MCC inhibits beta-catenin transcriptional activity by sequestering DBC1 in the cytoplasm

International Journal of Cancer

Volumn 136, Issue 1, 2015, Pages 55-64

  Pangon, Laurent ^a   Mladenova, Dessislava ^a   Watkins, Lauren ^a   Van Kralingen, Christa ^a   Currey, Nicola ^a   Al Sohaily, Sam ^a   Lecine, Patrick ^b,c,d   Borg, Jean Paul ^b,c,d   Kohonen Corish, Maija R J ^a,e,f  

^a GARVAN INSTITUTE OF MEDICAL RESEARCH   (Australia)

^b AIX MARSEILLE UNIVERSITY   (France)

^c INSTITUT PAOLI CALMETTES   (France)

^d AIX MARSEILLE UNIVERSITY   (France)

^e ST VINCENT'S CLINIC   (Australia)

^f UNIVERSITÉ LYON 1   (France)

Author keywords

beta catenin; colon cancer; DBC1; MCC; SIRT1; tumor suppressor

Indexed keywords

BETA CATENIN; DELETED IN BREAST CANCER 1 PROTEIN; LEUCINE ZIPPER PROTEIN; MUTATED IN COLORECTAL CANCER PROTEIN; NICOTINAMIDE; PEPTIDES AND PROTEINS; SMALL INTERFERING RNA; TUMOR SUPPRESSOR PROTEIN; UNCLASSIFIED DRUG; CTNNB1 PROTEIN, HUMAN; DBC1 PROTEIN, HUMAN; MCC PROTEIN, HUMAN; PROTEIN BINDING;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CELLULAR DISTRIBUTION; CONTROLLED STUDY; CYTOPLASM; DEACETYLATION; EF HAND DOMAIN; GENE; GENE OVEREXPRESSION; GENE SILENCING; HCT116 CELL LINE; HUMAN; HUMAN CELL; INTRACELLULAR SIGNALING; MCC GENE; MOLECULAR DYNAMICS; MUTATIONAL ANALYSIS; NUDIX DOMAIN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEPLETION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; RNA INTERFERENCE; STRUCTURE ACTIVITY RELATION; TRANSCRIPTION REGULATION; TRANSCRIPTIONAL REPRESSION; TUMOR SUPPRESSOR GENE; ACETYLATION; ACTIVE TRANSPORT; AMINO ACID SEQUENCE; CELL NUCLEUS; COLORECTAL TUMOR; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; GENETICS; HEK293 CELL LINE; METABOLISM; MISSENSE MUTATION; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHYSIOLOGY; PROTEIN PROCESSING;

ACETYLATION; ACTIVE TRANSPORT, CELL NUCLEUS; AMINO ACID SEQUENCE; BETA CATENIN; BINDING SITES; CELL NUCLEUS; COLORECTAL NEOPLASMS; CONSERVED SEQUENCE; CYTOPLASM; GENE EXPRESSION REGULATION, NEOPLASTIC; GENE SILENCING; HCT116 CELLS; HEK293 CELLS; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION, MISSENSE; PROTEIN BINDING; PROTEIN PROCESSING, POST-TRANSLATIONAL; TRANSCRIPTION, GENETIC; TUMOR SUPPRESSOR PROTEINS;

EID: 84925284727     PISSN: 00207136     EISSN: 10970215     Source Type: Journal    
DOI: 10.1002/ijc.28967     Document Type: Article

References (34)

1. Kinzler KW, Nilbert MC, Vogelstein B, et al., Identification of a gene located at chromosome 5q21 that is mutated in colorectal cancers. Science 1991; 251: 1366-70.
2. Starr TK, Allaei R, Silverstein KA, et al., A transposon-based genetic screen in mice identifies genes altered in colorectal cancer. Science 2009; 323: 1747-50.
3. Kohonen-Corish MR, Sigglekow ND, Susanto J, et al., Promoter methylation of the mutated in colorectal cancer gene is a frequent early event in colorectal cancer. Oncogene 2007; 26: 4435-41.
4. Fukuyama R, Niculaita R, Ng KP, et al., Mutated in colorectal cancer, a putative tumor suppressor for serrated colorectal cancer, selectively represses beta-catenin-dependent transcription. Oncogene 2008; 27: 6044-55.
5. Shukla R, Upton KR, Munoz-Lopez M, et al., Endogenous retrotransposition activates oncogenic pathways in hepatocellular carcinoma. Cell 2013; 153: 101-11.
6. Lim L, Balakrishnan A, Huskey N, et al., MiR-494 within an oncogenic MicroRNA megacluster regulates G1/S transition in liver tumorigenesis through suppression of MCC. Hepatology 2014; 59: 202-15.
7. Gamazon ER, Lamba JK, Pounds S, et al., Comprehensive genetic analysis of cytarabine sensitivity in a cell-based model identifies polymorphisms associated with outcome in AML patients. Blood 2013; 121: 4366-76.
8. Poursoltan P, Currey N, Pangon L, et al., Loss of heterozygosity of the Mutated in Colorectal Cancer gene is not associated with promoter methylation in non-small cell lung cancer. Lung Cancer 2012; 77: 272-6.
9. Pangon L, Sigglekow ND, Larance M, et al., The "Mutated in Colorectal Cancer" protein is a novel target of the UV-induced DNA damage checkpoint. Genes Cancer 2010; 1: 917-26.
10. Arnaud C, Sebbagh M, Nola S, et al., MCC, a new interacting protein for Scrib, is required for cell migration in epithelial cells. FEBS Lett 2009; 583: 2326-32.
11. Sigglekow ND, Pangon L, Brummer T, et al., Mutated in colorectal cancer protein modulates the NFkappaB pathway. Anticancer Res 2012; 32: 73-9.
12. Samowitz WS, Slattery ML, Sweeney C, et al., APC mutations and other genetic and epigenetic changes in colon cancer. Mol Cancer Res 2007; 5: 165-70.
13. Kim JE, Chen J, Lou Z,. DBC1 is a negative regulator of SIRT1. Nature 2008; 451: 583-6.
14. Zhao W, Kruse JP, Tang Y, et al., Negative regulation of the deacetylase SIRT1 by DBC1. Nature 2008; 451: 587-90.
15. Chini CC, Escande C, Nin V, et al., HDAC3 is negatively regulated by the nuclear protein DBC1. J Biol Chem 2010; 285: 40830-7.
16. Li Z, Chen L, Kabra N, et al., Inhibition of SUV39H1 methyltransferase activity by DBC1. J Biol Chem 2009; 284: 10361-6.
17. Hiraike H, Wada-Hiraike O, Nakagawa S, et al., Identification of DBC1 as a transcriptional repressor for BRCA1. Br J Cancer 2010; 102: 1061-7.
18. Fu J, Jiang J, Li J, et al., Deleted in breast cancer 1, a novel androgen receptor (AR) coactivator that promotes AR DNA-binding activity. J Biol Chem 2009; 284: 6832-40.
19. Yu EJ, Kim SH, Heo K, et al., Reciprocal roles of DBC1 and SIRT1 in regulating estrogen receptor alpha activity and co-activator synergy. Nucleic Acids Res 2011; 39: 6932-43.
20. Koyama S, Wada-Hiraike O, Nakagawa S, et al., Repression of estrogen receptor beta function by putative tumor suppressor DBC1. Biochem Biophys Res Commun 2010; 392: 357-62.
21. Firestein R, Blander G, Michan S, et al., The SIRT1 deacetylase suppresses intestinal tumorigenesis and colon cancer growth. PLoS One 2008; 3: e2020.
22. Cho IR, Koh SS, Malilas W, et al., SIRT1 inhibits proliferation of pancreatic cancer cells expressing pancreatic adenocarcinoma up-regulated factor (PAUF), a novel oncogene, by suppression of beta-catenin. Biochem Biophys Res Commun 2012; 423: 270-5.
23. Srisuttee R, Koh SS, Kim SJ, et al., Hepatitis B virus X (HBX) protein upregulates beta-catenin in a human hepatic cell line by sequestering SIRT1 deacetylase. Oncol Rep 2012; 28: 276-82.
24. Thalappilly S, Suliman M, Gayet O, et al., Identification of multi-SH3 domain-containing protein interactome in pancreatic cancer: a yeast two-hybrid approach. Proteomics 2008; 8: 3071-81.
25. Morris JR, Pangon L, Boutell C, et al., Genetic analysis of BRCA1 ubiquitin ligase activity and its relationship to breast cancer susceptibility. Hum Mol Genet 2006; 15: 599-606.
26. Veeman MT, Slusarski DC, Kaykas A, et al., Zebrafish prickle, a modulator of noncanonical Wnt/Fz signaling, regulates gastrulation movements. Curr Biol 2003; 13: 680-5.
27. Pangon L, Van Kralingen C, Abas M, et al., The PDZ-binding motif of MCC is phosphorylated at position-1 and controls lamellipodia formation in colon epithelial cells. Biochim Biophys Acta 2012; 1823: 1058-67.
28. Matsumine A, Senda T, Baeg GH, et al., MCC, a cytoplasmic protein that blocks cell cycle progression from the G0/G1 to S phase. J Biol Chem 1996; 271: 10341-6.
29. Anantharaman V, Aravind L,. Analysis of DBC1 and its homologs suggests a potential mechanism for regulation of sirtuin domain deacetylases by NAD metabolites. Cell Cycle 2008; 7: 1467-72.
30. Yang XJ, Seto E,. Lysine acetylation: codified crosstalk with other posttranslational modifications. Mol Cell 2008; 31: 449-61.
31. Simic P, Zainabadi K, Bell E, et al., SIRT1 regulates differentiation of mesenchymal stem cells by deacetylating beta-catenin. EMBO Mol Med 2013; 5: 430-40.
32. Li L, Fu X, Zhang W, et al., Wnt signaling pathway is activated in right colon serrated polyps correlating to specific molecular form of beta-catenin. Hum Pathol 2013; 44: 1079-88.
33. Zhang Y, Gu Y, Sha S, et al., DBC1 is over-expressed and associated with poor prognosis in colorectal cancer. Int J Clin Oncol 2014; 19: 106-12.
34. Kim W, Kim JE,. Deleted in breast cancer 1 (DBC1) deficiency results in apoptosis of breast cancer cells through impaired responses to UV-induced DNA damage. Cancer Lett 2013; 333: 180-6.