jiang, B., Pickard, R. K. L., Li, J., Swanson, B. J., Agrawal, A. D., Zucker, M., Stache-Crain, B., et al. (2018) · Genome Research · doi:10.1101/gr.241141.118 · Cited by 237 · see citing works
The role of ubiquitination and deubiquitination in tumor invasion and metastasis
Han, S., Wang, R., Zhang, Y., Li, X., Gan, Y., Gao, F., Rong, P., Wang, W., & Li, W. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.69411 · Cited by 215 · see citing works
Sancho, R., Cremona, C. A., & Behrens, A. (2015) · EMBO Reports · doi:10.15252/embr.201540188 · Cited by 196 · see citing works
Xiao, D., Yue, M., Su, H., Ren, P., Jiang, J., Li, F., Hu, Y., Du, H., Liu, H., & Qing, G. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.016 · Cited by 174 · see citing works
Niu, Z., Jin, R., Zhang, Y., & Li, H. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01200-x · Cited by 172 · see citing works
Systematic Functional Interrogation of Rare Cancer Variants Identifies Oncogenic Alleles
Kim, E., Ilić, N., Shrestha, Y., Zou, L., Kamburov, A., Zhu, C., Yang, X., Lubonja, R., Tran, N. H., Nguyen, C., et al. (2016) · Cancer Discovery · doi:10.1158/2159-8290.cd-16-0160 · Cited by 168 · see citing works
FBXW7 in Cancer: What Has Been Unraveled Thus Far?
Sailo, B. L., Banik, K., Girisa, S., Bordoloi, D., Fan, L., Halim, C. E., Wang, H., Kumar, A. P., Zheng, D., Mao, X., et al. (2019) · Cancers · doi:10.3390/cancers11020246 · Cited by 167 · see citing works
Tong, J., Tan, S., Zou, F., Yu, J., & Zhang, L. (2016) · Oncogene · doi:10.1038/onc.2016.247 · Cited by 160 · see citing works
Mutational patterns in chemotherapy resistant muscle-invasive bladder cancer
Liu, D., Abbosh, P. H., Keliher, D., Reardon, B. M., Miao, D., Mouw, K. W., Taylor-Weiner, A. N., Wankowicz, S. A. M., Han, G. C., Teo, M. Y., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02320-7 · Cited by 151 · see citing works
Kourtis, N., Moubarak, R. S., Aranda-Orgillés, B., Lui, K. P., Aydin, I. T., Trimarchi, T., Darvishian, F., Salvaggio, C., Zhong, J., Bhatt, K., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3121 · Cited by 150 · see citing works
Clinical significance of FBXW7 loss of function in human cancers
Fan, J., Bellon, M., Ju, M., Zhao, L., Wei, M., Fu, L., & Nicot, C. (2022) · Molecular Cancer · doi:10.1186/s12943-022-01548-2 · Cited by 148 · see citing works
Targeting the ubiquitin pathway for cancer treatment
Liu, J., Shaik, S., Dai, X., Wu, Q., Zhou, X., Wang, Z. P., & Wei, W. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.11.005 · Cited by 144 · see citing works
Mészáros, B., Kumar, M., Gibson, T. J., Uyar, B., & Dosztányi, Z. (2017) · Science Signaling · doi:10.1126/scisignal.aak9982 · Cited by 139 · see citing works
FBXW7 Facilitates Nonhomologous End-Joining via K63-Linked Polyubiquitylation of XRCC4
Zhang, Q., Karnak, D. M., Tan, M., Lawrence, T. S., Morgan, M. A., & Sun, Y. (2016) · Molecular Cell · doi:10.1016/j.molcel.2015.12.010 · Cited by 131 · see citing works
Discovery of PF-06873600, a CDK2/4/6 Inhibitor for the Treatment of Cancer
Freeman‐Cook, K. D., Hoffman, R. L., Behenna, D. C., Boras, B. W., Carelli, J. D., Diehl, W. C., Ferre, R. A., He, Y.-A., Hui, A., Huang, B., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00159 · Cited by 131 · see citing works
F-box proteins: Keeping the epithelial-to-mesenchymal transition (EMT) in check
Diaz, V. M., & de Herreros, A. G. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.10.003 · Cited by 126 · see citing works
STAT3 Interactors as Potential Therapeutic Targets for Cancer Treatment
Laudisi, F., Cherubini, F., Monteleone, G., & Stolfi, C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19061787 · Cited by 128 · see citing works
FBXW7β loss-of-function enhances FASN-mediated lipogenesis and promotes colorectal cancer growth
Wei, W., Qin, B., Wen, W., Zhang, B., Luo, H., Wang, Y., Xu, H., Xie, X., Liu, S., Jiang, X. J., et al. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01405-8 · Cited by 115 · see citing works
PRMT5 enhances tumorigenicity and glycolysis in pancreatic cancer via the FBW7/cMyc axis
Qin, Y., Hu, Q., Xu, J., Ji, S., Dai, W., Liu, W., Xu, W., Sun, Q., Zhang, Z., Ni, Q., et al. (2019) · Cell Communication and Signaling · doi:10.1186/s12964-019-0344-4 · Cited by 110 · see citing works
FBW7 Mediates Senescence and Pulmonary Fibrosis through Telomere Uncapping
Wang, L., Chen, R., Li, G., Wang, Z., Liu, J., Liang, Y., & Liu, J. (2020) · Cell Metabolism · doi:10.1016/j.cmet.2020.10.004 · Cited by 109 · see citing works
Synthetic Lethality of Wnt Pathway Activation and Asparaginase in Drug-Resistant Acute Leukemias
Hinze, L., Pfirrmann, M., Karim, S., Degar, J., McGuckin, C., Vinjamur, D. S., Sacher, J. R., Stevenson, K. E., Neuberg, D. S., Orellana, E. A., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.03.004 · Cited by 105 · see citing works
Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56
Wang, J., Okkeri, J., Pavic, K., Wang, Z., Kauko, O., Halonen, T., Sarek, G., Ojala, P. M., Rao, Z., Xu, W., et al. (2017) · The EMBO Reports · doi:10.15252/embr.201642788 · Cited by 95 · see citing works
Oncogenic mutations in the FBXW7 gene of adult T-cell leukemia patients
Yeh, C.-H., Bellon, M., Pancewicz, J., & Nicot, C. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1601537113 · Cited by 102 · see citing works
MYC and therapy resistance in cancer: risks and opportunities
Donati, G., & Amati, B. B. (2022) · Molecular Oncology · doi:10.1002/1878-0261.13319 · Cited by 99 · see citing works
Ubiquitin–proteasome system and the role of its inhibitors in cancer therapy
Aliabadi, F., Sohrabi, B., Mostafavi, E., Pazoki–Toroudi, H., & Webster, T. J. (2021) · Open Biology · doi:10.1098/rsob.200390 · Cited by 100 · see citing works
F-box protein interactions with the hallmark pathways in cancer
Randle, S. J., & Laman, H. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.09.013 · Cited by 95 · see citing works
APOBEC-induced mutations and their cancer effect size in head and neck squamous cell carcinoma
Cannataro, V. L., Gaffney, S. G., Sasaki, T., Issaeva, N., Grewal, N., Grandis, J. R., Yarbrough, W. G., Burtness, B. A., Anderson, K. S., & Townsend, J. P. (2019) · Oncogene · doi:10.1038/s41388-018-0657-6 · Cited by 91 · see citing works
MYC Modulation around the CDK2/p27/SKP2 Axis
Hydbring, P., Castell, A., & Larsson, L. (2017) · Genes · doi:10.3390/genes8070174 · Cited by 90 · see citing works
LUBAC determines chemotherapy resistance in squamous cell lung cancer
Ruiz, E. J., Diefenbacher, M. E., Nelson, J. K., Sancho, R., Pucci, F., Chakraborty, A., Moreno, P., Annibaldi, A., Liccardi, G., Encheva, V., et al. (2019) · The Journal of Experimental Medicine · doi:10.1084/jem.20180742 · Cited by 90 · see citing works
Close, V., Close, W., Kugler, S. J., Reichenzeller, M., Yosifov, D. Y., Bloehdorn, J., Pan, L., Tausch, E., Westhoff, M., Döhner, H., et al. (2018) · Blood · doi:10.1182/blood-2018-09-874529 · Cited by 88 · see citing works
Takada, M., Zhang, W., Suzuki, A., Kuroda, T. S., Yu, Z., Inuzuka, H., Gao, D., Wan, L., Zhuang, M., Hu, L., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-1240 · Cited by 86 · see citing works
Liu, R., Gao, J., Yang, Y., Qiu, R., Zheng, Y., Huang, W., Zeng, Y., Hou, Y., Wang, S., Leng, S., et al. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky461 · Cited by 85 · see citing works
Cao, J., Ge, M., & Ling, Z. (2016) · Medicine · doi:10.1097/md.0000000000002496 · Cited by 83 · see citing works
Systematic characterization of mutations altering protein degradation in human cancers
Tokheim, C. J., Wang, X., Timms, R. T., Zhang, B., Mena, E. L., Wang, B., Chen, C., Ge, J., Chu, J., Zhang, W., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.020 · Cited by 82 · see citing works
Xu, J., Zhou, W., Yang, F., Chen, G., Li, H., Zhao, Y., Liu, P., Li, H., Tan, M., Xiong, X., et al. (2017) · Nature Communications · doi:10.1038/ncomms14002 · Cited by 82 · see citing works
Cell cycle‐dependent ubiquitylation and destruction of NDE1 by CDK5‐FBW7 regulates ciliary length
Maskey, D., Marlin, M. C., Kim, S., Kim, S., Ong, E., Li, G., & Tsiokas, L. (2015) · The EMBO Journal · doi:10.15252/embj.201490831 · Cited by 80 · see citing works
FBW7 suppression leads to SOX9 stabilization and increased malignancy in medulloblastoma
Rahmanto, A. S., Savov, V., Brunner, A., Bolin, S., Weishaupt, H., Malyukova, A., Rosén, G., Čančer, M., Hutter, S., Sundström, A., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201693889 · Cited by 78 · see citing works
LSD1 destabilizes FBXW7 and abrogates FBXW7 functions independent of its demethylase activity
Lan, H., Tan, M., Zhang, Q., Yang, F., Wang, S., Li, H., Xiong, X., & Sun, Y. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1902012116 · Cited by 78 · see citing works
Guarding the Genome: CENP-A-Chromatin in Health and Cancer
Mahlke, M. A., & Nechemia‐Arbely, Y. (2020) · Genes · doi:10.3390/genes11070810 · Cited by 80 · see citing works
Inactivation of Fbxw7 Impairs dsRNA Sensing and Confers Resistance to PD-1 Blockade
Gstalder, C., Liu, D., Miao, D., Lutterbach, B. A., DeVine, A. L., Lin, C., Shettigar, M., Pancholi, P., Buchbinder, E. I., Carter, S. L., et al. (2020) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-1416 · Cited by 73 · see citing works
PD-1 regulation in immune homeostasis and immunotherapy
Gao, M., Shi, J., Xiao, X., Yao, Y., Chen, X., Wang, B., & Zhang, J. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.216726 · Cited by 82 · see citing works
SCFFBW7-mediated degradation of Brg1 suppresses gastric cancer metastasis
Huang, L.-Y., Zhao, J., Chen, H., Wan, L., Inuzuka, H., Guo, J., Fu, X., Zhai, Y., Lu, Z., Wang, X., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06038-y · Cited by 75 · see citing works
C/EBPδ links IL-6 and HIF-1 signaling to promote breast cancer stem cell-associated phenotypes
Balamurugan, K., Mendoza-Villanueva, D., Sharan, S., Summers, G. H., Dobrolecki, L. E., Lewis, M. T., & Sterneck, E. (2018) · Oncogene · doi:10.1038/s41388-018-0516-5 · Cited by 74 · see citing works
Gorelik, M., Orlicky, S. M., Sartori, M. A., Tang, X., Marcon, E., Kurinov, I. V., Greenblatt, J. F., Tyers, M., Moffat, J., Sicheri, F., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1519389113 · Cited by 74 · see citing works
Mcl-1 inhibition overcomes intrinsic and acquired Regorafenib resistance in Colorectal Cancer
Song, X., Shen, L., Tong, J., Kuang, C., Zeng, S., Schoen, R. E., Yu, J., Pei, H., & Zhang, L. (2020) · Theranostics · doi:10.7150/thno.45363 · Cited by 72 · see citing works
Pseudophosphatases as Regulators of MAPK Signaling
Hepworth, E. M. W., & Hinton, S. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222212595 · Cited by 71 · see citing works
Dysregulation of ubiquitin ligases in cancer
Qi, J., & Ronai, Z. A. (2015) · Drug Resistance Updates · doi:10.1016/j.drup.2015.09.001 · Cited by 69 · see citing works
Regulation of the p53 Family Proteins by the Ubiquitin Proteasomal Pathway
Bang, S., Kaur, S., & Kurokawa, M. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms21010261 · Cited by 69 · see citing works
Lu, H., Yao, B., Wen, X., & Jia, B. (2019) · BMC Cancer · doi:10.1186/s12885-019-6028-z · Cited by 69 · see citing works
Liu, J., Wei, L., Hu, N., Wang, D., Ni, J., Zhang, S., Liu, H., Lv, T., Yin, J., Ye, M., et al. (2022) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2022-005116 · Cited by 67 · see citing works
E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses
Song, Y., Lai, L., Chong, Z., He, J., Zhang, Y., Xue, Y., Xie, Y., Chen, S., Dong, P., Chen, L., et al. (2017) · Nature Communications · doi:10.1038/ncomms14654 · Cited by 69 · see citing works
FBW7 -Dependent Mcl-1 Degradation Mediates the Anticancer Effect of Hsp90 Inhibitors
Tong, J., Tan, S., Nikolovska‐Coleska, Z., Yu, J., Zou, F., & Zhang, L. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0032 · Cited by 66 · see citing works
SOX9 is targeted for proteasomal degradation by the E3 ligase FBW7 in response to DNA damage
Hong, X., Liu, W., Song, R., Shah, J. J., Feng, X., Tsang, C. K., Morgan, K. M., Bunting, S. F., Inuzuka, H., Zheng, X., et al. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw748 · Cited by 64 · see citing works
Ubiquitin and Ubiquitin-like Proteins in Cancer, Neurodegenerative Disorders, and Heart Diseases
Hwang, J., Lee, A., & Kho, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23095053 · Cited by 62 · see citing works
METTL3-mediated m6A mRNA modification of FBXW7 suppresses lung adenocarcinoma
Wu, Y., Chang, N., Zhang, Y., Zhang, X., Xu, L., Che, Y., Qiao, T., Wu, B., Zhou, Y., Jiang, J., et al. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-01880-3 · Cited by 62 · see citing works
PRMT5-mediated arginine methylation stabilizes GPX4 to suppress ferroptosis in cancer
Fan, Y., Wang, Y., Dan, W., Zhang, Y., Nie, L., Ma, Z., Zhuang, Y., Liu, B., Li, M., Liu, T., et al. (2025) · Nature Cell Biology · doi:10.1038/s41556-025-01610-3 · Cited by 62 · see citing works
Novel Molecular Markers for Breast Cancer
Inoue, K., & Fry, E. A. (2016) · Biomarkers in Cancer · doi:10.4137/bic.s38394 · Cited by 61 · see citing works
Shao, J., Fan, G., Yin, X., Gu, Y., Wang, X., Xin, Y., & Yao, Y. (2019) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2019.110541 · Cited by 59 · see citing works
Fbxo4-mediated degradation of Fxr1 suppresses tumorigenesis in head and neck squamous cell carcinoma
Qie, S., Majumder, M., Mackiewicz, K., Howley, B. V., Peterson, Y. K., Howe, P. H., Palanisamy, V., & Diehl, J. A. (2017) · Nature Communications · doi:10.1038/s41467-017-01199-8 · Cited by 60 · see citing works
mTOR-targeted cancer therapy: great target but disappointing clinical outcomes, why?
Sun, S. (2020) · Frontiers of Medicine · doi:10.1007/s11684-020-0812-7 · Cited by 57 · see citing works
Deregulation of F-box proteins and its consequence on cancer development, progression and metastasis
Heo, J., Eki, R., & Abbas, T. (2015) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.09.015 · Cited by 58 · see citing works
CDK1 and CDK2 regulate NICD1 turnover and the periodicity of the segmentation clock
Carrieri, F. A., Murray, P. J., Ditsova, D., Ferris, M. A., Davies, P., & Dale, J. K. (2019) · EMBO Reports · doi:10.15252/embr.201846436 · Cited by 62 · see citing works
Two diphosphorylated degrons control c-Myc degradation by the Fbw7 tumor suppressor
Welcker, M., Wang, B., Rusnac, D.-V., Hussaini, Y., Swanger, J., Zheng, N., & Clurman, B. E. (2022) · Science Advances · doi:10.1126/sciadv.abl7872 · Cited by 57 · see citing works
Self-citationMyelinating Schwann cells ensheath multiple axons in the absence of E3 ligase component Fbxw7
Harty, B. L., Coelho, F. M., Pease-Raissi, S. E., Mogha, A., Ackerman, S. D., Herbert, A. L., Gereau, R. W., Golden, J. P., Lyons, D. A., Chan, J. R., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-10881-y · Cited by 58 · see citing works
Zhu, J., Li, Y., Chen, C., Ma, J., Sun, W., Tian, Z., Li, J., Xu, J., Liu, C. S., Zhang, D., et al. (2017) · Neoplasia · doi:10.1016/j.neo.2017.06.002 · Cited by 56 · see citing works
Bengoechea-Alonso, M. T., & Ericsson, J. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1220456 · Cited by 55 · see citing works
Cyclin E Deregulation and Genomic Instability
Teixeira, L. K., & Reed, S. I. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-6955-0_22 · Cited by 55 · see citing works
Ruiz, E. J., Pinto-Fernandez, A., Turnbull, A. P., Lan, L., Charlton, T. M., Scott, H. C., Damianou, A., Vere, G., Riising, E. M., Costa, C. D., et al. (2021) · eLife · doi:10.7554/elife.71596 · Cited by 54 · see citing works
Gallo, M. L., Lozy, F., & Bell, D. W. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-43139-0_5 · Cited by 54 · see citing works
Cheng, X., Yuan, H., Shu, W., Zhao, M., Zhao, C. N., Wu, Y., Peng, X.-D., Yao, P.-F., Xiao, D., Qing, G., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.778001 · Cited by 54 · see citing works
PAM forms an atypical SCF ubiquitin ligase complex that ubiquitinates and degrades NMNAT2
Desbois, M., Crawley, O., Evans, P. R., Baker, S. T., Masuho, I., Yasuda, R., & Grill, B. J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002176 · Cited by 50 · see citing works
Control of mTOR Signaling by Ubiquitin
Jiang, Y., Su, S.-Y., Zhang, Y.-Q., Qian, J.-Y., & Liu, P.-D. (2019) · Oncogene · doi:10.1038/s41388-019-0713-x · Cited by 46 · see citing works
Deciphering and Targeting Oncogenic Mutations and Pathways in Breast Cancer
Santarpia, L., Bottai, G., Kelly, C. M., Győrffy, B., Székely, B., & Pusztai, L. (2016) · The Oncologist · doi:10.1634/theoncologist.2015-0369 · Cited by 51 · see citing works
Zhang, B., Liu, Q., Wen, W., Gao, H., Wei, W., Tang, A., Qin, B., Lyu, H., Meng, X., Li, K., et al. (2022) · Cell Discovery · doi:10.1038/s41421-022-00478-z · Cited by 50 · see citing works
Wang, J., Li, T., & Wang, B. (2021) · International Journal of Oncology · doi:10.3892/ijo.2021.5244 · Cited by 49 · see citing works
Hepatic F-Box Protein FBXW7 Maintains Glucose Homeostasis Through Degradation of Fetuin-A
Zhao, J., Xiong, X., Li, Y., Liu, X., Wang, T., Zhang, H., Jiao, Y., Jiang, J., Zhang, H., Tang, Q., et al. (2018) · Diabetes · doi:10.2337/db17-1348 · Cited by 47 · see citing works
Prevention of cancer dormancy by Fbxw7 ablation eradicates disseminated tumor cells
Shimizu, H., Takeishi, S., Nakatsumi, H., & Nakayama, K. I. (2019) · JCI Insight · doi:10.1172/jci.insight.125138 · Cited by 50 · see citing works
NOTCH2 Hajdu-Cheney Mutations Escape SCFFBW7-Dependent Proteolysis to Promote Osteoporosis
Fukushima, H., Shimizu, K., Watahiki, A., Hoshikawa, S., Kosho, T., Oba, D., Sakano, S., Arakaki, M., Yamada, A., Nagashima, K., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.018 · Cited by 46 · see citing works
Xi, Z., Mu, Y., Li, Y., Xie, C., Holst, J., Liu, T., Cai, S., Lao, Y., Tan, H., Xu, H., et al. (2016) · Cell Death and Disease · doi:10.1038/cddis.2016.123 · Cited by 46 · see citing works
FBXO45-MYCBP2 regulates mitotic cell fate by targeting FBXW7 for degradation
Richter, K. T., Kschonsak, Y. T., Vodicska, B., & Hoffmann, I. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0385-7 · Cited by 44 · see citing works
Disease Association and Druggability of WD40 Repeat Proteins
Song, R., Wang, Z.-D., & Schapira, M. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00451 · Cited by 45 · see citing works
FBXW7-mutated colorectal cancer cells exhibit aberrant expression of phosphorylated-p53 at Serine-15
Li, N., Lorenzi, F., Kalakouti, E., Normatova, M., Babaei‐Jadidi, R., Tomlinson, I. P. M., & Nateri, A. S. (2015) · Oncotarget · doi:10.18632/oncotarget.3284 · Cited by 43 · see citing works
ΔNp63/DGCR8-Dependent MicroRNAs Mediate Therapeutic Efficacy of HDAC Inhibitors in Cancer
Napoli, M., Venkatanarayan, A., Raulji, P., Meyers, B. A., Norton, W., Mangala, L. S., Sood, A. K., Rodriguez‐Aguayo, C., Lopez‐Berestein, G., Vin, H., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2016.04.016 · Cited by 45 · see citing works
The pseudophosphatase STYX targets the F‐box of FBXW7 and inhibits SCFFBXW7 function
Reiterer, V., Figueras-Puig, C., Guerroué, F. L., Confalonieri, S., Vecchi, M., Jalapothu, D., Kanse, S. M., Deshaies, R. J., Fiore, P. P. D., Behrends, C., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201694795 · Cited by 45 · see citing works
RNF4—A Paradigm for SUMOylation‐Mediated Ubiquitination
Kumar, R., & Sabapathy, K. (2019) · PROTEOMICS · doi:10.1002/pmic.201900185 · Cited by 44 · see citing works
Fbxw7 Deletion Accelerates KrasG12D-Driven Pancreatic Tumorigenesis via Yap Accumulation
Zhang, Q., Zhang, Y., Parsels, J. D., Lohse, I., Lawrence, T. S., di Magliano, M. P., Sun, Y., & Morgan, M. A. (2016) · Neoplasia · doi:10.1016/j.neo.2016.08.009 · Cited by 44 · see citing works
Skp2 stabilizes Mcl-1 and confers radioresistance in colorectal cancer
Yu, X., Zhou, L. Q., Liu, W., Liu, L., Gao, F., Li, W., & Liu, H. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04685-0 · Cited by 43 · see citing works
Davis, R. J., Gönen, M., Margineantu, D. H., Handeli, S., Swanger, J., Hoellerbauer, P., Paddison, P. J., Gu, H., Raftery, D., Grim, J. E., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718338115 · Cited by 43 · see citing works
Self-citationAtypical APC/C‐dependent degradation of Mcl‐1 provides an apoptotic timer during mitotic arrest
Allan, L. A., Skowyra, A., Rogers, K. I., Zeller, D., & Clarke, P. R. (2018) · The EMBO Journal · doi:10.15252/embj.201796831 · Cited by 43 · see citing works
Parker, D. J., Iyer, A. P., Shah, S., Moran, A., Hjelmeland, A. B., Basu, M. K., Liu, R., & Mitra, K. (2015) · Journal of Cell Science · doi:10.1242/jcs.172429 · Cited by 42 · see citing works
Lee, Y. S., Jung, Y. Y., Park, M. H., Yeo, I. J., Im, H. S., Nam, K. T., Kim, H. D., Kang, S. K., Song, J. K., Kim, Y. R., et al. (2018) · Cancer Letters · doi:10.1016/j.canlet.2018.07.007 · Cited by 42 · see citing works
A structural view of PA2G4 isoforms with opposing functions in cancer
Stevenson, B. W., Gorman, M. A., Koach, J., Cheung, B. B., Marshall, G. M., Parker, M. W., & Holien, J. K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.014293 · Cited by 41 · see citing works
Wang, Y., Shi, S., Wang, Y., Zhang, X., Liu, X., Li, J., Li, P., Du, L., & Wang, C. (2021) · Thoracic Cancer · doi:10.1111/1759-7714.14284 · Cited by 39 · see citing works
Zhang, Q., Mady, A. S. A., Ma, Y., Ryan, C., Lawrence, T. S., Nikolovska‐Coleska, Z., Sun, Y., & Morgan, M. A. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz058 · Cited by 41 · see citing works
- Authors
- Davis, R. J., Welcker, M., & Clurman, B. E.
- Affiliations
- University of Washington (US)
- Fred Hutch Cancer Center (US)
- Corresponding author
- Clurman, Bruce E.
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2014-10
- Volume
- 26
- Issue
- 4
- Pages
- 455-464
- ISSN
- 1535-6108 (ISSN-L)
- PMC
- PMC4227608
- OpenAlex
- W2055874017
- Cited by
- 343
- References
- 103
- Citations by year
- 2026: 15 · 2025: 18 · 2024: 14 · 2023: 22 · 2022: 28 · 2021: 36 · 2020: 32 · 2019: 46 · 2018: 31 · 2017: 39 · 2016: 35 · 2015: 24 · 2014: 2
- FWCI
- 3.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cancer Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Science Foundation
- National Institutes of Health
- National Cancer Institute (CA084069, R01CA084069, R01CA178143, CA102742, R01CA102742)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Degradation and Inhibitors
- Keywords
- FBXW7, SCF ubiquitin ligase, tumor suppression, protein degradation, FBXW7 mutation, carcinogenesis
- MeSH terms
- F-Box-WD Repeat-Containing Protein 7, Humans, Mutation, Neoplasms, Genes, Tumor Suppressor, Cell Cycle Proteins, Ubiquitin-Protein Ligases, F-Box Proteins
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