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Die Highlights vom Kongress des American College of Cardiology 2024

Im April diskutierten die Herz-Kreislauf-Spezialisten aus der ganzen Welt auf dem  Kongress des American College of Cardiology (ACC) u.a. neue Therapieansätze bei akutem Myokardinfarkt, koronarer Herzerkrankung, kardiogenem Schock oder Aortenklappenstenose. In unserem Kongress-Dossier haben wir für Sie Berichte über die „Late-Breaking Trials“ und andere wichtige Studien zusammengestellt. 
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Cancer and Metastasis Reviews
Erschienen in: Cancer and Metastasis Reviews 1-2/2012

01.06.2012 | NON-THEMATIC REVIEW

Role of the ubiquitin ligase Fbw7 in cancer progression

verfasst von: Yabin Cheng, Gang Li

Erschienen in: Cancer and Metastasis Reviews | Ausgabe 1-2/2012

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Abstract

Fbw7 is a member of F-box family proteins, which constitute one subunit of Skp1, Cul1, and F-box protein (SCF) ubiquitin ligase complex. SCFFbw7 targets a set of well-known oncoproteins, including c-Myc, cyclin E, Notch, c-Jun, and Mcl-1, for ubiquitylation and degradation. Fbw7 provides specificity of the ubiquitylation of these substrate proteins via recognition of a consensus phosphorylated degron. Through regulation of several important proteins, Fbw7 controls diverse cellular processes, including cell-cycle progression, cell proliferation, differentiation, DNA damage response, maintenance of genomic stability, and neural cell stemness. As reduced Fbw7 expression level and loss-of-function mutations are found in a wide range of human cancers, Fbw7 is generally considered as a tumor suppressor. However, the exact mechanisms underlying Fbw7-induced tumor suppression is unclear. This review focuses on regulation network, biological functions, and genetic alteration of Fbw7 in connection with its role in cancer development.
Literatur
1.
Crusio, K. M., King, B., Reavie, L. B., & Aifantis, I. (2010). The ubiquitous nature of cancer: the role of the SCF(Fbw7) complex in development and transformation. Oncogene, 29, 4865–4873.PubMedCrossRef
2.
Hershko, A. (1983). Ubiquitin: roles in protein modification and breakdown. Cell, 34, 11–12.PubMedCrossRef
3.
Schwartz, A. L., & Ciechanover, A. (2009). Targeting proteins for destruction by the ubiquitin system: implications for human pathobiology. Annual Review of Pharmacology and Toxicology, 49, 73–96.PubMedCrossRef
4.
Welcker, M., & Clurman, B. E. (2008). FBW7 ubiquitin ligase: a tumour suppressor at the crossroads of cell division, growth and differentiation. Nature Reviews. Cancer, 8, 83–93.PubMedCrossRef
5.
Yada, M., Hatakeyama, S., Kamura, T., et al. (2004). Phosphorylation-dependent degradation of c-Myc is mediated by the F-box protein Fbw7. The EMBO Journal, 23, 2116–2125.PubMedCrossRef
6.
Strohmaier, H., Spruck, C. H., Kaiser, P., et al. (2001). Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature, 413, 316–322.PubMedCrossRef
7.
Nateri, A. S., Riera-Sans, L., Da Costa, C., & Behrens, A. (2004). The ubiquitin ligase SCFFbw7 antagonizes apoptotic JNK signaling. Science, 303, 1374–1378.PubMedCrossRef
8.
Oberg, C., Li, J., Pauley, A., et al. (2001). The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog. Journal of Biological Chemistry, 276, 35847–35853.PubMedCrossRef
9.
Inuzuka, H., Shaik, S., Onoyama, I., et al. (2011). SCF(FBW7) regulates cellular apoptosis by targeting MCL1 for ubiquitylation and destruction. Nature, 471, 104–109.PubMedCrossRef
10.
Mao, J. H., Kim, I. J., Wu, D., et al. (2008). FBXW7 targets mTOR for degradation and cooperates with PTEN in tumor suppression. Science, 321, 1499–1502.PubMedCrossRef
11.
Tan, Y., Sangfelt, O., & Spruck, C. (2008). The Fbxw7/hCdc4 tumor suppressor in human cancer. Cancer Letters, 271, 1–12.PubMedCrossRef
12.
Maser, R. S., Choudhury, B., Campbell, P. J., et al. (2007). Chromosomally unstable mouse tumours have genomic alterations similar to diverse human cancers. Nature, 447, 966–971.PubMedCrossRef
13.
Mao, J. H., Perez-Losada, J., Wu, D., et al. (2004). Fbxw7/Cdc4 is a p53-dependent, haploinsufficient tumour suppressor gene. Nature, 432, 775–779.PubMedCrossRef
14.
Matsuoka, S., Oike, Y., Onoyama, I., et al. (2008). Fbxw7 acts as a critical fail-safe against premature loss of hematopoietic stem cells and development of T-ALL. Genes & Development, 22, 986–991.CrossRef
15.
Moberg, K. H., Bell, D. W., Wahrer, D. C., Haber, D. A., & Hariharan, I. K. (2001). Archipelago regulates cyclin E levels in Drosophila and is mutated in human cancer cell lines. Nature, 413, 311–316.PubMedCrossRef
16.
Kemp, Z., Rowan, A., Chambers, W., et al. (2005). CDC4 mutations occur in a subset of colorectal cancers but are not predicted to cause loss of function and are not associated with chromosomal instability. Cancer Research, 65, 11361–11366.PubMedCrossRef
17.
Calhoun, E. S., Jones, J. B., Ashfaq, R., et al. (2003). BRAF and FBXW7 (CDC4, FBW7, AGO, SEL10) mutations in distinct subsets of pancreatic cancer: potential therapeutic targets. American Journal of Pathology, 163, 1255–1260.PubMedCrossRef
18.
Akhoondi, S., Sun, D., von der Lehr, N., et al. (2007). FBXW7/hCDC4 is a general tumor suppressor in human cancer. Cancer Research, 67, 9006–9012.PubMedCrossRef
19.
Skaar, J. R., Pagan, J. K., & Pagano, M. (2009). SnapShot: F box proteins I. Cell, 137(1160–1160), e1161.
20.
Skaar, J. R., D’Angiolella, V., Pagan, J. K., & Pagano, M. (2009). SnapShot: F box proteins II. Cell, 137, 1358. 1358.e1.
21.
Ho, M. S., Tsai, P. I., & Chien, C. T. (2006). F-box proteins: the key to protein degradation. Journal of Biomedical Science, 13, 181–191.PubMedCrossRef
22.
Skowyra, D., Craig, K. L., Tyers, M., Elledge, S. J., & Harper, J. W. (1997). F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin–ligase complex. Cell, 91, 209–219.PubMedCrossRef
23.
Spruck, C. H., Strohmaier, H., Sangfelt, O., et al. (2002). hCDC4 gene mutations in endometrial cancer. Cancer Research, 62, 4535–4539.PubMed
24.
Grim, J. E., Gustafson, M. P., Hirata, R. K., et al. (2008). Isoform- and cell cycle-dependent substrate degradation by the Fbw7 ubiquitin ligase. The Journal of Cell Biology, 181, 913–920.PubMedCrossRef
25.
Matsumoto, A., Tateishi, Y., Onoyama, I., et al. (2011). Fbxw7beta resides in the endoplasmic reticulum membrane and protects cells from oxidative stress. Cancer Science, 102, 749–755.PubMedCrossRef
26.
Welcker, M., Orian, A., Grim, J. E., Eisenman, R. N., & Clurman, B. E. (2004). A nucleolar isoform of the Fbw7 ubiquitin ligase regulates c-Myc and cell size. Current Biology, 14, 1852–1857.PubMedCrossRef
27.
Zhang, W., & Koepp, D. M. (2006). Fbw7 isoform interaction contributes to cyclin E proteolysis. Molecular Cancer Research, 4, 935–943.PubMedCrossRef
28.
Bai, C., Sen, P., Hofmann, K., et al. (1996). SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box. Cell, 86, 263–274.PubMedCrossRef
29.
Perkins, G., Drury, L. S., & Diffley, J. F. (2001). Separate SCF(CDC4) recognition elements target Cdc6 for proteolysis in S phase and mitosis. The EMBO Journal, 20, 4836–4845.PubMedCrossRef
30.
Orlicky, S., Tang, X., Willems, A., Tyers, M., & Sicheri, F. (2003). Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase. Cell, 112, 243–256.PubMedCrossRef
31.
Hao, B., Oehlmann, S., Sowa, M. E., Harper, J. W., & Pavletich, N. P. (2007). Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases. Molecular Cell, 26, 131–143.PubMedCrossRef
32.
Nash, P., Tang, X., Orlicky, S., et al. (2001). Multisite phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature, 414, 514–521.PubMedCrossRef
33.
Welcker, M., & Clurman, B. E. (2007). Fbw7/hCDC4 dimerization regulates its substrate interactions. Cell Div, 2, 7.PubMedCrossRef
34.
Tang, X., Orlicky, S., Lin, Z., et al. (2007). Suprafacial orientation of the SCFCdc4 dimer accommodates multiple geometries for substrate ubiquitination. Cell, 129, 1165–1176.PubMedCrossRef
35.
Pawar, S. A., Sarkar, T. R., Balamurugan, K., et al. (2010). C/EBP{delta} targets cyclin D1 for proteasome-mediated degradation via induction of CDC27/APC3 expression. Proceedings of the National Academy of Sciences of the United States of America, 107, 9210–9215.PubMedCrossRef
36.
Balamurugan, K., Wang, J. M., Tsai, H. H., et al. (2010). The tumour suppressor C/EBPdelta inhibits FBXW7 expression and promotes mammary tumour metastasis. The EMBO Journal, 29, 4106–4117.PubMedCrossRef
37.
Strimpakos, A. S., Karapanagiotou, E. M., Saif, M. W., & Syrigos, K. N. (2009). The role of mTOR in the management of solid tumors: an overview. Cancer Treatment Reviews, 35, 148–159.PubMedCrossRef
38.
Isobe, T., Hattori, T., Kitagawa, K., et al. (2009). Adenovirus E1A inhibits SCF(Fbw7) ubiquitin ligase. Journal of Biological Chemistry, 284, 27766–27779.PubMedCrossRef
39.
Koo, E. H., & Kopan, R. (2004). Potential role of presenilin-regulated signaling pathways in sporadic neurodegeneration. Nature Medicine, 10(Suppl), S26–S33.PubMedCrossRef
40.
De Strooper, B., Annaert, W., Cupers, P., et al. (1999). A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain. Nature, 398, 518–522.PubMedCrossRef
41.
Rocher-Ros, V., Marco, S., Mao, J. H., et al. (2010). Presenilin modulates EGFR signaling and cell transformation by regulating the ubiquitin ligase Fbw7. Oncogene, 29, 2950–2961.PubMedCrossRef
42.
Kim, J., & Bartel, D. P. (2009). Allelic imbalance sequencing reveals that single-nucleotide polymorphisms frequently alter microRNA-directed repression. Nature Biotechnology, 27, 472–477.PubMedCrossRef
43.
Xu, Y., Sengupta, T., Kukreja, L., & Minella, A. C. (2010). MicroRNA-223 regulates cyclin E activity by modulating expression of F-box and WD-40 domain protein 7. Journal of Biological Chemistry, 285, 34439–34446.PubMedCrossRef
44.
Lerner, M., Lundgren, J., Akhoondi, S., et al. (2011). MiRNA-27a controls FBW7/hCDC4-dependent cyclin E degradation and cell cycle progression. Cell Cycle, 10, 2172–2183.PubMedCrossRef
45.
Mo, J. S., Ann, E. J., Yoon, J. H., et al. (2011). Serum- and glucocorticoid-inducible kinase 1 (SGK1) controls Notch1 signaling by downregulation of protein stability through Fbw7 ubiquitin ligase. Journal of Cell Science, 124, 100–112.PubMedCrossRef
46.
BelAiba, R. S., Djordjevic, T., Bonello, S., et al. (2006). The serum- and glucocorticoid-inducible kinase Sgk-1 is involved in pulmonary vascular remodeling: role in redox-sensitive regulation of tissue factor by thrombin. Circulation Research, 98, 828–836.PubMedCrossRef
47.
Kinugawa, K., Yonekura, K., Ribeiro, R. C., et al. (2001). Regulation of thyroid hormone receptor isoforms in physiological and pathological cardiac hypertrophy. Circulation Research, 89, 591–598.PubMedCrossRef
48.
Schulein, C., Eilers, M., & Popov, N. (2011). PI3K-dependent phosphorylation of Fbw7 modulates substrate degradation and activity. FEBS Letters, 585, 2151–2157.PubMedCrossRef
49.
Durgan, J., & Parker, P. J. (2010). Regulation of the tumour suppressor Fbw7alpha by PKC-dependent phosphorylation and cancer-associated mutations. Biochemistry Journal, 432, 77–87.CrossRef
50.
Evans, T., Rosenthal, E. T., Youngblom, J., Distel, D., & Hunt, T. (1983). Cyclin: a protein specified by maternal mRNA in sea urchin eggs that is destroyed at each cleavage division. Cell, 33, 389–396.PubMedCrossRef
51.
Harper, J. W., Burton, J. L., & Solomon, M. J. (2002). The anaphase-promoting complex: it’s not just for mitosis any more. Genes & Development, 16, 2179–2206.CrossRef
52.
Castro, A., Bernis, C., Vigneron, S., Labbe, J. C., & Lorca, T. (2005). The anaphase-promoting complex: a key factor in the regulation of cell cycle. Oncogene, 24, 314–325.PubMedCrossRef
53.
Nakayama, K. I., & Nakayama, K. (2006). Ubiquitin ligases: cell-cycle control and cancer. Nature Reviews. Cancer, 6, 369–381.PubMedCrossRef
54.
Hartwell, L. H., Mortimer, R. K., Culotti, J., & Culotti, M. (1973). Genetic control of the cell division cycle in yeast: V. Genetic Analysis of cdc Mutants. Genetics, 74, 267–286.
55.
Hubbard, E. J., Wu, G., Kitajewski, J., & Greenwald, I. (1997). sel-10, a negative regulator of lin-12 activity in Caenorhabditis elegans, encodes a member of the CDC4 family of proteins. Genes & Development, 11, 3182–3193.CrossRef
56.
Koepp, D. M., Schaefer, L. K., Ye, X., et al. (2001). Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. Science, 294, 173–177.PubMedCrossRef
57.
Welcker, M., Orian, A., Jin, J., et al. (2004). The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation. Proceedings of the National Academy of Sciences of the United States of America, 101, 9085–9090.PubMedCrossRef
58.
Wei, W., Jin, J., Schlisio, S., Harper, J. W., & Kaelin, W. G., Jr. (2005). The v-Jun point mutation allows c-Jun to escape GSK3-dependent recognition and destruction by the Fbw7 ubiquitin ligase. Cancer Cell, 8, 25–33.PubMedCrossRef
59.
Ishikawa, Y., Onoyama, I., Nakayama, K. I., & Nakayama, K. (2008). Notch-dependent cell cycle arrest and apoptosis in mouse embryonic fibroblasts lacking Fbxw7. Oncogene, 27, 6164–6174.PubMedCrossRef
60.
Zhao, D., Zheng, H. Q., Zhou, Z., & Chen, C. (2010). The Fbw7 tumor suppressor targets KLF5 for ubiquitin-mediated degradation and suppresses breast cell proliferation. Cancer Research, 70, 4728–4738.PubMedCrossRef
61.
Clurman, B. E., Sheaff, R. J., Thress, K., Groudine, M., & Roberts, J. M. (1996). Turnover of cyclin E by the ubiquitin-proteasome pathway is regulated by cdk2 binding and cyclin phosphorylation. Genes & Development, 10, 1979–1990.CrossRef
62.
Won, K. A., & Reed, S. I. (1996). Activation of cyclin E/CDK2 is coupled to site-specific autophosphorylation and ubiquitin-dependent degradation of cyclin E. The EMBO Journal, 15, 4182–4193.PubMed
63.
Spruck, C. H., Won, K. A., & Reed, S. I. (1999). Deregulated cyclin E induces chromosome instability. Nature, 401, 297–300.PubMedCrossRef
64.
Minella, A. C., Grim, J. E., Welcker, M., & Clurman, B. E. (2007). p53 and SCFFbw7 cooperatively restrain cyclin E-associated genome instability. Oncogene, 26, 6948–6953.PubMedCrossRef
65.
Ye, X., Nalepa, G., Welcker, M., et al. (2004). Recognition of phosphodegron motifs in human cyclin E by the SCF(Fbw7) ubiquitin ligase. Journal of Biological Chemistry, 279, 50110–50119.PubMedCrossRef
66.
Eilers, M., Schirm, S., & Bishop, J. M. (1991). The MYC protein activates transcription of the alpha-prothymosin gene. The EMBO Journal, 10, 133–141.PubMed
67.
Bahram, F., von der Lehr, N., Cetinkaya, C., & Larsson, L. G. (2000). c-Myc hot spot mutations in lymphomas result in inefficient ubiquitination and decreased proteasome-mediated turnover. Blood, 95, 2104–2110.PubMed
68.
Grandori, C., Cowley, S. M., James, L. P., & Eisenman, R. N. (2000). The Myc/Max/Mad network and the transcriptional control of cell behavior. Annual Review of Cell and Developmental Biology, 16, 653–699.PubMedCrossRef
69.
Adhikary, S., & Eilers, M. (2005). Transcriptional regulation and transformation by Myc proteins. Nature Reviews Molecular Cell Biology, 6, 635–645.PubMedCrossRef
70.
Hann, S. R., & Eisenman, R. N. (1984). Proteins encoded by the human c-myc oncogene: differential expression in neoplastic cells. Molecular and Cellular Biology, 4, 2486–2497.PubMed
71.
Amati, B. (2004). Myc degradation: dancing with ubiquitin ligases. Proceedings of the National Academy of Sciences of the United States of America, 101, 8843–8844.PubMedCrossRef
72.
Salghetti, S. E., Muratani, M., Wijnen, H., Futcher, B., & Tansey, W. P. (2000). Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis. Proceedings of the National Academy of Sciences of the United States of America, 97, 3118–3123.PubMedCrossRef
73.
Flinn, E. M., Busch, C. M., & Wright, A. P. (1998). myc boxes, which are conserved in myc family proteins, are signals for protein degradation via the proteasome. Molecular and Cellular Biology, 18, 5961–5969.PubMed
74.
Sears, R., Nuckolls, F., Haura, E., et al. (2000). Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability. Genes & Development, 14, 2501–2514.CrossRef
75.
Popov, N., Schulein, C., Jaenicke, L. A., & Eilers, M. (2010). Ubiquitylation of the amino terminus of Myc by SCF(beta-TrCP) antagonizes SCF(Fbw7)-mediated turnover. Nature Cell Biology, 12, 973–981.PubMedCrossRef
76.
Hartl, M., Bader, A. G., & Bister, K. (2003). Molecular targets of the oncogenic transcription factor jun. Current Cancer Drug Targets, 3, 41–55.PubMedCrossRef
77.
Behrens, A., Sibilia, M., & Wagner, E. F. (1999). Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation. Nature Genetics, 21, 326–329.PubMedCrossRef
78.
Shaulian, E., Schreiber, M., Piu, F., et al. (2000). The mammalian UV response: c-Jun induction is required for exit from p53-imposed growth arrest. Cell, 103, 897–907.PubMedCrossRef
79.
Szabowski, A., Maas-Szabowski, N., Andrecht, S., et al. (2000). c-Jun and JunB antagonistically control cytokine-regulated mesenchymal–epidermal interaction in skin. Cell, 103, 745–755.PubMedCrossRef
80.
Fuchs, S. Y., Xie, B., Adler, V., et al. (1997). c-Jun NH2-terminal kinases target the ubiquitination of their associated transcription factors. Journal of Biological Chemistry, 272, 32163–32168.PubMedCrossRef
81.
Musti, A. M., Treier, M., & Bohmann, D. (1997). Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases. Science, 275, 400–402.PubMedCrossRef
82.
Radtke, F., Schweisguth, F., & Pear, W. (2005). The Notch ‘gospel’. EMBO Reports, 6, 1120–1125.PubMedCrossRef
83.
Artavanis-Tsakonas, S., Rand, M. D., & Lake, R. J. (1999). Notch signaling: cell fate control and signal integration in development. Science, 284, 770–776.PubMedCrossRef
84.
Demarest, R. M., Ratti, F., & Capobianco, A. J. (2008). It’s T-ALL about Notch. Oncogene, 27, 5082–5091.PubMedCrossRef
85.
Radtke, F., Wilson, A., Mancini, S. J., & MacDonald, H. R. (2004). Notch regulation of lymphocyte development and function. Nature Immunology, 5, 247–253.PubMedCrossRef
86.
Gupta-Rossi, N., Le Bail, O., Gonen, H., et al. (2001). Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor. Journal of Biological Chemistry, 276, 34371–34378.PubMedCrossRef
87.
Wu, G., Lyapina, S., Das, I., et al. (2001). SEL-10 is an inhibitor of notch signaling that targets notch for ubiquitin-mediated protein degradation. Molecular and Cellular Biology, 21, 7403–7415.PubMedCrossRef
88.
Wu, G., Hubbard, E. J., Kitajewski, J. K., & Greenwald, I. (1998). Evidence for functional and physical association between Caenorhabditis elegans SEL-10, a Cdc4p-related protein, and SEL-12 presenilin. Proceedings of the National Academy of Sciences of the United States of America, 95, 15787–15791.PubMedCrossRef
89.
Fryer, C. J., White, J. B., & Jones, K. A. (2004). Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover. Molecular Cell, 16, 509–520.PubMedCrossRef
90.
O’Neil, J., Grim, J., Strack, P., et al. (2007). FBW7 mutations in leukemic cells mediate NOTCH pathway activation and resistance to gamma-secretase inhibitors. The Journal of Experimental Medicine, 204, 1813–1824.PubMedCrossRef
91.
Thompson, B. J., Buonamici, S., Sulis, M. L., et al. (2007). The SCFFBW7 ubiquitin ligase complex as a tumor suppressor in T cell leukemia. The Journal of Experimental Medicine, 204, 1825–1835.PubMedCrossRef
92.
Weng, A. P., Ferrando, A. A., Lee, W., et al. (2004). Activating mutations of NOTCH1 in human T cell acute lymphoblastic leukemia. Science, 306, 269–271.PubMedCrossRef
93.
Girard, L., Hanna, Z., Beaulieu, N., et al. (1996). Frequent provirus insertional mutagenesis of Notch1 in thymomas of MMTVD/myc transgenic mice suggests a collaboration of c-myc and Notch1 for oncogenesis. Genes & Development, 10, 1930–1944.CrossRef
94.
Feldman, B. J., Hampton, T., & Cleary, M. L. (2000). A carboxy-terminal deletion mutant of Notch1 accelerates lymphoid oncogenesis in E2A-PBX1 transgenic mice. Blood, 96, 1906–1913.PubMed
95.
Beverly, L. J., & Capobianco, A. J. (2003). Perturbation of Ikaros isoform selection by MLV integration is a cooperative event in Notch(IC)-induced T cell leukemogenesis. Cancer Cell, 3, 551–564.PubMedCrossRef
96.
Rohn, J. L., Lauring, A. S., Linenberger, M. L., & Overbaugh, J. (1996). Transduction of Notch2 in feline leukemia virus-induced thymic lymphoma. Journal of Virology, 70, 8071–8080.PubMed
97.
Yan, X. Q., Sarmiento, U., Sun, Y., et al. (2001). A novel Notch ligand, Dll4, induces T-cell leukemia/lymphoma when overexpressed in mice by retroviral-mediated gene transfer. Blood, 98, 3793–3799.PubMedCrossRef
98.
Dorsch, M., Zheng, G., Yowe, D., et al. (2002). Ectopic expression of Delta4 impairs hematopoietic development and leads to lymphoproliferative disease. Blood, 100, 2046–2055.PubMed
99.
Kuiperij, H. B., van der Horst, A., Raaijmakers, J., et al. (2005). Activation of FoxO transcription factors contributes to the antiproliferative effect of cAMP. Oncogene, 24, 2087–2095.PubMedCrossRef
100.
Fan, X., Matsui, W., Khaki, L., et al. (2006). Notch pathway inhibition depletes stem-like cells and blocks engraftment in embryonal brain tumors. Cancer Research, 66, 7445–7452.PubMedCrossRef
101.
Fernandez-Majada, V., Aguilera, C., Villanueva, A., et al. (2007). Nuclear IKK activity leads to dysregulated notch-dependent gene expression in colorectal cancer. Proceedings of the National Academy of Sciences of the United States of America, 104, 276–281.PubMedCrossRef
102.
Moriyama, M., Osawa, M., Mak, S. S., et al. (2006). Notch signaling via Hes1 transcription factor maintains survival of melanoblasts and melanocyte stem cells. The Journal of Cell Biology, 173, 333–339.PubMedCrossRef
103.
Miyamoto, Y., Maitra, A., Ghosh, B., et al. (2003). Notch mediates TGF alpha-induced changes in epithelial differentiation during pancreatic tumorigenesis. Cancer Cell, 3, 565–576.PubMedCrossRef
104.
Sriuranpong, V., Borges, M. W., Ravi, R. K., et al. (2001). Notch signaling induces cell cycle arrest in small cell lung cancer cells. Cancer Research, 61, 3200–3205.PubMed
105.
Nicolas, M., Wolfer, A., Raj, K., et al. (2003). Notch1 functions as a tumor suppressor in mouse skin. Nature Genetics, 33, 416–421.PubMedCrossRef
106.
Qi, R., An, H., Yu, Y., et al. (2003). Notch1 signaling inhibits growth of human hepatocellular carcinoma through induction of cell cycle arrest and apoptosis. Cancer Research, 63, 8323–8329.PubMed
107.
Nguyen, B. C., Lefort, K., Mandinova, A., et al. (2006). Cross-regulation between Notch and p63 in keratinocyte commitment to differentiation. Genes & Development, 20, 1028–1042.CrossRef
108.
Onoyama, I., Tsunematsu, R., Matsumoto, A., et al. (2007). Conditional inactivation of Fbxw7 impairs cell-cycle exit during T cell differentiation and results in lymphomatogenesis. The Journal of Experimental Medicine, 204, 2875–2888.PubMedCrossRef
109.
Liu, Y., Wen, J. K., Dong, L. H., Zheng, B., & Han, M. (2010). Kruppel-like factor (KLF) 5 mediates cyclin D1 expression and cell proliferation via interaction with c-Jun in Ang II-induced VSMCs. Acta Pharmacologica Sinica, 31, 10–18.PubMedCrossRef
110.
Nandan, M. O., Chanchevalap, S., Dalton, W. B., & Yang, V. W. (2005). Kruppel-like factor 5 promotes mitosis by activating the cyclin B1/Cdc2 complex during oncogenic Ras-mediated transformation. FEBS Letters, 579, 4757–4762.PubMedCrossRef
111.
Chen, C., Benjamin, M. S., Sun, X., et al. (2006). KLF5 promotes cell proliferation and tumorigenesis through gene regulation and the TSU-Pr1 human bladder cancer cell line. International Journal of Cancer, 118, 1346–1355.CrossRef
112.
Zheng, H. Q., Zhou, Z., Huang, J., et al. (2009). Kruppel-like factor 5 promotes breast cell proliferation partially through upregulating the transcription of fibroblast growth factor binding protein 1. Oncogene, 28, 3702–3713.PubMedCrossRef
113.
Yagi, N., Manabe, I., Tottori, T., et al. (2009). A nanoparticle system specifically designed to deliver short interfering RNA inhibits tumor growth in vivo. Cancer Research, 69, 6531–6538.PubMedCrossRef
114.
Chen, C., Zhou, Z., Guo, P., & Dong, J. T. (2007). Proteasomal degradation of the KLF5 transcription factor through a ubiquitin-independent pathway. FEBS Letters, 581, 1124–1130.PubMedCrossRef
115.
Oh, I. H., & Reddy, E. P. (1999). The myb gene family in cell growth, differentiation and apoptosis. Oncogene, 18, 3017–3033.PubMedCrossRef
116.
Slamon, D. J., Boone, T. C., Murdock, D. C., et al. (1986). Studies of the human c-myb gene and its product in human acute leukemias. Science, 233, 347–351.PubMedCrossRef
117.
Siegert, W., Beutler, C., Langmach, K., Keitel, C., & Schmidt, C. A. (1990). Differential expression of the oncoproteins c-myc and c-myb in human lymphoproliferative disorders. European Journal of Cancer, 26, 733–737.PubMedCrossRef
118.
Kitagawa, K., Hiramatsu, Y., Uchida, C., et al. (2009). Fbw7 promotes ubiquitin-dependent degradation of c-Myb: involvement of GSK3-mediated phosphorylation of Thr-572 in mouse c-Myb. Oncogene, 28, 2393–2405.PubMedCrossRef
119.
Kanei-Ishii, C., Nomura, T., Takagi, T., et al. (2008). Fbxw7 acts as an E3 ubiquitin ligase that targets c-Myb for nemo-like kinase (NLK)-induced degradation. Journal of Biological Chemistry, 283, 30540–30548.PubMedCrossRef
120.
Kern, S. E., Kinzler, K. W., Bruskin, A., et al. (1991). Identification of p53 as a sequence-specific DNA-binding protein. Science, 252, 1708–1711.PubMedCrossRef
121.
Kimura, T., Gotoh, M., Nakamura, Y., & Arakawa, H. (2003). hCDC4b, a regulator of cyclin E, as a direct transcriptional target of p53. Cancer Science, 94, 431–436.PubMedCrossRef
122.
Finkin, S., Aylon, Y., Anzi, S., Oren, M., & Shaulian, E. (2008). Fbw7 regulates the activity of endoreduplication mediators and the p53 pathway to prevent drug-induced polyploidy. Oncogene, 27, 4411–4421.PubMedCrossRef
123.
Flores, E. R., Sengupta, S., Miller, J. B., et al. (2005). Tumor predisposition in mice mutant for p63 and p73: evidence for broader tumor suppressor functions for the p53 family. Cancer Cell, 7, 363–373.PubMedCrossRef
124.
Yang, A., Schweitzer, R., Sun, D., et al. (1999). p63 is essential for regenerative proliferation in limb, craniofacial and epithelial development. Nature, 398, 714–718.PubMedCrossRef
125.
Mills, A. A., Zheng, B., Wang, X. J., et al. (1999). p63 is a p53 homologue required for limb and epidermal morphogenesis. Nature, 398, 708–713.PubMedCrossRef
126.
Thurfjell, N., Coates, P. J., Uusitalo, T., et al. (2004). Complex p63 mRNA isoform expression patterns in squamous cell carcinoma of the head and neck. International Journal of Oncology, 25, 27–35.PubMed
127.
van Bokhoven, H., & McKeon, F. (2002). Mutations in the p53 homolog p63: allele-specific developmental syndromes in humans. Trends in Molecular Medicine, 8, 133–139.PubMedCrossRef
128.
Laurikkala, J., Mikkola, M. L., James, M., et al. (2006). p63 regulates multiple signalling pathways required for ectodermal organogenesis and differentiation. Development, 133, 1553–1563.PubMedCrossRef
129.
Rossi, M., De Simone, M., Pollice, A., et al. (2006). Itch/AIP4 associates with and promotes p63 protein degradation. Cell Cycle, 5, 1816–1822.PubMedCrossRef
130.
Rossi, M., Aqeilan, R. I., Neale, M., et al. (2006). The E3 ubiquitin ligase Itch controls the protein stability of p63. Proceedings of the National Academy of Sciences of the United States of America, 103, 12753–12758.PubMedCrossRef
131.
Galli, F., Rossi, M., D’Alessandra, Y., et al. (2010). MDM2 and Fbw7 cooperate to induce p63 protein degradation following DNA damage and cell differentiation. Journal of Cell Science, 123, 2423–2433.PubMedCrossRef
132.
Massague, J., & Wotton, D. (2000). Transcriptional control by the TGF-beta/Smad signaling system. The EMBO Journal, 19, 1745–1754.PubMedCrossRef
133.
Miyazono, K., Suzuki, H., & Imamura, T. (2003). Regulation of TGF-beta signaling and its roles in progression of tumors. Cancer Science, 94, 230–234.PubMedCrossRef
134.
Bengoechea-Alonso, M. T., & Ericsson, J. (2010). Tumor suppressor Fbxw7 regulates TGFbeta signaling by targeting TGIF1 for degradation. Oncogene, 29, 5322–5328.PubMedCrossRef
135.
Besirli, C. G., Wagner, E. F., & Johnson, E. M., Jr. (2005). The limited role of NH2-terminal c-Jun phosphorylation in neuronal apoptosis: identification of the nuclear pore complex as a potential target of the JNK pathway. The Journal of Cell Biology, 170, 401–411.PubMedCrossRef
136.
Hoeck, J. D., Jandke, A., Blake, S. M., et al. (2010). Fbw7 controls neural stem cell differentiation and progenitor apoptosis via Notch and c-Jun. Nature Neuroscience, 13, 1365–1372.PubMedCrossRef
137.
Matsumoto, A., Onoyama, I., Sunabori, T., et al. (2011). Fbxw7-dependent degradation of Notch is required for control of “stemness” and neuronal-glial differentiation in neural stem cells. Journal of Biological Chemistry, 286, 13754–13764.PubMedCrossRef
138.
Willis, S. N., Fletcher, J. I., Kaufmann, T., et al. (2007). Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak. Science, 315, 856–859.PubMedCrossRef
139.
Wertz, I. E., Kusam, S., Lam, C., et al. (2011). Sensitivity to antitubulin chemotherapeutics is regulated by MCL1 and FBW7. Nature, 471, 110–114.PubMedCrossRef
140.
141.
Howe, A., Aplin, A. E., Alahari, S. K., & Juliano, R. L. (1998). Integrin signaling and cell growth control. Current Opinion in Cell Biology, 10, 220–231.PubMedCrossRef
142.
Coussens, L. M., & Werb, Z. (1996). Matrix metalloproteinases and the development of cancer. Chemistry & Biology, 3, 895–904.CrossRef
143.
Chambers, A. F., & Matrisian, L. M. (1997). Changing views of the role of matrix metalloproteinases in metastasis. Journal of the National Cancer Institute, 89, 1260–1270.PubMedCrossRef
144.
145.
Massague, J., Blain, S. W., & Lo, R. S. (2000). TGFbeta signaling in growth control, cancer, and heritable disorders. Cell, 103, 295–309.PubMedCrossRef
146.
Knuutila, S., Aalto, Y., Autio, K., et al. (1999). DNA copy number losses in human neoplasms. American Journal of Pathology, 155, 683–694.PubMedCrossRef
147.
Rajagopalan, H., Jallepalli, P. V., Rago, C., et al. (2004). Inactivation of hCDC4 can cause chromosomal instability. Nature, 428, 77–81.PubMedCrossRef
148.
Woo Lee, J., Hwa Soung, Y., Young Kim, S., et al. (2006). Somatic mutation of hCDC4 gene is rare in lung adenocarcinomas. Acta Oncologica, 45, 487–488.PubMedCrossRef
149.
Nowak, D., Mossner, M., Baldus, C. D., et al. (2006). Mutation analysis of hCDC4 in AML cells identifies a new intronic polymorphism. International Journal of Medical Sciences, 3, 148–151.PubMedCrossRef
150.
Kwak, E. L., Moberg, K. H., Wahrer, D. C., et al. (2005). Infrequent mutations of Archipelago (hAGO, hCDC4, Fbw7) in primary ovarian cancer. Gynecologic Oncology, 98, 124–128.PubMedCrossRef
151.
Yan, T., Wunder, J. S., Gokgoz, N., et al. (2006). hCDC4 variation in osteosarcoma. Cancer Genetics and Cytogenetics, 169, 138–142.PubMedCrossRef
152.
Fresno Vara, J. A., Casado, E., de Castro, J., et al. (2004). PI3K/Akt signalling pathway and cancer. Cancer Treatment Reviews, 30, 193–204.PubMedCrossRef
153.
Larson Gedman, A., Chen, Q., Kugel Desmoulin, S., et al. (2009). The impact of NOTCH1, FBW7 and PTEN mutations on prognosis and downstream signaling in pediatric T-cell acute lymphoblastic leukemia: a report from the Children’s Oncology Group. Leukemia, 23, 1417–1425.PubMedCrossRef
Metadaten
Titel
Role of the ubiquitin ligase Fbw7 in cancer progression
verfasst von
Yabin Cheng
Gang Li
Publikationsdatum
01.06.2012
Verlag
Springer US
Erschienen in
Cancer and Metastasis Reviews / Ausgabe 1-2/2012
Print ISSN: 0167-7659
Elektronische ISSN: 1573-7233
DOI
https://doi.org/10.1007/s10555-011-9330-z

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