메뉴 건너뛰기




Volumn 9, Issue 4, 2014, Pages

Different roles for the Axin interactions with the SAMP versus the second twenty amino acid repeat of adenomatous polyposis coli

Author keywords

[No Author keywords available]

Indexed keywords

APC LIKE PROTEIN; APC PROTEIN; AXIN; AXIN 2; BETA CATENIN; UNCLASSIFIED DRUG; APC PROTEIN, HUMAN; APC2 PROTEIN, HUMAN; AXIN1 PROTEIN, HUMAN; AXIN2 PROTEIN, HUMAN; CTNNB1 PROTEIN, HUMAN; CYTOSKELETON PROTEIN; PROTEIN BINDING;

EID: 84899530105     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0094413     Document Type: Article
Times cited : (7)

References (71)
  • 1
    • 84861986053 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling and disease
    • Clevers H, Nusse R (2012) Wnt/beta-catenin signaling and disease. Cell 149: 1192-1205.
    • (2012) Cell , vol.149 , pp. 1192-1205
    • Clevers, H.1    Nusse, R.2
  • 4
    • 0032473355 scopus 로고    scopus 로고
    • Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta-catenin and promotes GSK-3beta-dependent phosphorylation of beta-catenin
    • DOI 10.1093/emboj/17.5.1371
    • Ikeda S, Kishida S, Yamamoto H, Murai H, Koyama S, et al. (1998) Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta-catenin and promotes GSK-3beta-dependent phosphorylation of beta-catenin. EMBO J 17: 1371-1384. (Pubitemid 28105516)
    • (1998) EMBO Journal , vol.17 , Issue.5 , pp. 1371-1384
    • Ikeda, S.1    Kishida, S.2    Yamamoto, H.3    Murai, H.4    Koyama, S.5    Kikuchi, A.6
  • 5
    • 67650230896 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling: Components, mechanisms, and diseases
    • MacDonald BT, Tamai K, He X (2009) Wnt/beta-catenin signaling: components, mechanisms, and diseases. Dev Cell 17: 9-26.
    • (2009) Dev Cell , vol.17 , pp. 9-26
    • MacDonald, B.T.1    Tamai, K.2    He, X.3
  • 6
    • 4344562126 scopus 로고    scopus 로고
    • Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation
    • DOI 10.1016/j.molcel.2004.08.010, PII S109727650400471X
    • Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI (2004) Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. Mol Cell 15: 511-521. (Pubitemid 39141779)
    • (2004) Molecular Cell , vol.15 , Issue.4 , pp. 511-521
    • Ha, N.-C.1    Tonozuka, T.2    Stamos, J.L.3    Choi, H.-J.4    Weis, W.I.5
  • 7
    • 4344684495 scopus 로고    scopus 로고
    • Crystal structure of a beta-catenin/APC complex reveals a critical role for APC phosphorylation in APC function
    • DOI 10.1016/j.molcel.2004.08.001, PII S1097276504004460
    • Xing Y, Clements WK, Le Trong I, Hinds TR, Stenkamp R, et al. (2004) Crystal structure of a beta-catenin/APC complex reveals a critical role for APC phosphorylation in APC function. Mol Cell 15: 523-533. (Pubitemid 39141780)
    • (2004) Molecular Cell , vol.15 , Issue.4 , pp. 523-533
    • Xing, Y.1    Clements, W.K.2    Le, T.I.3    Hinds, T.R.4    Stenkamp, R.5    Kimelman, D.6    Xu, W.7
  • 8
    • 79957597124 scopus 로고    scopus 로고
    • Deconstructing the beta-catenin destruction complex: Mechanistic roles for the tumor suppressor APC in regulating Wnt signaling
    • Roberts DM, Pronobis MI, Poulton JS, Waldmann JD, Stephenson EM, et al. (2011) Deconstructing the beta-catenin destruction complex: mechanistic roles for the tumor suppressor APC in regulating Wnt signaling. Mol Biol Cell 22: 1845-1863.
    • (2011) Mol Biol Cell , vol.22 , pp. 1845-1863
    • Roberts, D.M.1    Pronobis, M.I.2    Poulton, J.S.3    Waldmann, J.D.4    Stephenson, E.M.5
  • 9
    • 84861972831 scopus 로고    scopus 로고
    • Wnt signaling through inhibition of β-catenin degradation in an intact Axin1 complex
    • Li VS, Ng SS, Boersema PJ, Low TY, Karthaus WR, et al. (2012) Wnt signaling through inhibition of β-catenin degradation in an intact Axin1 complex. Cell 149: 1245-1256.
    • (2012) Cell , vol.149 , pp. 1245-1256
    • Li, V.S.1    Ng, S.S.2    Boersema, P.J.3    Low, T.Y.4    Karthaus, W.R.5
  • 10
    • 38549180413 scopus 로고    scopus 로고
    • Abundance, complexation, and trafficking of Wnt/beta-catenin signaling elements in response to Wnt3a
    • Yokoyama N, Yin D, Malbo CC (2007) Abundance, complexation, and trafficking of Wnt/beta-catenin signaling elements in response to Wnt3a. J Mol Signal: 2, e11.
    • (2007) J Mol Signal , vol.2
    • Yokoyama, N.1    Yin, D.2    Malbo, C.C.3
  • 11
    • 84856635802 scopus 로고    scopus 로고
    • Triple SILAC to determine stimulus specific interactions in the Wnt pathway
    • Hilger M, Mann M (2012) Triple SILAC to determine stimulus specific interactions in the Wnt pathway. J Proteome Res 11: 982-994.
    • (2012) J Proteome Res , vol.11 , pp. 982-994
    • Hilger, M.1    Mann, M.2
  • 12
    • 0025938038 scopus 로고
    • Identification and characterization of the familial adenomatous polyposis coli gene
    • Groden J, Thliveris A, Samowitz W, Carlson M, Gelbert L, et al. (1991) Identification and characterization of the familial adenomatous polyposis coli gene. Cell 66: 589-600.
    • (1991) Cell , vol.66 , pp. 589-600
    • Groden, J.1    Thliveris, A.2    Samowitz, W.3    Carlson, M.4    Gelbert, L.5
  • 13
    • 33847397617 scopus 로고    scopus 로고
    • The canonical Wnt signalling pathway and its APC partner in colon cancer development
    • DOI 10.1136/gut.2006.093310
    • Schneikert J, Behrens J (2007) The canonical Wnt signalling pathway and its APC partner in colon cancer development. Gut 56: 417-425. (Pubitemid 46579774)
    • (2007) Gut , vol.56 , Issue.3 , pp. 417-425
    • Schneikert, J.1    Behrens, J.2
  • 14
    • 0034604366 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal coiled-coil domain of the APC tumor suppressor
    • Day CL, Alber T (2000) Crystal structure of the amino-terminal coiled-coil domain of the APC tumor suppressor. J Mol Biol 301: 147-156.
    • (2000) J Mol Biol , vol.301 , pp. 147-156
    • Day, C.L.1    Alber, T.2
  • 15
    • 46749094255 scopus 로고    scopus 로고
    • Novel self-association of the APC molecule affects APC clusters and cell migration
    • DOI 10.1242/jcs.029470
    • Li Z, Kroboth K, Newton IP, Näthke IS (2008) Novel self-association of the APC molecule affects APC clusters and cell migration. J Cell Sci 121: 1916-1925. (Pubitemid 351943385)
    • (2008) Journal of Cell Science , vol.121 , Issue.11 , pp. 1916-1925
    • Li, Z.1    Kroboth, K.2    Newton, I.P.3    Nathke, I.S.4
  • 16
    • 0027756014 scopus 로고
    • Association of the APC tumor suppressor protein with catenins
    • Su LK, Vogelstein B, Kinzler KW (1993) Association of the APC tumor suppressor protein with catenins. Science 262: 1734-1737. (Pubitemid 24030097)
    • (1993) Science , vol.262 , Issue.5140 , pp. 1734-1737
    • Su, L.-K.1    Vogelstein, B.2    Kinzler, K.W.3
  • 17
    • 0035890060 scopus 로고    scopus 로고
    • Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex
    • DOI 10.1093/emboj/20.22.6203
    • Eklof Spink K, Fridman SG, Weis WI (2001). Molecular mechanisms of beta-catenin recognition by adenomatous polyposis coli revealed by the structure of an APC-beta-catenin complex. EMBO J 20: 6203-6212. (Pubitemid 33078694)
    • (2001) EMBO Journal , vol.20 , Issue.22 , pp. 6203-6212
    • Spink, K.E.1    Fridman, S.G.2    Weis, W.I.3
  • 18
    • 33745276261 scopus 로고    scopus 로고
    • The Third 20 Amino Acid Repeat Is the Tightest Binding Site of APC for beta-Catenin
    • DOI 10.1016/j.jmb.2006.04.064, PII S0022283606005572
    • Liu J, Xing Y, Hinds TR, Zheng J, Xu W (2006) The third 20 amino acid repeat is the tightest binding site of APC for beta-catenin. J Mol Biol 360: 133-144. (Pubitemid 43927813)
    • (2006) Journal of Molecular Biology , vol.360 , Issue.1 , pp. 133-144
    • Liu, J.1    Xing, Y.2    Hinds, T.R.3    Zheng, J.4    Xu, W.5
  • 20
    • 58049196841 scopus 로고    scopus 로고
    • Beta-catenin degradation mediated by the CID domain of APC provides a model for the selection of APC mutations in colorectal, desmoid and duodenal tumours
    • Kohler EM, Chandra SH, Behrens J, Schneikert J (2009) Beta-catenin degradation mediated by the CID domain of APC provides a model for the selection of APC mutations in colorectal, desmoid and duodenal tumours. Hum Mol Genet 18: 213-226.
    • (2009) Hum Mol Genet , vol.18 , pp. 213-226
    • Kohler, E.M.1    Chandra, S.H.2    Behrens, J.3    Schneikert, J.4
  • 21
    • 0032562603 scopus 로고    scopus 로고
    • Functional interaction of an Axin homolog, conductin, with beta-catenin, APC, and GSK3beta
    • Behrens J, Jerchow BA, Wurtele M, Grimm J, Asbrand C, et al. (1998) Functional interaction of an Axin homolog, conductin, with beta-catenin, APC, and GSK3beta. Science 280: 596-599.
    • (1998) Science , vol.280 , pp. 596-599
    • Behrens, J.1    Jerchow, B.A.2    Wurtele, M.3    Grimm, J.4    Asbrand, C.5
  • 22
    • 0034657187 scopus 로고    scopus 로고
    • Structural basis of the Axin-adenomatous polyposis coli interaction
    • Spink KE, Polakis P, Weis WI (2000) Structural basis of the Axin-adenomatous polyposis coli interaction. EMBO J 19: 2270-2279. (Pubitemid 30259008)
    • (2000) EMBO Journal , vol.19 , Issue.10 , pp. 2270-2279
    • Spink, K.E.1    Polakis, P.2    Weis, W.I.3
  • 23
    • 41549117418 scopus 로고    scopus 로고
    • Cell regulation by the Apc protein Apc as master regulator of epithelia
    • McCartney B, Näthke IS (2008) Cell regulation by the Apc protein Apc as master regulator of epithelia. Curr Opin Cell Biol 20: 186-193.
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 186-193
    • McCartney, B.1    Näthke, I.S.2
  • 24
    • 77949659176 scopus 로고    scopus 로고
    • Contribution of the 15 amino acid repeats of truncated APC to beta-catenin degradation and selection of APC mutations in colorectal tumours from FAP patients
    • Kohler EM, Brauburger K, Behrens J, Schneikert J (2010) Contribution of the 15 amino acid repeats of truncated APC to beta-catenin degradation and selection of APC mutations in colorectal tumours from FAP patients. Oncogene 29: 1663-1671.
    • (2010) Oncogene , vol.29 , pp. 1663-1671
    • Kohler, E.M.1    Brauburger, K.2    Behrens, J.3    Schneikert, J.4
  • 25
    • 0030871048 scopus 로고    scopus 로고
    • Loss of beta-catenin regulation by the APC tumor suppressor protein correlates with loss of structure due to common somatic mutations of the gene
    • Rubinfeld B, Albert I, Porfiri E, Munemitsu S, Polakis P (1997) Loss of beta-catenin regulation by the APC tumor suppressor protein correlates with loss of structure due to common somatic mutations of the gene. Cancer Res 57: 4624-4630. (Pubitemid 27441070)
    • (1997) Cancer Research , vol.57 , Issue.20 , pp. 4624-4630
    • Rubinfeld, B.1    Albert, I.2    Porfiri, E.3    Munemitsu, S.4    Polakis, P.5
  • 26
    • 84863922124 scopus 로고    scopus 로고
    • Comprehensive molecular characterization of human colon and rectal cancer
    • Muzny DM, Bainbridge MN, Chang K, Dinh HH, Drummond JA, et al. (2012) Comprehensive molecular characterization of human colon and rectal cancer. Nature 487: 330-337.
    • (2012) Nature , vol.487 , pp. 330-337
    • Muzny, D.M.1    Bainbridge, M.N.2    Chang, K.3    Dinh, H.H.4    Drummond, J.A.5
  • 27
    • 0026894053 scopus 로고
    • Somatic mutations of the APC gene in colorectal tumors: Mutation cluster region in the APC gene
    • Miyoshi Y, Nagase H, Ando H, Horii A, Ichii S, et al. (1992) Somatic mutations of the APC gene in colorectal tumors: mutation cluster region in the APC gene. Hum Mol Genet 1: 229-233.
    • (1992) Hum Mol Genet , vol.1 , pp. 229-233
    • Miyoshi, Y.1    Nagase, H.2    Ando, H.3    Horii, A.4    Ichii, S.5
  • 29
    • 0037416148 scopus 로고    scopus 로고
    • Nuclear export of the APC tumour suppressor controls beta-catenin function in transcription
    • DOI 10.1093/emboj/cdg105
    • Rosin-Arbesfeld R, Cliffe A, Brabletz T, Bienz M (2003) Nuclear export of the APC tumour suppressor controls beta-catenin function in transcription. EMBO J 22: 1101-1113. (Pubitemid 36313594)
    • (2003) EMBO Journal , vol.22 , Issue.5 , pp. 1101-1113
    • Rosin-Arbesfeld, R.1    Cliffe, A.2    Brabletz, T.3    Bienz, M.4
  • 30
    • 45749140081 scopus 로고    scopus 로고
    • Functional definition of the mutation cluster region of adenomatous polyposis coli in colorectal tumours
    • DOI 10.1093/hmg/ddn095
    • Kohler EM, Derungs A, Daum G, Behrens J, Schneikert J (2008) Functional definition of the mutation cluster region of adenomatous polyposis coli in colorectal tumours. Hum Mol Genet 17: 1978-1987. (Pubitemid 351865846)
    • (2008) Human Molecular Genetics , vol.17 , Issue.13 , pp. 1978-1987
    • Kohler, E.M.1    Derungs, A.2    Daum, G.3    Behrens, J.4    Schneikert, J.5
  • 31
    • 80052258209 scopus 로고    scopus 로고
    • APC mutations in colorectal tumours from FAP patients are selected for CtBP-mediated oligomerisation of truncated APC
    • Schneikert J, Brauburger K, Behrens J (2011) APC mutations in colorectal tumours from FAP patients are selected for CtBP-mediated oligomerisation of truncated APC. Hum Mol Genet 20: 3554-3564.
    • (2011) Hum Mol Genet , vol.20 , pp. 3554-3564
    • Schneikert, J.1    Brauburger, K.2    Behrens, J.3
  • 36
    • 36549030350 scopus 로고    scopus 로고
    • AMER1 regulates the distribution of the tumor suppressor APC between microtubules and the plasma membrane
    • DOI 10.1242/jcs.011320
    • Grohmann A, Tanneberger K, Alzner A, Schneikert J, Behrens J (2007) AMER1 regulates the distribution of the tumor suppressor APC between microtubules and the plasma membrane. J. Cell Sci 120: 3738-3747. (Pubitemid 350187356)
    • (2007) Journal of Cell Science , vol.120 , Issue.21 , pp. 3738-3747
    • Grohmann, A.1    Tanneberger, K.2    Alzner, A.3    Schneikert, J.4    Behrens, J.5
  • 40
    • 4243067196 scopus 로고    scopus 로고
    • The roles of APC and Axin derived from experimental and theoretical analysis of the Wnt pathway
    • Lee E, Salic A, Krüger R, Heinrich R, Kirschner MW (2003) The roles of APC and Axin derived from experimental and theoretical analysis of the Wnt pathway. PLoS Biol 1: e10.
    • (2003) PLoS Biol , vol.1
    • Lee, E.1    Salic, A.2    Krüger, R.3    Heinrich, R.4    Kirschner, M.W.5
  • 41
    • 0032492954 scopus 로고    scopus 로고
    • Downregulation of beta-catenin by human Axin and its association with the APC tumor suppressor, beta-catenin and GSK3beta
    • Hart MJ, de los Santos R, Albert IN, Rubinfeld B, Polakis P (1998) Downregulation of beta-catenin by human Axin and its association with the APC tumor suppressor, beta-catenin and GSK3 beta. Curr Biol 8: 573-581. (Pubitemid 28222891)
    • (1998) Current Biology , vol.8 , Issue.10 , pp. 573-581
    • Hart, M.J.1    De Los, S.R.2    Albert, I.N.3    Rubinfeld, B.4    Polakis, P.5
  • 42
    • 0031813650 scopus 로고    scopus 로고
    • Axin, an inhibitor of the Wnt signalling pathway, interacts with β- catenin, GSK-3β and APC and reduces the β-catenin level
    • Nakamura T, Hamada F, Ishidate T, Anai K, Kawahara K, et al. (1998) Axin, an inhibitor of the Wnt signalling pathway interacts with β-catenin, GSK-3β and APC and reduces the β-catenin level. Genes Cells 3: 395-403. (Pubitemid 28387083)
    • (1998) Genes to Cells , vol.3 , Issue.6 , pp. 395-403
    • Nakamura, T.1    Hamada, F.2    Ishidate, T.3    Anai, K.-I.4    Kawahara, K.5    Toyoshima, K.6    Akiyama, T.7
  • 43
    • 53249090244 scopus 로고    scopus 로고
    • Recruitment of adenomatous polyposis coli and beta-catenin to Axin-puncta
    • Faux MC, Coates JL, Catimel B, Cody S, Clayton AH, et al. (2008) Recruitment of adenomatous polyposis coli and beta-catenin to Axin-puncta. Oncogene 27: 5808-5820.
    • (2008) Oncogene , vol.27 , pp. 5808-5820
    • Faux, M.C.1    Coates, J.L.2    Catimel, B.3    Cody, S.4    Clayton, A.H.5
  • 45
    • 84861699364 scopus 로고    scopus 로고
    • The Adenomatous polyposis coli tumour suppressor is essential for Axin complex assembly and function and opposes Axin's interaction with Dishevelled
    • Mendoza-Topaz C, Mieszczanek J, Bienz M (2011) The Adenomatous polyposis coli tumour suppressor is essential for Axin complex assembly and function and opposes Axin's interaction with Dishevelled. Open Biol 1: e110013.
    • (2011) Open Biol , vol.1
    • Mendoza-Topaz, C.1    Mieszczanek, J.2    Bienz, M.3
  • 46
    • 79952148045 scopus 로고    scopus 로고
    • Dishevelled interacts with the DIX domain oligomerisation interface of Axin to interfere with its function in down-regulating β-catenin
    • Fiedler M, Mendoza-Topaz C, Rutherford TJ, Mieszczanek J, Bienz M (2011) Dishevelled interacts with the DIX domain oligomerisation interface of Axin to interfere with its function in down-regulating β-catenin. Proc Natl Acad Sci USA 108: 1937-1942.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 1937-1942
    • Fiedler, M.1    Mendoza-Topaz, C.2    Rutherford, T.J.3    Mieszczanek, J.4    Bienz, M.5
  • 47
    • 33745809820 scopus 로고    scopus 로고
    • Adenomatous polyposis coli (APC) differentially regulates beta-catenin phosphorylation and ubiquitination in colon cancer cells
    • DOI 10.1074/jbc.M600831200
    • Yang J, Zhang W, Evans PM, Chen X, He X et al. (2006) Adenomatous polyposis coli (APC) differentially regulates beta-catenin phosphorylation and ubiquitination in colon cancer cells. J Biol Chem 281: 17751-17757. (Pubitemid 44035574)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.26 , pp. 17751-17757
    • Yang, J.1    Zhang, W.2    Evans, P.M.3    Chen, X.4    He, X.5    Liu, C.6
  • 48
    • 84863012691 scopus 로고    scopus 로고
    • Adenomatous polyposis coli (APC) regulates multiple signaling pathways by enhancing glycogen synthase kinase-3 (GSK-3) activity
    • Valvezan AJ, Zhang F, Diehl JA, Klein PS (2012) Adenomatous polyposis coli (APC) regulates multiple signaling pathways by enhancing glycogen synthase kinase-3 (GSK-3) activity. J Biol Chem 287: 3823-3832.
    • (2012) J Biol Chem , vol.287 , pp. 3823-3832
    • Valvezan, A.J.1    Zhang, F.2    Diehl, J.A.3    Klein, P.S.4
  • 49
    • 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, 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. J Biol Chem 287: 28552-28563.
    • (2012) J Biol Chem , vol.287 , pp. 28552-28563
    • Tran, H.1    Polakis, P.2
  • 50
    • 0033577808 scopus 로고    scopus 로고
    • Domains of Axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization
    • DOI 10.1083/jcb.145.4.741
    • Fagotto F, Jho E, Zeng L, Kurth T, Joos T, et al. (1999) Domains of Axin involved in protein-protein interactions, Wnt pathway inhibition, and Intracellular localisation. J Cell Biol 145: 741-756. (Pubitemid 29240852)
    • (1999) Journal of Cell Biology , vol.145 , Issue.4 , pp. 741-756
    • Fagotto, F.1    Jho, E.-H.2    Zeng, L.3    Kurth, T.4    Joos, T.5    Kaufmann, C.6    Costantini, F.7
  • 52
    • 3042585855 scopus 로고    scopus 로고
    • Downregulation of beta-catenin by p53 involves changes in the rate of beta-catenin phosphorylation and Axin dynamics
    • DOI 10.1038/sj.onc.1207587
    • Levina E, Oren M, Ben-Ze'evA (2004) Downregulation of betacatenin by p53 involves changes in the rate of beta-catenin phosphorylation and Axin dynamics. Oncogene 23: 4444-4453. (Pubitemid 38850423)
    • (2004) Oncogene , vol.23 , Issue.25 , pp. 4444-4453
    • Levina, E.1    Oren, M.2    Ben-Ze'ev, A.3
  • 53
    • 1242272084 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic Shuttling of Axin, a Negative Regulator of the Wnt-beta-Catenin Pathway
    • DOI 10.1074/jbc.M307253200
    • Wiechens N, Heinle K, Englmeier L, Schohl A, Fagotto F (2004) Nucleo-cytoplasmic shuttling of Axin, a negative regulator of the Wnt-beta-catenin Pathway. J Biol Chem 279: 5263-5267. (Pubitemid 38220546)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5263-5267
    • Wiechens, N.1    Heinle, K.2    Englmeier, L.3    Schohl, A.4    Fagotto, F.5
  • 54
    • 0027930066 scopus 로고
    • The APC gene product associates with microtubules in vivo and promotes their assembly in vitro
    • Munemitsu S, Souza B, Müller O, Albert I, Rubinfeld B, et al. (1994) The APC gene product associates with microtubules in vivo and promotes their assembly in vitro. Cancer Res 54: 3676-3681. (Pubitemid 24241177)
    • (1994) Cancer Research , vol.54 , Issue.14 , pp. 3676-3681
    • Munemitsu, S.1    Souza, B.2    Muller, O.3    Albert, I.4    Rubinfeld, B.5    Polakis, P.6
  • 55
    • 0037054547 scopus 로고    scopus 로고
    • The adenomatous polyposis coli protein unambiguously localizes to microtubule plus ends and is involved in establishing parallel arrays of microtubule bundles in highly polarized epithelial cells
    • DOI 10.1083/jcb.200203001
    • Mogensuen MM, Tucker JB, Mackie JB, Prescott AR, Näthke IS (2002) The adenomatous polyposis coli protein unambiguously localises to microtubule plus ends and is involved in establishing parallel arrays of microtubule bundles in highly polarized epithelial cells. J Cell Biol 157: 1041-1048. (Pubitemid 34839778)
    • (2002) Journal of Cell Biology , vol.157 , Issue.6 , pp. 1041-1048
    • Mogensen, M.M.1    Tucker, J.B.2    Mackie, J.B.3    Prescott, A.R.4    Nathke, I.S.5
  • 57
    • 0027244942 scopus 로고
    • Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa
    • Linstedt AD, Hauri HP (1993) Giantin, a novel conserved Golgi membrane protein containing a cytoplasmic domain of at least 350 kDa. Mol Biol Cell 4: 679-93. (Pubitemid 23227154)
    • (1993) Molecular Biology of the Cell , vol.4 , Issue.7 , pp. 679-693
    • Linstedt, A.D.1    Hauri, H.-P.2
  • 59
    • 84879723716 scopus 로고    scopus 로고
    • Functional comparison of human Adenomatous Polyposis Coli (APC) and APC-Like in targeting beta-catenin for degradation
    • in press
    • Schneikert J, Vijaya Chandra SH, Ruppert JG, Ray S, Wenzel EM et al. (2013) Functional comparison of human Adenomatous Polyposis Coli (APC) and APC-Like in targeting beta-catenin for degradation. PloS ONE, in press.
    • (2013) PloS ONE
    • Schneikert, J.1    Vijaya Chandra, S.H.2    Ruppert, J.G.3    Ray, S.4    Wenzel, E.M.5
  • 60
    • 33646583259 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic distribution of beta-catenin is regulated by retention
    • Krieghoff E, Behrens J, Mayr B (2006) Nucleo-cytoplasmic distribution of beta-catenin is regulated by retention. J Cell Sci 119: 1453-1463.
    • (2006) J Cell Sci , vol.119 , pp. 1453-1463
    • Krieghoff, E.1    Behrens, J.2    Mayr, B.3
  • 61
    • 33846626414 scopus 로고    scopus 로고
    • Truncated APC regulates the transcriptional activity of beta-catenin in a cell cycle dependent manner
    • DOI 10.1093/hmg/ddl464
    • Schneikert J, Grohmann A, Behrens J (2007) Truncated APC regulates the transcriptional activity of beta-catenin in a cell cycle dependent manner. Hum Mol Genet 16: 199-209. (Pubitemid 46179002)
    • (2007) Human Molecular Genetics , vol.16 , Issue.2 , pp. 199-209
    • Schneikert, J.1    Grohmann, A.2    Behrens, J.3
  • 62
    • 0034602160 scopus 로고    scopus 로고
    • Complex formation of adenomatous polyposis coli gene product and axin facilitates glycogen synthase kinase-3 beta-dependent phosphorylation of beta-catenin and down-regulates beta-catenin
    • Hinoi T, Yamamoto H, Kishida M, Takada S, Kishida S et al. (2000) Complex formation of adenomatous polyposis coli gene product and axin facilitates glycogen synthase kinase-3 beta-dependent phosphorylation of beta-catenin and down-regulates beta-catenin. J Biol Chem 275: 34399-34406.
    • (2000) J Biol Chem , vol.275 , pp. 34399-34406
    • Hinoi, T.1    Yamamoto, H.2    Kishida, M.3    Takada, S.4    Kishida, S.5
  • 64
    • 68249083454 scopus 로고    scopus 로고
    • A targeted constitutive mutation in the APC tumor suppressor gene underlies mammary but not intestinal tumorigenesis
    • Gaspar C, Franken P, Molenaar L, Breukel C, van der Valk M, et al. (2009) A targeted constitutive mutation in the APC tumor suppressor gene underlies mammary but not intestinal tumorigenesis. PLoS Genet 5: e1000547.
    • (2009) PLoS Genet , vol.5
    • Gaspar, C.1    Franken, P.2    Molenaar, L.3    Breukel, C.4    Van Der Valk, M.5
  • 65
    • 84870690295 scopus 로고    scopus 로고
    • Kinetic responses of β-catenin specify the sites of Wnt control
    • Hernández AR, Klein AM, Kirschner MW (2012) Kinetic responses of β-catenin specify the sites of Wnt control. Science 338:1337-1340.
    • (2012) Science , vol.338 , pp. 1337-1340
    • Hernández, A.R.1    Klein, A.M.2    Kirschner, M.W.3
  • 67
    • 84859239880 scopus 로고    scopus 로고
    • A common role for various human truncated adenomatous polyposis coli isoforms in the control of Beta-catenin activity and cell proliferation
    • Vijaya-Chandra SH, Wacker I, Appelt UK, Behrens J, Schneikert J (2012) A common role for various human truncated adenomatous polyposis coli isoforms in the control of Beta-catenin activity and cell proliferation. PLoS One 7: e34479.
    • (2012) PLoS One , vol.7
    • Vijaya-Chandra, S.H.1    Wacker, I.2    Appelt, U.K.3    Behrens, J.4    Schneikert, J.5
  • 70
    • 0036166297 scopus 로고    scopus 로고
    • Wnt signals are transmitted through N-terminally dephosphorylated beta-catenin
    • DOI 10.1093/embo-reports/kvf002
    • Staal FJ, Noort MM, Strous GJ, Clevers HC (2002) Wnt signals are transmitted through N-terminally dephosphorylated beta-catenin. EMBO Rep 3: 63-68. (Pubitemid 34144817)
    • (2002) EMBO Reports , vol.3 , Issue.1 , pp. 63-68
    • Staal, F.J.T.1    Van Noort, M.2    Strous, G.J.3    Clevers, H.C.4
  • 71
    • 0022341148 scopus 로고
    • Dissociation of Madin-Darby canine kidney epithelial cells by the monoclonal antibody anti-Arc-1: Mechanistic aspects and identification of the antigen as a component related to uvomorulin
    • DOI 10.1083/jcb.101.4.1307
    • Behrens J, Birchmeier W, Goodman SL, Imhof BA (1985) Dissociation of Madin-Darby canine kidney epithelial cells by the monoclonal antibody anti-arc-1: mechanistic aspects and identification of the antigen as a component related to uvomorulin. J Cell Biol 101: 1307-1315. (Pubitemid 16203747)
    • (1985) Journal of Cell Biology , vol.101 , Issue.4 , pp. 1307-1315
    • Behrens, J.1    Birchmeier, W.2    Goodman, S.L.3    Imhof, B.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.