메뉴 건너뛰기




Volumn 288, Issue 6, 2013, Pages 3753-3767

HectDI E3 ligase modifies adenomatous polyposis coli (APC) with polyubiquitin to promote the APC-axin interaction

Author keywords

[No Author keywords available]

Indexed keywords

ADENOMATOUS POLYPOSIS COLI; E3 LIGASE; NEGATIVE REGULATORS; POLYUBIQUITIN; POLYUBIQUITYLATION; PROTEIN FUNCTIONS; UBIQUITIN LIGASES; UBIQUITYLATION; WNT SIGNALING; WNT SIGNALING PATHWAYS;

EID: 84873674014     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.415240     Document Type: Article
Times cited : (54)

References (55)
  • 1
    • 17244376814 scopus 로고    scopus 로고
    • Wnt signalling in stem cells and cancer
    • Reya, T., and Clevers, H. (2005) Wnt signalling in stem cells and cancer. Nature 434, 843-850
    • (2005) Nature , vol.434 , pp. 843-850
    • Reya, T.1    Clevers, H.2
  • 2
    • 84865109330 scopus 로고    scopus 로고
    • Wnt signaling in cancer
    • doi: 10.1101/cshperspect.a008052
    • Polakis, P. (2013) Wnt signaling in cancer. Cold Spring Hark Perspect. Biol. 4, doi: 10.1101/cshperspect.a008052
    • (2013) Cold Spring Hark Perspect. Biol. , vol.4
    • Polakis, P.1
  • 3
    • 77957005350 scopus 로고    scopus 로고
    • The various roles of ubiquitin in Wnt pathway regulation
    • Tauriello, D. V., and Maurice, M. M. (2010) The various roles of ubiquitin in Wnt pathway regulation. Cell Cycle 9, 3700-3709
    • (2010) Cell Cycle , vol.9 , pp. 3700-3709
    • Tauriello, D.V.1    Maurice, M.M.2
  • 5
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains. New molecular signals. "protein Modifications." beyond the Usual Suspects review series
    • Ikeda, F., and Dikic, I. (2008) Atypical ubiquitin chains. New molecular signals. "Protein Modifications." Beyond the Usual Suspects review series. EMBORep. 9, 536-542
    • (2008) EMBORep. , vol.9 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 6
    • 84255168970 scopus 로고    scopus 로고
    • The emerging role of linear ubiquitination in cell signaling
    • Emmerich, C. H., Schmukle, A. C, and Walczak, H. (2011) The emerging role of linear ubiquitination in cell signaling. Sei. Signal. 4, re5
    • (2011) Sei. Signal. , vol.4
    • Emmerich, C.H.1    Schmukle, A.C.2    Walczak, H.3
  • 7
    • 0030978351 scopus 로고    scopus 로고
    • β-Catenin is a target for the ubiquitin-proteasome pathway
    • Aberle, H., Bauer, A., Stappert, J., Kispert, A., and Kemler, R. (1997) β-Catenin is a target for the ubiquitin-proteasome pathway. EMBOJ. 16, 3797-3804
    • (1997) EMBOJ , vol.16 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 10
    • 0029664368 scopus 로고    scopus 로고
    • Binding of GSK3/3 to the APC-β-catenin complex and regulation of complex assembly
    • Rubinfeld, B., Albert, I., Porfiri, E., Fiol, C, Munemitsu, S., and Polakis, P. (1996) Binding of GSK3/3 to the APC-β-catenin complex and regulation of complex assembly. Science 272, 1023-1026
    • (1996) Science , vol.272 , pp. 1023-1026
    • Rubinfeld, B.1    Albert, I.2    Porfiri, E.3    Fiol, C.4    Munemitsu, S.5    Polakis, P.6
  • 12
    • 0032492954 scopus 로고    scopus 로고
    • Downregulation of β-catenin by human Axin and its association with the APC tumor suppressor, β-catenin and GSK3/3
    • Hart, M. J., de los Santos, R., Albert, I. N, Rubinfeld, B., and Polakis, P. (1998) Downregulation of β-catenin by human Axin and its association with the APC tumor suppressor, β-catenin and GSK3/3. Curr. Biol. 8, 573-581
    • (1998) Curr. Biol. , vol.8 , pp. 573-581
    • Hart, M.J.1    De Los Santos, R.2    Albert, I.N.3    Rubinfeld, B.4    Polakis, P.5
  • 13
    • 0037155691 scopus 로고    scopus 로고
    • Control of β-catenin phosphorylation/degradation by a dual-kinase mechanism
    • Liu, C., Li, Y., Semenov, M., Han, C., Baeg, G.H., Tan, Y., Zhang, Z., Lin, X., and He, X. (2002) Control of β-catenin phosphorylation/degradation by a dual-kinase mechanism. Cell 108, 837-847
    • (2002) Cell , vol.108 , pp. 837-847
    • Liu, C.1    Li, Y.2    Semenov, M.3    Han, C.4    Baeg, G.H.5    Tan, Y.6    Zhang, Z.7    Lin, X.8    He, X.9
  • 14
    • 84865228580 scopus 로고    scopus 로고
    • Reversible modification of adenomatous polyposis coli (APC) with K63-linked polyubiquitin regulates the assembly and activity of the β-catenin destruction complex
    • Tran, H., and Polakis, P. (2012) Reversible modification of adenomatous polyposis coli (APC) with K63-linked polyubiquitin regulates the assembly and activity of the β-catenin destruction complex. Biol. Chem. 287, 28552-28563
    • (2012) Biol. Chem. , vol.287 , pp. 28552-28563
    • Tran, H.1    Polakis, P.2
  • 15
    • 33645714061 scopus 로고    scopus 로고
    • The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-β-catenin pathway by targeting Dishevelled for degradation
    • Angers, S., Thorpe, C. J., Biechele, T. L., Goldenberg, S. J., Zheng, N, MacCoss, M. J., and Moon, R. T. (2006) The KLHL12-Cullin-3 ubiquitin ligase negatively regulates the Wnt-β-catenin pathway by targeting Dishevelled for degradation. Nat. Cell Biol. 8, 348-357
    • (2006) Nat. Cell Biol. , vol.8 , pp. 348-357
    • Angers, S.1    Thorpe, C.J.2    Biechele, T.L.3    Goldenberg, S.J.4    Zheng, N.5    MacCoss, M.J.6    Moon, R.T.7
  • 19
    • 84863012691 scopus 로고    scopus 로고
    • Adenomatous polyposis coli (APC) regulates multiple signaling pathways by enhancing glycogen synthase kinase-3 (GSK-3) activity
    • Valvezan, A.J., Zhang, F., Diehl, J.A., and Klein, P.S. (2012) Adenomatous polyposis coli (APC) regulates multiple signaling pathways by enhancing glycogen synthase kinase-3 (GSK-3) activity, Biol. Chem. 287, 3823-3832
    • (2012) Biol. Chem. , vol.287 , pp. 3823-3832
    • Valvezan, A.J.1    Zhang, F.2    Diehl, J.A.3    Klein, P.S.4
  • 20
    • 33746326169 scopus 로고    scopus 로고
    • NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiq-uitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF)
    • Yamada, M., Ohnishi, J., Ohkawara, B., Iemura, S., Satoh, K., Hyodo-Miura, J., Kawachi, IC, Natsume, T., and Shibuya, H. (2006) NARF, an nemo-like kinase (NLK)-associated ring finger protein regulates the ubiq-uitylation and degradation of T cell factor/lymphoid enhancer factor (TCF/LEF). Biol. Chem. 281, 20749-20760
    • (2006) Biol. Chem. , vol.281 , pp. 20749-20760
    • Yamada, M.1    Ohnishi, J.2    Ohkawara, B.3    Iemura, S.4    Satoh, K.5    Hyodo-Miura, J.6    Kawachi, I.C.7    Natsume, T.8    Shibuya, H.9
  • 22
    • 84864076896 scopus 로고    scopus 로고
    • The ciliary protein nephrocystin-4 translocates the canonical Wnt regulator Jade-1 to the nucleus to negatively regulate β-catenin signaling
    • Borgal, L., Habbig, S., Hatzold, J., Liebau, M. C, Dafinger, C, Sacarea, I., Hammerschmidt, M., Benzing, T., and Schermer, B. (2012) The ciliary protein nephrocystin-4 translocates the canonical Wnt regulator Jade-1 to the nucleus to negatively regulate β-catenin signaling. Biol. Chem. 287, 25370-25380
    • (2012) Biol. Chem. , vol.287 , pp. 25370-25380
    • Borgal, L.1    Habbig, S.2    Hatzold, J.3    Liebau, M.C.4    Dafinger, C.5    Sacarea, I.6    Hammerschmidt, M.7    Benzing, T.8    Schermer, B.9
  • 23
    • 77954903507 scopus 로고    scopus 로고
    • Balanced ubiquitylation and deubiquitylation of Friz-zledregulate cellular responsiveness to Wg/Wnt
    • Mukai, A., Yamamoto-Hino, M., Awano, W., Watanabe, W., Komada, M., and Goto, S. (2010) Balanced ubiquitylation and deubiquitylation of Friz-zledregulate cellular responsiveness to Wg/Wnt.EMBOJ. 29, 2114-2125
    • (2010) EMBOJ , vol.29 , pp. 2114-2125
    • Mukai, A.1    Yamamoto-Hino, M.2    Awano, W.3    Watanabe, W.4    Komada, M.5    Goto, S.6
  • 24
    • 39449084931 scopus 로고    scopus 로고
    • Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains
    • Tran, H., Hamada, F., Schwarz-Romond, T., and Bienz, M. (2008) Trabid, a new positive regulator of Wnt-induced transcription with preference for binding and cleaving K63-linked ubiquitin chains. Genes Dev. 22, 528-542
    • (2008) Genes Dev. , vol.22 , pp. 528-542
    • Tran, H.1    Hamada, F.2    Schwarz-Romond, T.3    Bienz, M.4
  • 25
    • 84860272868 scopus 로고    scopus 로고
    • Hectdl regulates intracellular localization and secretion of Hsp90 to control cellular behavior of the cranial mesenchyme
    • Sarkar, A. A., and Zohn, I. E. (2012) Hectdl regulates intracellular localization and secretion of Hsp90 to control cellular behavior of the cranial mesenchyme. Cell Biol. 196, 789-800
    • (2012) Cell Biol. , vol.196 , pp. 789-800
    • Sarkar, A.A.1    Zohn, I.E.2
  • 27
    • 0028987249 scopus 로고
    • Regulation of intracellular β-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein
    • Munemitsu, S., Albert, I., Souza, B., Rubinfeld, B., and Polakis, P. (1995) Regulation of intracellular β-catenin levels by the adenomatous polyposis coli (APC) tumor-suppressor protein. Proc. Natl. Acad. Sei. U.S.A. 92, 3046-3050
    • (1995) Proc. Natl. Acad. Sei. U.S.A. , vol.92 , pp. 3046-3050
    • Munemitsu, S.1    Albert, I.2    Souza, B.3    Rubinfeld, B.4    Polakis, P.5
  • 32
    • 3042555013 scopus 로고    scopus 로고
    • A novel isoform of sarcolemmal membrane-associated protein (SLMAP) is a component of the microtubule organizing centre
    • Guzzo, R. M., Sevinc, S., Salih, M., and Tuana, B. S. (2004) A novel isoform of sarcolemmal membrane-associated protein (SLMAP) is a component of the microtubule organizing centre, J. Cell Sei. 117, 2271-2281
    • (2004) J. Cell Sei. , vol.117 , pp. 2271-2281
    • Guzzo, R.M.1    Sevinc, S.2    Salih, M.3    Tuana, B.S.4
  • 35
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa, M. E., Bennett, E. J., Gygi, S. P., and Harper, J. W. (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138, 389-403
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 36
    • 34249671135 scopus 로고    scopus 로고
    • The Hectdl ubiq-uitin ligase is required for development of the head mesenchyme and neural tube closure
    • Zohn, I. E., Anderson, K. V, and Niswander, L. (2007) The Hectdl ubiq-uitin ligase is required for development of the head mesenchyme and neural tube closure. Dev. Biol. 306, 208-221
    • (2007) Dev. Biol. , vol.306 , pp. 208-221
    • Zohn, I.E.1    Anderson, K.V.2    Niswander, L.3
  • 37
    • 67349231313 scopus 로고    scopus 로고
    • Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains
    • Komander, D., Reyes-Turcu, F., Licchesi, J. D., Odenwaelder, P., Wilkinson, K. D., and Barford, D. (2009) Molecular discrimination of structurally equivalent Lys 63-linked and linear polyubiquitin chains. EMBO Rep. 10, 466-473
    • (2009) EMBO Rep. , vol.10 , pp. 466-473
    • Komander, D.1    Reyes-Turcu, F.2    Licchesi, J.D.3    Odenwaelder, P.4    Wilkinson, K.D.5    Barford, D.6
  • 39
    • 77955417276 scopus 로고    scopus 로고
    • Lysll-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne
    • Bremm, A., Freund, S. M., and Komander, D. (2010) Lysll-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne. Nat. Struct. Mol. Biol. 17, 939-947
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 939-947
    • Bremm, A.1    Freund, S.M.2    Komander, D.3
  • 40
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • Deng, L., Wang, C, Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C, Pickart, C, and Chen, Z. J. (2000) Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Cell 103, 351-361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 41
    • 50849096682 scopus 로고    scopus 로고
    • The armadillo repeat domain of the APC tumor suppressor protein interacts with Striatin family members
    • Breitman, M., Zilberberg, A., Caspi, M., and Rosin-Arbesfeld, R. (2008) The armadillo repeat domain of the APC tumor suppressor protein interacts with Striatin family members. Biochim. Biophys. Acta 1783, 1792-1802
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1792-1802
    • Breitman, M.1    Zilberberg, A.2    Caspi, M.3    Rosin-Arbesfeld, R.4
  • 42
    • 0029982877 scopus 로고    scopus 로고
    • The adenomatous polyposis coli tumor suppressor protein localizes to plasma membrane sites involved in active cell migration
    • Näthke, I. S., Adams, C. L., Polakis, P., Sellin, I. H., and Nelson, W. J. (1996) The adenomatous polyposis coli tumor suppressor protein localizes to plasma membrane sites involved in active cell migration. Cell Biol. 134, 165-179
    • (1996) Cell Biol. , vol.134 , pp. 165-179
    • Näthke, I.S.1    Adams, C.L.2    Polakis, P.3    Sellin, I.H.4    Nelson, W.J.5
  • 44
    • 84860797975 scopus 로고    scopus 로고
    • Identification of small molecule TRABID deubiquitinase inhibitors by computation-based virtual screen
    • Shi, T., Bao, J., Wang, N. X., Zheng, J., and Wu, D. (2012) Identification of small molecule TRABID deubiquitinase inhibitors by computation-based virtual screen. BMC Chem. Biol. 12, 4
    • (2012) BMC Chem. Biol. , vol.12 , pp. 4
    • Shi, T.1    Bao, J.2    Wang, N.X.3    Zheng, J.4    Wu, D.5
  • 45
    • 0034657187 scopus 로고    scopus 로고
    • Structural basis of the Axin-adenomatous polyposis coli interaction
    • Spink, K. E., Polakis, P., and Weis, W. I. (2000) Structural basis of the Axin-adenomatous polyposis coli interaction. EMBO J. 19, 2270-2279
    • (2000) EMBO J , vol.19 , pp. 2270-2279
    • Spink, K.E.1    Polakis, P.2    Weis, W.I.3
  • 46
    • 0034733727 scopus 로고    scopus 로고
    • Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat proteins principally expressed in the brain
    • Castets, F., Rakitina, T., Gaillard, S., Moqrich, A., Mattei, M. G., and Mon-neron, A. (2000) Zinedin, SG2NA, and striatin are calmodulin-binding, WD repeat proteins principally expressed in the brain. Biol. Chem. 275, 19970-19977
    • (2000) Biol. Chem. , vol.275 , pp. 19970-19977
    • Castets, F.1    Rakitina, T.2    Gaillard, S.3    Moqrich, A.4    Mattei, M.G.5    Mon-Neron, A.6
  • 47
    • 78149456945 scopus 로고    scopus 로고
    • WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins
    • Pashkova, N, Gakhar, L., Winistorfer, S. C, Yu, L., Ramaswamy, S., and Piper, R. C (2010) WD40 repeat propellers define a ubiquitin-binding domain that regulates turnover of F box proteins. Mol. Cell 40, 433-443
    • (2010) Mol. Cell , vol.40 , pp. 433-443
    • Pashkova, N.1    Gakhar, L.2    Winistorfer, S.C.3    Yu, L.4    Ramaswamy, S.5    Piper, R.C.6
  • 48
    • 36749082959 scopus 로고    scopus 로고
    • A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway
    • Cohn, M. A., Kowal, P., Yang, IC, Haas, W., Huang, T. T., Gygi, S. P., and DAndrea, A. D. (2007) A UAF1-containing multisubunit protein complex regulates the Fanconi anemia pathway. Mol. Cell 28, 786-797
    • (2007) Mol. Cell , vol.28 , pp. 786-797
    • Cohn, M.A.1    Kowal, P.2    Yang, I.C.3    Haas, W.4    Huang, T.T.5    Gygi, S.P.6    Dandrea, A.D.7
  • 49
    • 64149129169 scopus 로고    scopus 로고
    • UAF1 is a subunit of multiple deubiquitinating enzyme complexes
    • Cohn, M. A., Kee, Y., Haas, W., Gygi, S. P., and DAndrea, A. D. (2009) UAF1 is a subunit of multiple deubiquitinating enzyme complexes. Biol. Chem. 284, 5343-5351
    • (2009) Biol. Chem. , vol.284 , pp. 5343-5351
    • Cohn, M.A.1    Kee, Y.2    Haas, W.3    Gygi, S.P.4    Dandrea, A.D.5
  • 50
    • 77951247308 scopus 로고    scopus 로고
    • WDR20 regulates activity of the USP12 x UAF1 deubiquitinating enzyme complex
    • Kee, Y., Yang, IC, Cohn, M. A., Haas, W., Gygi, S. P., and DAndrea, A. D. (2010) WDR20 regulates activity of the USP12 x UAF1 deubiquitinating enzyme complex. Biol. Chem. 285, 11252-11257
    • (2010) Biol. Chem. , vol.285 , pp. 11252-11257
    • Kee, Y.1    Yang, I.C.2    Cohn, M.A.3    Haas, W.4    Gygi, S.P.5    Dandrea, A.D.6
  • 54
    • 77955988806 scopus 로고    scopus 로고
    • Combined functional genomic and proteomic approaches identify a PP2A complex as a negative regulator of Hippo signaling
    • Ribeiro, P. S., Josué, F., Wepf, A., Wehr, M. C, Rinn er, O., Kelly, G., Tapon, N., and Gstaiger, M. (2010) Combined functional genomic and proteomic approaches identify a PP2A complex as a negative regulator of Hippo signaling. Mol. Cell 39, 521-534
    • (2010) Mol. Cell , vol.39 , pp. 521-534
    • Ribeiro, P.S.1    Josué, F.2    Wepf, A.3    Wehr, M.C.4    Rinn Er, O.5    Kelly, G.6    Tapon, N.7    Gstaiger, M.8
  • 55
    • 0036148208 scopus 로고    scopus 로고
    • Wnt//3-catenin/Tcf signaling induces the transcription of Axin2, a negative regulator of the signaling pathway
    • Jho, E. H, Zhang, T., Domon, C, Joo, C. IC, Freund, J. N, and Costantini, F. (2002) Wnt//3-catenin/Tcf signaling induces the transcription of Axin2, a negative regulator of the signaling pathway. Mol. Cell. Biol. 22, 1172-1183
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1172-1183
    • Jho, E.H.1    Zhang, T.2    Domon, C.3    Joo, C.I.C.4    Freund, J.N.5    Costantini, F.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.