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1
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0026562404
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Multiple intestinal neoplasia caused by mutations in the murine homolog of the APC gene
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This paper identifies the Apc locus as the site for mutations in intestinal neplasia.
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Su L.K., Kinzler K.W., Vogelstein B., Preisinger A.C., Moser A., Luongo C., Gould K.A., and Dove W.F. Multiple intestinal neoplasia caused by mutations in the murine homolog of the APC gene. Science 256 (1992) 668-670. This paper identifies the Apc locus as the site for mutations in intestinal neplasia.
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(1992)
Science
, vol.256
, pp. 668-670
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Su, L.K.1
Kinzler, K.W.2
Vogelstein, B.3
Preisinger, A.C.4
Moser, A.5
Luongo, C.6
Gould, K.A.7
Dove, W.F.8
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2
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0026568524
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The Min (multiple intestinal neoplasia) mutation: its effect on gut epithelial cell differentiation and interaction with a modifier system
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This paper identifies the Apc locus as the site for mutations in intesitnal neplasia, but also demonstrates the effects of genetic background on penetrance of phenotype
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Moser A.R., Dove W.F., Roth K.A., and Gordon J.I. The Min (multiple intestinal neoplasia) mutation: its effect on gut epithelial cell differentiation and interaction with a modifier system. J Cell Biol 116 (1992) 1517-1526. This paper identifies the Apc locus as the site for mutations in intesitnal neplasia, but also demonstrates the effects of genetic background on penetrance of phenotype
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(1992)
J Cell Biol
, vol.116
, pp. 1517-1526
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Moser, A.R.1
Dove, W.F.2
Roth, K.A.3
Gordon, J.I.4
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3
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0029143510
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ApcMin: a mouse model for intestinal and mammary tumorigenesis
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This paper established the causal relationship between Apc heterozygosity and intestinal neoplasia. The Min mouse described in this paper is one of the most commonly used mouse strains in the world.
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Moser A.R., Luongo C., Gould K.A., McNeley M.K., Shoemaker A.R., and Dove W.F. ApcMin: a mouse model for intestinal and mammary tumorigenesis. Eur J Cancer 31A (1995) 1061-1064. This paper established the causal relationship between Apc heterozygosity and intestinal neoplasia. The Min mouse described in this paper is one of the most commonly used mouse strains in the world.
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(1995)
Eur J Cancer
, vol.31 A
, pp. 1061-1064
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Moser, A.R.1
Luongo, C.2
Gould, K.A.3
McNeley, M.K.4
Shoemaker, A.R.5
Dove, W.F.6
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4
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0027738023
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Association of the APC gene product with β-catenin
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This paper shows the interaction of Apc protein with β-catenin, which set the stage for the identifying the Wnt-regulated degradation of β-catenin as a central pathway in colon tumour development.
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Rubinfeld B., Souza B., Albert I., Müller O., Chamberlain S.H., Masiarz F.R., Munemitsu S., and Polakis P. Association of the APC gene product with β-catenin. Science 262 (1993) 1731-1734. This paper shows the interaction of Apc protein with β-catenin, which set the stage for the identifying the Wnt-regulated degradation of β-catenin as a central pathway in colon tumour development.
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(1993)
Science
, vol.262
, pp. 1731-1734
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Rubinfeld, B.1
Souza, B.2
Albert, I.3
Müller, O.4
Chamberlain, S.H.5
Masiarz, F.R.6
Munemitsu, S.7
Polakis, P.8
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5
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0027756014
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Association of the APC tumor suppressor protein with catenins
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Shows the interaction of Apc protein with β-catenin, which set the stage for the identifying the Wnt-regulated degradation of β-catenin as a central pathway in colon tumour development.
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Su L.-K., Vogelstein B., and Kinzler K.W. Association of the APC tumor suppressor protein with catenins. Science 262 (1993) 1734-1737. Shows the interaction of Apc protein with β-catenin, which set the stage for the identifying the Wnt-regulated degradation of β-catenin as a central pathway in colon tumour development.
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(1993)
Science
, vol.262
, pp. 1734-1737
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Su, L.-K.1
Vogelstein, B.2
Kinzler, K.W.3
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6
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33846193290
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The many ways of Wnt in cancer
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Polakis P. The many ways of Wnt in cancer. Curr Opin Genet Dev 17 (2007) 45-51
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(2007)
Curr Opin Genet Dev
, vol.17
, pp. 45-51
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Polakis, P.1
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7
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41549133195
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Kennell J, Cadigan K: APC and ß-catenin degradation. In APC proteins. Edited by Näthke IS, McCartney BM: Landes Bioscience; 2008, in press. http://www.eurekah.com/chapter/3776.
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Kennell J, Cadigan K: APC and ß-catenin degradation. In APC proteins. Edited by Näthke IS, McCartney BM: Landes Bioscience; 2008, in press. http://www.eurekah.com/chapter/3776.
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8
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0029664368
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Binding of GSK3beta to the APC-beta-catenin complex and regulation of complex assembly
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This paper provides significant insights into the assembly and regulation of the complex that governs the degradation of β-catenin. Of particular importance to this discussion was the finding that the phosphorylation of the central repeat region of Apc significantly enhances its affinity for β-catenin.
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Rubinfeld B., Albert I., Porfiri E., Fiol C., Munemitsu S., and Polakis P. Binding of GSK3beta to the APC-beta-catenin complex and regulation of complex assembly. Science 272 (1996) 1023-1026. This paper provides significant insights into the assembly and regulation of the complex that governs the degradation of β-catenin. Of particular importance to this discussion was the finding that the phosphorylation of the central repeat region of Apc significantly enhances its affinity for β-catenin.
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(1996)
Science
, vol.272
, pp. 1023-1026
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Rubinfeld, B.1
Albert, I.2
Porfiri, E.3
Fiol, C.4
Munemitsu, S.5
Polakis, P.6
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9
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33745276261
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The third 20 amino acid repeat is the tightest binding site of APC for beta-catenin
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The authors present a detailed analysis of the binding affinities of individual phosphorylated and unphosphorylated 15R and 20R for β-catenin. They showed that individual repeats have distinct binding affinities, with 20R3 being the highest, and the phosphorylation increases the binding affinities for all of them. Furthermore, specific amino acids in the 20R N-terminal flanking sequences significantly enhance the binding affinities of unphosphorylated 20R for β-catenin. Further study is required to determine the functional significance of these distinctions.
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Liu J., Xing Y., Hinds T.R., Zheng J., and Xu W. The third 20 amino acid repeat is the tightest binding site of APC for beta-catenin. J Mol Biol 360 (2006) 133-144. The authors present a detailed analysis of the binding affinities of individual phosphorylated and unphosphorylated 15R and 20R for β-catenin. They showed that individual repeats have distinct binding affinities, with 20R3 being the highest, and the phosphorylation increases the binding affinities for all of them. Furthermore, specific amino acids in the 20R N-terminal flanking sequences significantly enhance the binding affinities of unphosphorylated 20R for β-catenin. Further study is required to determine the functional significance of these distinctions.
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(2006)
J Mol Biol
, vol.360
, pp. 133-144
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Liu, J.1
Xing, Y.2
Hinds, T.R.3
Zheng, J.4
Xu, W.5
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11
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4344684495
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Crystal structure of a beta-catenin/APC complex reveals a critical role for APC phosphorylation in APC function
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••] demonstrated that phosphorylated Apc (P-Apc) competes with Axin for binding to β-catenin, while non-P-Apc and Axin can bind β-catenin simultaneously. These findings suggest a novel model for interactions within the destruction complex. Phosphorylation may be a 'critical switch' for Apc outside of the destruction complex as well. Xing et al. 2004 showed that P-Apc competes with Tcf binding to β-catenin, and thus may provide an additional mechanism for the downregulation of β-catenin transcription by Apc.
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••] demonstrated that phosphorylated Apc (P-Apc) competes with Axin for binding to β-catenin, while non-P-Apc and Axin can bind β-catenin simultaneously. These findings suggest a novel model for interactions within the destruction complex. Phosphorylation may be a 'critical switch' for Apc outside of the destruction complex as well. Xing et al. 2004 showed that P-Apc competes with Tcf binding to β-catenin, and thus may provide an additional mechanism for the downregulation of β-catenin transcription by Apc.
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(2004)
Mol Cell
, vol.15
, pp. 523-533
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Xing, Y.1
Clements, W.K.2
Le Trong, I.3
Hinds, T.R.4
Stenkamp, R.5
Kimelman, D.6
Xu, W.7
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12
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0344442773
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Crystal structure of a beta-catenin/axin complex suggests a mechanism for the beta-catenin destruction complex
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This paper provided important structural insights into the nature of the β-catenin-Axin complex that set the stage for the later structural work.
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Xing Y., Clements W.K., Kimelman D., and Xu W. Crystal structure of a beta-catenin/axin complex suggests a mechanism for the beta-catenin destruction complex. Genes Dev 17 (2003) 2753-2764. This paper provided important structural insights into the nature of the β-catenin-Axin complex that set the stage for the later structural work.
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(2003)
Genes Dev
, vol.17
, pp. 2753-2764
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Xing, Y.1
Clements, W.K.2
Kimelman, D.3
Xu, W.4
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13
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0037022275
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Casein kinase I phosphorylates and destabilizes the beta-catenin degradation complex
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Gao Z.H., Seeling J.M., Hill V., Yochum A., and Virshup D.M. Casein kinase I phosphorylates and destabilizes the beta-catenin degradation complex. Proc Natl Acad Sci U S A 99 (2002) 1182-1187
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(2002)
Proc Natl Acad Sci U S A
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Gao, Z.H.1
Seeling, J.M.2
Hill, V.3
Yochum, A.4
Virshup, D.M.5
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14
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0034719170
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GSK-3beta-dependent phosphorylation of adenomatous polyposis coli gene product can be modulated by beta-catenin and protein phosphatase 2A complexed with Axin
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Ikeda S., Kishida M., Matsuura Y., Usui H., and Kikuchi A. GSK-3beta-dependent phosphorylation of adenomatous polyposis coli gene product can be modulated by beta-catenin and protein phosphatase 2A complexed with Axin. Oncogene 19 (2000) 537-545
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Oncogene
, vol.19
, pp. 537-545
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Ikeda, S.1
Kishida, M.2
Matsuura, Y.3
Usui, H.4
Kikuchi, A.5
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15
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0033524929
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Identification of a domain of Axin that binds to the serin/threonine protein phosphatase 2A and a self-binding domain
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Hsu W., Zeng L., and Constantini F. Identification of a domain of Axin that binds to the serin/threonine protein phosphatase 2A and a self-binding domain. J Biol Chem 274 (1999) 3439-3445
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(1999)
J Biol Chem
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, pp. 3439-3445
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Hsu, W.1
Zeng, L.2
Constantini, F.3
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16
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0033605639
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Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A
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This paper demonstrates the involvement of PP2A as an important regulator of β-catenin degradation.
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Seeling J., Miller J., Gil R., Moon R., White R., and Virshup D. Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A. Science 283 (1999) 2089-2091. This paper demonstrates the involvement of PP2A as an important regulator of β-catenin degradation.
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(1999)
Science
, vol.283
, pp. 2089-2091
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Seeling, J.1
Miller, J.2
Gil, R.3
Moon, R.4
White, R.5
Virshup, D.6
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17
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0035920201
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Inhibition of the Wnt signaling pathway by the PR61 subunit of protein phosphatase 2A
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Yamamoto H., Hinoi T., Michiue T., Fukui A., Usui H., Janssens V., Van Hoof C., Goris J., Asashima M., and Kikuchi A. Inhibition of the Wnt signaling pathway by the PR61 subunit of protein phosphatase 2A. J Biol Chem 276 (2001) 26875-26882
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(2001)
J Biol Chem
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Yamamoto, H.1
Hinoi, T.2
Michiue, T.3
Fukui, A.4
Usui, H.5
Janssens, V.6
Van Hoof, C.7
Goris, J.8
Asashima, M.9
Kikuchi, A.10
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18
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33745919542
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Testing hypotheses for the functions of APC family proteins using null and truncation alleles in Drosophila
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The authors showed that Drosophila null for both Apc genes (Apc1 and APC2) do not exhibit significant defects in a variety of processes in which Apc has been implicated, including cell viability, cadherin-based adhesion, spindle morphology and orientation, or cytokinesis. Complete loss of Drosophila Apc proteins does result in significant activation of Wnt signalling throughout development. These findings are consistent with the hypothesis that although Apc proteins may function in many cellular processes, they are not strictly required for most of these processes, but rather function in their fidelity and/or efficiency.
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McCartney B.M., Price M.H., Webb R.L., Hayden M.A., Holot L.M., Zhou M., Bejsovec A., and Peifer M. Testing hypotheses for the functions of APC family proteins using null and truncation alleles in Drosophila. Development 133 (2006) 2407-2418. The authors showed that Drosophila null for both Apc genes (Apc1 and APC2) do not exhibit significant defects in a variety of processes in which Apc has been implicated, including cell viability, cadherin-based adhesion, spindle morphology and orientation, or cytokinesis. Complete loss of Drosophila Apc proteins does result in significant activation of Wnt signalling throughout development. These findings are consistent with the hypothesis that although Apc proteins may function in many cellular processes, they are not strictly required for most of these processes, but rather function in their fidelity and/or efficiency.
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(2006)
Development
, vol.133
, pp. 2407-2418
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McCartney, B.M.1
Price, M.H.2
Webb, R.L.3
Hayden, M.A.4
Holot, L.M.5
Zhou, M.6
Bejsovec, A.7
Peifer, M.8
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19
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0033602227
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The F-box protein beta-TrCP associates with phosphorylated beta-catenin and regulates its activity in the cell
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Hart M., Concordet J.P., Lassot I., Albert I., del los Santos R., Durand H., Perret C., Rubinfeld B., Margottin F., Benarous R., et al. The F-box protein beta-TrCP associates with phosphorylated beta-catenin and regulates its activity in the cell. Curr Biol 9 (1999) 207-210
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(1999)
Curr Biol
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Hart, M.1
Concordet, J.P.2
Lassot, I.3
Albert, I.4
del los Santos, R.5
Durand, H.6
Perret, C.7
Rubinfeld, B.8
Margottin, F.9
Benarous, R.10
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20
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0033588939
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Drosophila APC2 is a cytoskeletally-associated protein that regulates Wnt signaling in the embryonic epidermis
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McCartney B.M., Dierick H.A., Kirkpatrick C., Moline M.M., Baas A., Peifer M., and Bejsovec A. Drosophila APC2 is a cytoskeletally-associated protein that regulates Wnt signaling in the embryonic epidermis. J Cell Biol 146 (1999) 1303-1318
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(1999)
J Cell Biol
, vol.146
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McCartney, B.M.1
Dierick, H.A.2
Kirkpatrick, C.3
Moline, M.M.4
Baas, A.5
Peifer, M.6
Bejsovec, A.7
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21
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A new Drosophila APC homologue associated with adhesive zones of epithelial cells
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Yu X., Waltzer L., and Bienz M. A new Drosophila APC homologue associated with adhesive zones of epithelial cells. Nat Cell Biol 1 (1999) 144-151
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(1999)
Nat Cell Biol
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Yu, X.1
Waltzer, L.2
Bienz, M.3
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22
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1842479447
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Adenomatous polyposis coli and EB1 localize in close proximity of the mother centriole and EB1 is a functional component of centrosomes
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Louie R.K., Bahmanyar S., Siemers K.A., Votin V., Chang P., Stearns T., Nelson W.J., and Barth A.I. Adenomatous polyposis coli and EB1 localize in close proximity of the mother centriole and EB1 is a functional component of centrosomes. J Cell Sci 117 (2004) 1117-1128
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J Cell Sci
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Louie, R.K.1
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Barth, A.I.8
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Neufeld K: Nuclear APC. In APC proteins. Edited by Näthke IS, McCartney BM: Landes Bioscience; 2008, in press. http://www.eurekah.com/chapter/3835.
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Neufeld K: Nuclear APC. In APC proteins. Edited by Näthke IS, McCartney BM: Landes Bioscience; 2008, in press. http://www.eurekah.com/chapter/3835.
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24
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0033740339
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Phosphorylation near nuclear localization signal regulates nuclear import of adenomatous polyposis coli protein
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This paper provided key evidence that the NLS activity of Apc is regulated by the phosphorylation of NLS flanking sites in two different ways. Phosphorylation by casein kinase 2 appears to enhance NLS activity, while phosphorylation by protein kinase A, inhibits NLS activity.
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Zhang F., White R.L., and Neufeld K.L. Phosphorylation near nuclear localization signal regulates nuclear import of adenomatous polyposis coli protein. Proc Natl Acad Sci U S A 97 (2000) 12577-12582. This paper provided key evidence that the NLS activity of Apc is regulated by the phosphorylation of NLS flanking sites in two different ways. Phosphorylation by casein kinase 2 appears to enhance NLS activity, while phosphorylation by protein kinase A, inhibits NLS activity.
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(2000)
Proc Natl Acad Sci U S A
, vol.97
, pp. 12577-12582
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Zhang, F.1
White, R.L.2
Neufeld, K.L.3
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25
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20444437586
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Casein kinase 2- and protein kinase A-regulated adenomatous polyposis coli and beta-catenin cellular localization is dependent on p38 MAPK
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Hildesheim J., Salvador J.M., Hollander M.C., and Fornace Jr. A.J. Casein kinase 2- and protein kinase A-regulated adenomatous polyposis coli and beta-catenin cellular localization is dependent on p38 MAPK. J Biol Chem 280 (2005) 17221-17226
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Hildesheim, J.1
Salvador, J.M.2
Hollander, M.C.3
Fornace Jr., A.J.4
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Association and regulation of casein kinase 2 activity by adenomatous polyposis coli protein
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Homma M.K., Li D., Krebs E.G., Yuasa Y., and Homma Y. Association and regulation of casein kinase 2 activity by adenomatous polyposis coli protein. Proc Natl Acad Sci U S A 99 (2002) 5959-5964
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Homma, M.K.1
Li, D.2
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Homma, Y.5
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27
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33646583259
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Nucleo-cytoplasmic distribution of beta-catenin is regulated by retention
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Using live cell imaging and fluorescence recovery after photobleaching, the authors demonstrated that none of the factors known to bind to β-catenin in the nucleus influence the rate of β-catenin nuclear import and export. Instead, these binding partners may act to sequester β-catenin in specific cellular compartments. This elegant study strongly supports the model that one function of Apc in the nucleus is to sequester β-catenin and thus downregulate its transcriptional activity.
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Krieghoff E., Behrens J., and Mayr B. Nucleo-cytoplasmic distribution of beta-catenin is regulated by retention. J Cell Sci 119 (2006) 1453-1463. Using live cell imaging and fluorescence recovery after photobleaching, the authors demonstrated that none of the factors known to bind to β-catenin in the nucleus influence the rate of β-catenin nuclear import and export. Instead, these binding partners may act to sequester β-catenin in specific cellular compartments. This elegant study strongly supports the model that one function of Apc in the nucleus is to sequester β-catenin and thus downregulate its transcriptional activity.
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(2006)
J Cell Sci
, vol.119
, pp. 1453-1463
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Krieghoff, E.1
Behrens, J.2
Mayr, B.3
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28
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The APC tumor suppressor binds to C-terminal binding protein to divert nuclear beta-catenin from TCF
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Hamada F., and Bienz M. The APC tumor suppressor binds to C-terminal binding protein to divert nuclear beta-catenin from TCF. Dev Cell 7 (2004) 677-685
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Bienz, M.2
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CK2 controls the recruitment of Wnt regulators to target genes in vivo
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(2006)
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Casein kinase 2 (CK2) increases survivin expression via enhanced beta-catenin-T cell factor/lymphoid enhancer binding factor-dependent transcription
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•] provide evidence for additional roles for casein kinase 2 (CK2) in Wnt signalling. Not only does CK2 appear to regulate the nuclear localisation of Apc (24), but it also plays a role in the assembly of LEF1-β-catenin transcriptional complexes.
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•] provide evidence for additional roles for casein kinase 2 (CK2) in Wnt signalling. Not only does CK2 appear to regulate the nuclear localisation of Apc (24), but it also plays a role in the assembly of LEF1-β-catenin transcriptional complexes.
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(2006)
Proc Natl Acad Sci U S A
, vol.103
, pp. 15079-15084
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Tapia, J.C.1
Torres, V.A.2
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Mizumoto K., and Sawa H. Cortical beta-catenin and APC regulate asymmetric nuclear beta-catenin localization during asymmetric cell division in C. elegans. Dev Cell 12 (2007) 287-299
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The APC protein binds to A/T rich DNA sequences
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Deka J., Herter P., Sprenger-Haussels M., Koosch S., Franz D., Muller K.M., Kuhnen C., Hoffmann I., and Muller O. The APC protein binds to A/T rich DNA sequences. Oncogene 18 (1999) 5654-5661
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Tumor suppressor APC blocks DNA polymerase beta-dependent strand displacement synthesis during long patch but not short patch base excision repair and increases sensitivity to methylmethane sulfonate
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Narayan S., Jaiswal A.S., and Balusu R. Tumor suppressor APC blocks DNA polymerase beta-dependent strand displacement synthesis during long patch but not short patch base excision repair and increases sensitivity to methylmethane sulfonate. J Biol Chem 280 (2005) 6942-6949
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Characterization of epithelial cell shedding from human small intestine
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Bullen T.F., Forrest S., Campbell F., Dodson A.R., Hershman M.J., Pritchard D.M., Turner J.R., Montrose M.H., and Watson A.J. Characterization of epithelial cell shedding from human small intestine. Lab Invest 86 (2006) 1052-1063
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Lab Invest
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Benchabane H, Ahmed Y: The adenomatous polyposis coli tumor suppressor and wnt signaling in the regulation of apoptosis. In APC Proteins. Edited by Näthke IS, McCartney BM. Landes Bioscience, vol 1; 2008, in press. http://www.eurekah.com/chapter/3784.
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Benchabane H, Ahmed Y: The adenomatous polyposis coli tumor suppressor and wnt signaling in the regulation of apoptosis. In APC Proteins. Edited by Näthke IS, McCartney BM. Landes Bioscience, vol 1; 2008, in press. http://www.eurekah.com/chapter/3784.
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The beta-catenin - TCF-1 pathway ensures CD4(+)CD8(+) thymocyte survival
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Ioannidis V., Beermann F., Clevers H., and Held W. The beta-catenin - TCF-1 pathway ensures CD4(+)CD8(+) thymocyte survival. Nat Immunol 2 (2001) 691-697
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Huang M., Wang Y., Sun D., Zhu H., Yin Y., Zhang W., Yang S., Quan L., Bai J., Wang S., et al. Identification of genes regulated by Wnt/beta-catenin pathway and involved in apoptosis via microarray analysis. BMC Cancer 6 (2006) 221
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BMC Cancer
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Huang, M.1
Wang, Y.2
Sun, D.3
Zhu, H.4
Yin, Y.5
Zhang, W.6
Yang, S.7
Quan, L.8
Bai, J.9
Wang, S.10
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38
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33846419846
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Loss of APC induces polyploidy as a result of a combination of defects in mitosis and apoptosis
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This paper demonstrates immediate defects in cell cycle machinery, including the spindle checkpoint, after the loss of Apc in cells and tissue.
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Dikovskaya D., Schiffmann D., Newton I.P., Oakley A., Kroboth K., Sansom O., Jamieson T.J., Meniel V., Clarke A., and Näthke I.S. Loss of APC induces polyploidy as a result of a combination of defects in mitosis and apoptosis. J Cell Biol 176 (2007) 183-195. This paper demonstrates immediate defects in cell cycle machinery, including the spindle checkpoint, after the loss of Apc in cells and tissue.
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J Cell Biol
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, pp. 183-195
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Dikovskaya, D.1
Schiffmann, D.2
Newton, I.P.3
Oakley, A.4
Kroboth, K.5
Sansom, O.6
Jamieson, T.J.7
Meniel, V.8
Clarke, A.9
Näthke, I.S.10
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39
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33947177629
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Lack of adenomatous polyposis coli protein correlates with a decrease in cell migration and overall changes in microtubule stability
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This paper shows that Apc status correlates with over microtubule stability in cells and affects cell migration.
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Kroboth K., Newton I.P., Kita K., Dikovskaya D., Zumbrunn J., Waterman-Storer C.M., and Näthke I.S. Lack of adenomatous polyposis coli protein correlates with a decrease in cell migration and overall changes in microtubule stability. Mol Biol Cell 18 (2007) 910-918. This paper shows that Apc status correlates with over microtubule stability in cells and affects cell migration.
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(2007)
Mol Biol Cell
, vol.18
, pp. 910-918
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Kroboth, K.1
Newton, I.P.2
Kita, K.3
Dikovskaya, D.4
Zumbrunn, J.5
Waterman-Storer, C.M.6
Näthke, I.S.7
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40
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0037434790
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Cdc42 regulates GSK-3beta and adenomatous polyposis coli to control cell polarity
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This paper provides important link between small GTPases and Apc in migrating protrusions.
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Etienne-Manneville S., and Hall A. Cdc42 regulates GSK-3beta and adenomatous polyposis coli to control cell polarity. Nature 421 (2003) 753-756. This paper provides important link between small GTPases and Apc in migrating protrusions.
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(2003)
Nature
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, pp. 753-756
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Etienne-Manneville, S.1
Hall, A.2
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Cdc42 and Par6-PKCzeta regulate the spatially localized association of Dlg1 and APC to control cell polarization
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Etienne-Manneville S., Manneville J.B., Nicholls S., Ferenczi M.A., and Hall A. Cdc42 and Par6-PKCzeta regulate the spatially localized association of Dlg1 and APC to control cell polarization. J Cell Biol 170 (2005) 895-901
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(2005)
J Cell Biol
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Etienne-Manneville, S.1
Manneville, J.B.2
Nicholls, S.3
Ferenczi, M.A.4
Hall, A.5
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42
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0027930066
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The APC gene product associates with microtubules in vivo and promotes their assembly in vitro
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This is the first demonstration that Apc can bind to microtubules.
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Munemitsu S., Souza B., Müller O., Albert I., Rubinfeld B., and Polakis P. The APC gene product associates with microtubules in vivo and promotes their assembly in vitro. Cancer Res 54 (1994) 3676-3681. This is the first demonstration that Apc can bind to microtubules.
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(1994)
Cancer Res
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Munemitsu, S.1
Souza, B.2
Müller, O.3
Albert, I.4
Rubinfeld, B.5
Polakis, P.6
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43
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0035176077
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Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3b phosphorylation
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This paper shows the direct effect of Apc on microtubule stability in vitro and in cells and provides evidence that this function can be regulated by the phosphorylation with GSK3b.
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Zumbrunn J., Inoshita K., Hyman A.A., and Näthke I.S. Binding of the adenomatous polyposis coli protein to microtubules increases microtubule stability and is regulated by GSK3b phosphorylation. Curr Biol 11 (2001) 44-49. This paper shows the direct effect of Apc on microtubule stability in vitro and in cells and provides evidence that this function can be regulated by the phosphorylation with GSK3b.
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(2001)
Curr Biol
, vol.11
, pp. 44-49
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Zumbrunn, J.1
Inoshita, K.2
Hyman, A.A.3
Näthke, I.S.4
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44
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33745737636
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APC on microtubule plus ends in cell extensions can promote microtubule net growth with or without EB1
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This paper demonstrates direct link between endogenous Apc protein and microtubule dynamics in cells.
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Kita K., Wittmann T., Näthke I.S., and Waterman-Storer C.M. APC on microtubule plus ends in cell extensions can promote microtubule net growth with or without EB1. Mol Biol Cell 17 (2006) 2331-2345. This paper demonstrates direct link between endogenous Apc protein and microtubule dynamics in cells.
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(2006)
Mol Biol Cell
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, pp. 2331-2345
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Kita, K.1
Wittmann, T.2
Näthke, I.S.3
Waterman-Storer, C.M.4
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45
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0029066006
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APC binds to the novel protein EB1
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This paper identifies EB1 as an Apc binding partner and thus brings Apc closer to the microtubule cytoskeleton.
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Su L.-K., Burrell M., Hill D.E., Gyuris J., Brent R., Wiltshire R., Trent J., Vogelstein B., and Kinzler K.W. APC binds to the novel protein EB1. Cancer Res 55 (1995) 2972-2977. This paper identifies EB1 as an Apc binding partner and thus brings Apc closer to the microtubule cytoskeleton.
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Cancer Res
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Su, L.-K.1
Burrell, M.2
Hill, D.E.3
Gyuris, J.4
Brent, R.5
Wiltshire, R.6
Trent, J.7
Vogelstein, B.8
Kinzler, K.W.9
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46
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Regulated binding of adenomatous polyposis coli protein to actin
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Moseley J.B., Bartolini F., Okada K., Wen Y., Gundersen G.G., and Goode B.L. Regulated binding of adenomatous polyposis coli protein to actin. J Biol Chem 282 (2007) 12661-12668
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J Biol Chem
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Moseley, J.B.1
Bartolini, F.2
Okada, K.3
Wen, Y.4
Gundersen, G.G.5
Goode, B.L.6
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47
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0034682888
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Asef, a link between the tumor suppressor APC and G-protein signaling
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Identifies Apc as a regulator for the activity of an exchange factor for small GTP-ases thus establishing a functional link between Apc and actin.
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Kawasaki Y., Senda T., Ishidate T., Koyama R., Morishita T., Iwayama Y., Higuchi O., and Akiyama T. Asef, a link between the tumor suppressor APC and G-protein signaling. Science 289 (2000) 1194-1197. Identifies Apc as a regulator for the activity of an exchange factor for small GTP-ases thus establishing a functional link between Apc and actin.
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(2000)
Science
, vol.289
, pp. 1194-1197
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Kawasaki, Y.1
Senda, T.2
Ishidate, T.3
Koyama, R.4
Morishita, T.5
Iwayama, Y.6
Higuchi, O.7
Akiyama, T.8
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48
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10644281068
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Interaction with IQGAP1 links APC to Rac1, Cdc42, and actin filaments during cell polarization and migration
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Watanabe T., Wang S., Noritake J., Sato K., Fukata M., Takefuji M., Nakagawa M., Izumi N., Akiyama T., and Kaibuchi K. Interaction with IQGAP1 links APC to Rac1, Cdc42, and actin filaments during cell polarization and migration. Dev Cell 7 (2004) 871-883
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(2004)
Dev Cell
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Watanabe, T.1
Wang, S.2
Noritake, J.3
Sato, K.4
Fukata, M.5
Takefuji, M.6
Nakagawa, M.7
Izumi, N.8
Akiyama, T.9
Kaibuchi, K.10
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49
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4444360489
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EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration
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Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J., Chen M., Wallar B.J., Alberts A.S., and Gundersen G.G. EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration. Nat Cell Biol 6 (2004) 820-830
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(2004)
Nat Cell Biol
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Wen, Y.1
Eng, C.H.2
Schmoranzer, J.3
Cabrera-Poch, N.4
Morris, E.J.5
Chen, M.6
Wallar, B.J.7
Alberts, A.S.8
Gundersen, G.G.9
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50
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Loss of Apc in vivo immediately perturbs Wnt signaling, differentiation, and migration
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Shows that conditionally inactivating Apc in the gut immediately leads to changes that underlie tumourigenesis.
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Sansom O.J., Reed K.R., Hayes A.J., Ireland H., Brinkmann H., Newton I.P., Batlle E., Simon-Assmann P., Clevers H., Näthke I.S., et al. Loss of Apc in vivo immediately perturbs Wnt signaling, differentiation, and migration. Genes Dev 18 (2004) 1385-1390. Shows that conditionally inactivating Apc in the gut immediately leads to changes that underlie tumourigenesis.
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Genes Dev
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Sansom, O.J.1
Reed, K.R.2
Hayes, A.J.3
Ireland, H.4
Brinkmann, H.5
Newton, I.P.6
Batlle, E.7
Simon-Assmann, P.8
Clevers, H.9
Näthke, I.S.10
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51
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33745542004
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Misorientation and reduced stretching of aligned sister kinetochores promote chromosome missegregation in EB1- or APC-depleted cells
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Draviam V.M., Shapiro I., Aldridge B., and Sorger P.K. Misorientation and reduced stretching of aligned sister kinetochores promote chromosome missegregation in EB1- or APC-depleted cells. EMBO J 25 (2006) 2814-2827
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EMBO J
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Draviam, V.M.1
Shapiro, I.2
Aldridge, B.3
Sorger, P.K.4
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Chromosomal instability by beta-catenin/TCF transcription in APC or beta-catenin mutant cells
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Aoki K., Aoki M., Sugai M., Harada N., Miyoshi H., Tsukamoto T., Mizoshita T., Tatematsu M., Seno H., Chiba T., et al. Chromosomal instability by beta-catenin/TCF transcription in APC or beta-catenin mutant cells. Oncogene 26 (2007) 3511-3520
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Oncogene
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Aoki, K.1
Aoki, M.2
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Harada, N.4
Miyoshi, H.5
Tsukamoto, T.6
Mizoshita, T.7
Tatematsu, M.8
Seno, H.9
Chiba, T.10
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53
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Chromosome instability in colorectal tumor cells is associated with defects in microtubule plus-end attachments caused by a dominant mutation in APC
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This paper demonstrates a dominant effect of N-terminal Apc fragments in mitosis.
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Green R.A., and Kaplan K.B. Chromosome instability in colorectal tumor cells is associated with defects in microtubule plus-end attachments caused by a dominant mutation in APC. J Cell Biol 163 (2003) 949-961. This paper demonstrates a dominant effect of N-terminal Apc fragments in mitosis.
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J Cell Biol
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Green, R.A.1
Kaplan, K.B.2
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APC mutations lead to cytokinetic failures in vitro and tetraploid genotypes in Min mice
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Caldwell C.M., Green R.A., and Kaplan K.B. APC mutations lead to cytokinetic failures in vitro and tetraploid genotypes in Min mice. J Cell Biol 178 (2007) 1109-1120
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J Cell Biol
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Caldwell, C.M.1
Green, R.A.2
Kaplan, K.B.3
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55
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2-terminal fragments are the most stable part of the adenomatous polyposis coli protein and can be regulated by interactions with COOH-terminal domains
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2-terminal fragments are the most stable part of the adenomatous polyposis coli protein and can be regulated by interactions with COOH-terminal domains. Cancer Res 65 (2005) 5195-5204
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Cancer Res
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Li, Z.1
Näthke, I.S.2
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APC and EB1 function together in mitosis to regulate spindle dynamics and chromosome alignment
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Green R.A., Wollman R., and Kaplan K.B. APC and EB1 function together in mitosis to regulate spindle dynamics and chromosome alignment. Mol Biol Cell 16 (2005) 4609-4622
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Mol Biol Cell
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Green, R.A.1
Wollman, R.2
Kaplan, K.B.3
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The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain
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Berrueta L., Tirnauer J.S., Schuyler S.C., Pellman D., and Bierer B.E. The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain. Curr Biol 9 (1999) 425-428
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Curr Biol
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Berrueta, L.1
Tirnauer, J.S.2
Schuyler, S.C.3
Pellman, D.4
Bierer, B.E.5
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Interaction between EB1 and p150glued is required for anaphase astral microtubule elongation and stimulation of cytokinesis
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Strickland L.I., Wen Y., Gundersen G.G., and Burgess D.R. Interaction between EB1 and p150glued is required for anaphase astral microtubule elongation and stimulation of cytokinesis. Curr Biol 15 (2005) 2249-2255
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Curr Biol
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Strickland, L.I.1
Wen, Y.2
Gundersen, G.G.3
Burgess, D.R.4
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Drosophila APC2 and Armadillo participate in tethering mitotic spindles to cortical actin
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McCartney B.M., McEwen D.G., Grevengoed E., Maddox P., Bejsovec A., and Peifer M. Drosophila APC2 and Armadillo participate in tethering mitotic spindles to cortical actin. Nat Cell Biol 3 (2001) 933-938
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Nat Cell Biol
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McCartney, B.M.1
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Peifer, M.6
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A target-selected Apc-mutant rat kindred enhances the modeling of familial human colon cancer
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This paper introduces a novel rat model for Apc-mediated tumourigenesis that mimics the human disease more accurately.
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Amos-Landgraf J.M., Kwong L.N., Kendziorski C.M., Reichelderfer M., Torrealba J., Weichert J., Haag J.D., Chen K.S., Waller J.L., Gould M.N., et al. A target-selected Apc-mutant rat kindred enhances the modeling of familial human colon cancer. Proc Natl Acad Sci U S A 104 (2007) 4036-4041. This paper introduces a novel rat model for Apc-mediated tumourigenesis that mimics the human disease more accurately.
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Proc Natl Acad Sci U S A
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Amos-Landgraf, J.M.1
Kwong, L.N.2
Kendziorski, C.M.3
Reichelderfer, M.4
Torrealba, J.5
Weichert, J.6
Haag, J.D.7
Chen, K.S.8
Waller, J.L.9
Gould, M.N.10
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61
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34247187543
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Myc deletion rescues Apc deficiency in the small intestine
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This paper demonstrates that Myc is absolutely required for Apc-deficient cells to survive in intestinal tissue and form tumours and that de-regulated, nuclear β-catenin is not sufficient.
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Sansom O.J., Meniel V.S., Muncan V., Phesse T.J., Wilkins J.A., Reed K.R., Vass J.K., Athineos D., Clevers H., and Clarke A.R. Myc deletion rescues Apc deficiency in the small intestine. Nature 446 (2007) 676-679. This paper demonstrates that Myc is absolutely required for Apc-deficient cells to survive in intestinal tissue and form tumours and that de-regulated, nuclear β-catenin is not sufficient.
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Nature
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Sansom, O.J.1
Meniel, V.S.2
Muncan, V.3
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Wilkins, J.A.5
Reed, K.R.6
Vass, J.K.7
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Clevers, H.9
Clarke, A.R.10
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Downregulation of ß-catenin by human axin and its association with the APC tumor suppressor, ß-catenin and GSK3ß
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Hart M.J., de los Santos R., Albert I., Rubinfeld B., and Polakis P. Downregulation of ß-catenin by human axin and its association with the APC tumor suppressor, ß-catenin and GSK3ß. Curr Biol 8 (1998) 573-581
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Hart, M.J.1
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Polakis, P.5
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