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Volumn 4, Issue 12, 1999, Pages 757-767

The deubiquitinating enzyme Fam interacts with and stabilizes β-catenin

Author keywords

[No Author keywords available]

Indexed keywords

BETA CATENIN; FAM PROTEIN; GUANOSINE TRIPHOSPHATASE; PROTEASOME; RAS PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 0033392501     PISSN: 13569597     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2443.1999.00297.x     Document Type: Article
Times cited : (121)

References (43)
  • 1
    • 0030978351 scopus 로고    scopus 로고
    • β-catenin is a target for the ubiquitin-proteasome pathway
    • Aberle, H., Bauer, A., Stappert, J., Kispert, A. & Kemler, R. (1997) β-catenin is a target for the ubiquitin-proteasome pathway. EMBO J. 16, 3797-3804.
    • (1997) EMBO J. , vol.16 , pp. 3797-3804
    • Aberle, H.1    Bauer, A.2    Stappert, J.3    Kispert, A.4    Kemler, R.5
  • 2
    • 0031692261 scopus 로고    scopus 로고
    • Cytomechanics of cadherin-mediated cell-cell adhesion
    • Adams, C.L. & Nelson, W.J. (1998) Cytomechanics of cadherin-mediated cell-cell adhesion. Curr. Opin. Cell Biol 10, 572-577.
    • (1998) Curr. Opin. Cell Biol , vol.10 , pp. 572-577
    • Adams, C.L.1    Nelson, W.J.2
  • 3
    • 0029781509 scopus 로고    scopus 로고
    • Functional interaction of β-catenin with the transcription factor LEF-1
    • Behrens, J., von Kries, J.P., Kuhl, M., et al. (1996) Functional interaction of β-catenin with the transcription factor LEF-1. Nature 382, 638-642.
    • (1996) Nature , vol.382 , pp. 638-642
    • Behrens, J.1    Von Kries, J.P.2    Kuhl, M.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 5
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K. & Goldberg, A.L. (1996) Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 6
    • 0031760462 scopus 로고    scopus 로고
    • Deubiquitinating enzymes, a new class of biological regulators
    • D'Andrea, A. & Pellman, D. (1998) Deubiquitinating enzymes, a new class of biological regulators. Crit. Rev. Biochem. Mol. Biol. 33, 337-352.
    • (1998) Crit. Rev. Biochem. Mol. Biol. , vol.33 , pp. 337-352
    • D'Andrea, A.1    Pellman, D.2
  • 7
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion, the molecular basis of tissue architecture and morphogenesis
    • Gumbiner, B.M. (1996) Cell adhesion, the molecular basis of tissue architecture and morphogenesis. Cell 84, 345-357.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 8
    • 0003448569 scopus 로고
    • Cold Spring Harbor, New York: Cold Spring Habor Laboratory Press
    • Harlow, E. & Lame, D. (1988) Antibodies: A Laboratory Manual. Cold Spring Harbor, New York: Cold Spring Habor Laboratory Press.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lame, D.2
  • 9
    • 0033602227 scopus 로고    scopus 로고
    • The F-box protein β-TrCP associates with phosphorylated β-catenin and regulates its activity in the cell
    • Hart, M., Concordet, J.P., Lassot, I., et al. (1999) The F-box protein β-TrCP associates with phosphorylated β-catenin and regulates its activity in the cell. Curr. Biol. 9, 207-210.
    • (1999) Curr. Biol. , vol.9 , pp. 207-210
    • Hart, M.1    Concordet, J.P.2    Lassot, I.3
  • 10
    • 0032492954 scopus 로고    scopus 로고
    • Downregulation of β-catenin by human Axin and its association with the APC tumor suppressor, β-catenin and GSK3-β
    • Hart, M.J., de los Santos, R., Albert, I.N., Rubinfeld, B. & Polakis, P. (1998) Downregulation of β-catenin by human Axin and its association with the APC tumor suppressor, β-catenin and GSK3-β. Curr. Biol. 10, 573-581.
    • (1998) Curr. Biol. , vol.10 , pp. 573-581
    • Hart, M.J.1    De Los Santos, R.2    Albert, I.N.3    Rubinfeld, B.4    Polakis, P.5
  • 12
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser, M. (1995) Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol. 7, 215-223.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 13
    • 0029561529 scopus 로고
    • Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene
    • Huang, Y., Baker, R.T. & Fischer-Vize, J.A. (1995) Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene. Science 270, 1828-1831.
    • (1995) Science , vol.270 , pp. 1828-1831
    • Huang, Y.1    Baker, R.T.2    Fischer-Vize, J.A.3
  • 14
    • 0029826308 scopus 로고    scopus 로고
    • Undifferentiated cells in the developing Drosophila eye influence facet assembly and require the Fat facets ubiquitin-specific protease
    • Huang, Y. & Fischer-Vize, J.A. (1996) Undifferentiated cells in the developing Drosophila eye influence facet assembly and require the Fat facets ubiquitin-specific protease. Development 122, 3207-3216.
    • (1996) Development , vol.122 , pp. 3207-3216
    • Huang, Y.1    Fischer-Vize, J.A.2
  • 15
    • 0345343608 scopus 로고    scopus 로고
    • Nuclear localization of β-catenin by interaction with transcription factor LEF-1
    • Huber, O., Korn, R., McLaughlin, J., Ohsugi, M., Herrmann, B.G. & Kemler, R. (1996) Nuclear localization of β-catenin by interaction with transcription factor LEF-1. Mech. Dev. 59, 3-10.
    • (1996) Mech. Dev. , vol.59 , pp. 3-10
    • Huber, O.1    Korn, R.2    McLaughlin, J.3    Ohsugi, M.4    Herrmann, B.G.5    Kemler, R.6
  • 16
    • 0032473355 scopus 로고    scopus 로고
    • Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3β and β-catenin and promotes GSK-3β-dependent phosphorylation of β-catenin
    • Ikeda, S., Kishida, S., Yamamoto, H., Murai, H., Koyama, S. & Kikuchi, A. (1998) Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3β and β-catenin and promotes GSK-3β-dependent phosphorylation of β-catenin. EMBO J. 17, 1371-1384.
    • (1998) EMBO J. , vol.17 , pp. 1371-1384
    • Ikeda, S.1    Kishida, S.2    Yamamoto, H.3    Murai, H.4    Koyama, S.5    Kikuchi, A.6
  • 17
    • 0032576777 scopus 로고    scopus 로고
    • Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb
    • Jiang, J. & Struhl, G. (1998) Regulation of the Hedgehog and Wingless signalling pathways by the F-box/WD40-repeat protein Slimb. Nature 391, 493-496.
    • (1998) Nature , vol.391 , pp. 493-496
    • Jiang, J.1    Struhl, G.2
  • 18
    • 0032079884 scopus 로고    scopus 로고
    • Axin, a negative regulator of the wnt signaling pathway, directly interacts with adenomatous polyposis coli and regulates the stabilization of β-catenin
    • Kishida, S., Yamamoto, H., Ikeda, S., et al. (1998) Axin, a negative regulator of the wnt signaling pathway, directly interacts with adenomatous polyposis coli and regulates the stabilization of β-catenin. J. Biol. Chem. 273, 10823-10826.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10823-10826
    • Kishida, S.1    Yamamoto, H.2    Ikeda, S.3
  • 19
    • 13344281006 scopus 로고    scopus 로고
    • Identification of AF-6 and canoe as putative targets for Ras
    • Kuriyama, M., Harada, N., Kuroda, S., et al. (1996) Identification of AF-6 and canoe as putative targets for Ras. J. Biol. Chem. 271, 607-610.
    • (1996) J. Biol. Chem. , vol.271 , pp. 607-610
    • Kuriyama, M.1    Harada, N.2    Kuroda, S.3
  • 20
    • 0032493903 scopus 로고    scopus 로고
    • Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin-mediated cell-cell adhesion
    • Kuroda, S., Fukata, M., Nakagawa, M., et al. (1998) Role of IQGAP1, a target of the small GTPases Cdc42 and Rac1, in regulation of E-cadherin-mediated cell-cell adhesion. Science 281, 832-835.
    • (1998) Science , vol.281 , pp. 832-835
    • Kuroda, S.1    Fukata, M.2    Nakagawa, M.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0033611567 scopus 로고    scopus 로고
    • The human F box protein β-TrCP associates with the Cul1/Skp1 complex and regulates the stability of β-catenin
    • Latres, E., Chiaur, D.S. & Pagano, M. (1999) The human F box protein β-TrCP associates with the Cul1/Skp1 complex and regulates the stability of β-catenin. Oncogene 18, 849-854.
    • (1999) Oncogene , vol.18 , pp. 849-854
    • Latres, E.1    Chiaur, D.S.2    Pagano, M.3
  • 23
    • 0032170327 scopus 로고    scopus 로고
    • β-TrCP is a negative regulator of Wnt/ β-catenin signaling pathway and dorsal axis formation in Xenopus embryos
    • Marikawa, Y. & Elinson, R.P. (1998) β-TrCP is a negative regulator of Wnt/ β-catenin signaling pathway and dorsal axis formation in Xenopus embryos. Mech. Dev. 77, 75-80.
    • (1998) Mech. Dev. , vol.77 , pp. 75-80
    • Marikawa, Y.1    Elinson, R.P.2
  • 24
    • 0029964851 scopus 로고    scopus 로고
    • Signal transduction through β-catenin and specification of cell fate during embryogenesis
    • Miller, J.R. & Moon, R.T. (1996) Signal transduction through β-catenin and specification of cell fate during embryogenesis. Genes Dev. 10, 2527-2539.
    • (1996) Genes Dev. , vol.10 , pp. 2527-2539
    • Miller, J.R.1    Moon, R.T.2
  • 25
    • 0001003110 scopus 로고    scopus 로고
    • XTcf-3 transcription factor mediates β-catenin-induced axis formation in Xenopus embryos
    • Molenaar, M., van de Wetering, M., Oosterwegel, M., et al. (1996) XTcf-3 transcription factor mediates β-catenin-induced axis formation in Xenopus embryos. Cell 86, 391-399.
    • (1996) Cell , vol.86 , pp. 391-399
    • Molenaar, M.1    Van De Wetering, M.2    Oosterwegel, M.3
  • 26
    • 0031866596 scopus 로고    scopus 로고
    • Direct association of presenilin-1 with β-catenin
    • Murayama, M., Tanaka, S., Palacino, J., et al. (1998) Direct association of presenilin-1 with β-catenin. FEBS Lett. 433, 73-77.
    • (1998) FEBS Lett. , vol.433 , pp. 73-77
    • Murayama, M.1    Tanaka, S.2    Palacino, J.3
  • 27
    • 0028087729 scopus 로고
    • The roles of catenins in the cadherin-mediated cell adhesion, functional analysis of E-cadherin-α-catenin fusion molecules
    • Nagafuchi, A., Ishihara, S. & Tsukita, S. (1994) The roles of catenins in the cadherin-mediated cell adhesion, functional analysis of E-cadherin-α-catenin fusion molecules. J. Cell Biol. 127, 235-245.
    • (1994) J. Cell Biol. , vol.127 , pp. 235-245
    • Nagafuchi, A.1    Ishihara, S.2    Tsukita, S.3
  • 28
    • 0030917251 scopus 로고    scopus 로고
    • A versatile transcriptional effector of Wingless signaling
    • Nusse, R. (1997) A versatile transcriptional effector of Wingless signaling. Cell 89, 321-323.
    • (1997) Cell , vol.89 , pp. 321-323
    • Nusse, R.1
  • 29
    • 0030779038 scopus 로고    scopus 로고
    • Serine phosphorylation-regulated ubiquitination and degradation of β-catenin
    • Orford, K., Crockett, C., Jensen, J.P., Weissman, A.M. & Byers, S.W. (1997) Serine phosphorylation-regulated ubiquitination and degradation of β-catenin. J. Biol. Chem. 272, 24735-24738.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24735-24738
    • Orford, K.1    Crockett, C.2    Jensen, J.P.3    Weissman, A.M.4    Byers, S.W.5
  • 30
    • 0029920839 scopus 로고    scopus 로고
    • Wnt-1 regulates free pools of catenins and stabilizes APC-catenin complexes
    • Papkoff, J., Rubinfeld, B., Schryver, B. & Polakis, P. (1996) Wnt-1 regulates free pools of catenins and stabilizes APC-catenin complexes. Mol. Cell. Biol. 16, 2128-2134.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2128-2134
    • Papkoff, J.1    Rubinfeld, B.2    Schryver, B.3    Polakis, P.4
  • 31
    • 0028569010 scopus 로고
    • Phosphorylation of the Drosophila adherens junction protein Armadillo, roles for wingless signal and zeste-white 3 kinase
    • Peifer, M., Pai, L.M. & Casey, M. (1994) Phosphorylation of the Drosophila adherens junction protein Armadillo, roles for wingless signal and zeste-white 3 kinase. Dev. Biol. 166, 543-556.
    • (1994) Dev. Biol. , vol.166 , pp. 543-556
    • Peifer, M.1    Pai, L.M.2    Casey, M.3
  • 32
    • 0031557898 scopus 로고    scopus 로고
    • The adenomatous polyposis coli (APC) tumor suppressor
    • Polakis, P. (1997) The adenomatous polyposis coli (APC) tumor suppressor. Biochim. Biophys. Acta. 1332, F127-F147.
    • (1997) Biochim. Biophys. Acta , vol.1332
    • Polakis, P.1
  • 33
    • 0027373678 scopus 로고
    • Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation
    • Prasad, R., Gu, Y., Alder, H., et al. (1993) Cloning of the ALL-1 fusion partner, the AF-6 gene, involved in acute myeloid leukemias with the t(6;11) chromosome translocation. Cancer Res. 53, 5624-5628.
    • (1993) Cancer Res. , vol.53 , pp. 5624-5628
    • Prasad, R.1    Gu, Y.2    Alder, H.3
  • 34
    • 0028953279 scopus 로고
    • The APC protein and E-cadherin form similar but independent complexes with α-catenin, β-catenin, and plakoglobin
    • Rubinfeld, B., Souza, B., Albert, I., Munemitsu, S. & Polakis, P. (1995) The APC protein and E-cadherin form similar but independent complexes with α-catenin, β-catenin, and plakoglobin. J. Biol. Chem. 270, 5549-5555.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5549-5555
    • Rubinfeld, B.1    Souza, B.2    Albert, I.3    Munemitsu, S.4    Polakis, P.5
  • 35
    • 0030900696 scopus 로고    scopus 로고
    • Stabilization of β-catenin by genetic defects in melanoma cell lines
    • Rubinfeld, B., Robbins, P., El-Gamil, M., Albert, I., Porfiri, E. & Polakis, P. (1997) Stabilization of β-catenin by genetic defects in melanoma cell lines. Science 275, 1790-1792.
    • (1997) Science , vol.275 , pp. 1790-1792
    • Rubinfeld, B.1    Robbins, P.2    El-Gamil, M.3    Albert, I.4    Porfiri, E.5    Polakis, P.6
  • 36
    • 0029160437 scopus 로고
    • Morphogenetic roles of classic cadherins
    • Takeichi, M. (1995) Morphogenetic roles of classic cadherins. Curr. Opin. Cell Biol. 7, 619-627.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 619-627
    • Takeichi, M.1
  • 37
    • 14444268087 scopus 로고    scopus 로고
    • The Ras target AF-6 is a substrate of the Fam deubiquitinating enzyme
    • Taya, S., Yamamoto, T., Kano, K., et al. (1998) The Ras target AF-6 is a substrate of the Fam deubiquitinating enzyme. J. Cell Biol. 142, 1053-1062.
    • (1998) J. Cell Biol. , vol.142 , pp. 1053-1062
    • Taya, S.1    Yamamoto, T.2    Kano, K.3
  • 38
    • 0026940189 scopus 로고
    • Molecular linkage between cadherins and actin filaments in cell-cell adherens junctions
    • Tsukita, S., Tsukita, S., Nagafuchi, A. & Yonemura, S. (1992) Molecular linkage between cadherins and actin filaments in cell-cell adherens junctions. Curr. Opin. Cell Biol. 4, 834-839.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 834-839
    • Tsukita, S.1    Tsukita, S.2    Nagafuchi, A.3    Yonemura, S.4
  • 39
    • 0030660073 scopus 로고    scopus 로고
    • Regulation of ubiquitin-dependent processes by deubiquitinating enzymes
    • Wilkinson, K.D. (1997) Regulation of ubiquitin-dependent processes by deubiquitinating enzymes. FASEB. J. 11, 1245-1256.
    • (1997) FASEB. J. , vol.11 , pp. 1245-1256
    • Wilkinson, K.D.1
  • 40
    • 0030959380 scopus 로고    scopus 로고
    • Cloning and expression analysis of a novel mouse gene with sequence similarity to the Drosophila fat facets gene
    • Wood, S.A., Pascoe, W.S., Ru, K., et al. (1997) Cloning and expression analysis of a novel mouse gene with sequence similarity to the Drosophila fat facets gene. Mech. Dev. 63, 29-38.
    • (1997) Mech. Dev. , vol.63 , pp. 29-38
    • Wood, S.A.1    Pascoe, W.S.2    Ru, K.3
  • 41
    • 0030724368 scopus 로고    scopus 로고
    • The Ras target AF-6 interacts with ZO-1 and serves as a peripheral component of tight junctions in epithelial cells
    • Yamamoto, T., Harada, N., Kano, K., et al. (1997) The Ras target AF-6 interacts with ZO-1 and serves as a peripheral component of tight junctions in epithelial cells. J. Cell Biol. 139, 785-795.
    • (1997) J. Cell Biol. , vol.139 , pp. 785-795
    • Yamamoto, T.1    Harada, N.2    Kano, K.3
  • 42
    • 0029683606 scopus 로고    scopus 로고
    • The axis-inducing activity, stability, and subcellular distribution of β-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3
    • Yost, C., Torres, M., Miller, J.R., Huang, E., Kimelman, D. & Moon, R.T. (1996) The axis-inducing activity, stability, and subcellular distribution of β-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3. Genes Dev. 10, 1443-1454.
    • (1996) Genes Dev. , vol.10 , pp. 1443-1454
    • Yost, C.1    Torres, M.2    Miller, J.R.3    Huang, E.4    Kimelman, D.5    Moon, R.T.6
  • 43
    • 0032531793 scopus 로고    scopus 로고
    • Destabilization of β-catenin by mutations in presenilin-1 potentiates neuronal apoptosis
    • Zhang, Z., Hartmann, H., Do, V.M., et al. (1998) Destabilization of β-catenin by mutations in presenilin-1 potentiates neuronal apoptosis. Nature 395, 698-702.
    • (1998) Nature , vol.395 , pp. 698-702
    • Zhang, Z.1    Hartmann, H.2    Do, V.M.3


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