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Volumn 34, Issue 23, 2014, Pages 4244-4256

Plakophilins 1 and 3 Bind to FXR1 and thereby influence the mRNA stability of desmosomal proteins

Author keywords

[No Author keywords available]

Indexed keywords

CATENIN; DESMOPLAKIN; FXR1 PROTEIN; G3BP PROTEIN; MESSENGER RNA; PABPC1 PROTEIN; PLAKOPHILIN; PLAKOPHILIN 1; PLAKOPHILIN 3; RIBONUCLEASE; RNA BINDING PROTEIN; UNCLASSIFIED DRUG; UPF1 PROTEIN; CARRIER PROTEIN; FXR1 PROTEIN, HUMAN; G3BP PROTEIN, HUMAN; PABPC1L PROTEIN, HUMAN; PKP1 PROTEIN, HUMAN; PKP3 PROTEIN, HUMAN; POLYADENYLIC ACID BINDING PROTEIN; PROTEIN BINDING; TRANSACTIVATOR PROTEIN; UPF1 PROTEIN, HUMAN;

EID: 84909582227     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00766-14     Document Type: Article
Times cited : (32)

References (90)
  • 1
    • 84862171364 scopus 로고    scopus 로고
    • The many faces and functions of beta-catenin
    • Valenta T, Hausmann G, Basler K. 2012. The many faces and functions of beta-catenin. EMBOJ. 31:2714-2736. http://dx.doi.org/10.1038/emboj .2012.150.
    • (2012) EMBOJ , vol.31 , pp. 2714-2736
    • Valenta, T.1    Hausmann, G.2    Basler, K.3
  • 2
    • 79251502958 scopus 로고    scopus 로고
    • The molecular evolution of the p120-catenin subfamily and its functional associations
    • Carnahan RH, Rokas A, Gaucher EA, Reynolds AB. 2010. The molecular evolution of the p120-catenin subfamily and its functional associations. PLoS One 5:e15747. http://dx.doi.org/10.1371/journal.pone.0015747.
    • (2010) PLoS One , vol.5 , pp. e15747
    • Carnahan, R.H.1    Rokas, A.2    Gaucher, E.A.3    Reynolds, A.B.4
  • 6
    • 33845383688 scopus 로고    scopus 로고
    • Plakophilins: multifunctional proteins or just regulators of desmosomal adhesion?
    • Hatzfeld M. 2007. Plakophilins: multifunctional proteins or just regulators of desmosomal adhesion? Biochim. Biophys. Acta 1773:69-77. http: //dx.doi.org/10.1016/j.bbamcr.2006.04.009.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 69-77
    • Hatzfeld, M.1
  • 7
    • 0041342100 scopus 로고    scopus 로고
    • Alterations in desmosome size and number coincide with the loss of keratinocyte cohesion in skin with homozygous and heterozygous defects in the desmosomal protein plakophilin 1
    • McMillan JR, Haftek M, Akiyama M, South AP, Perrot H, McGrath JA, Eady RA, Shimizu H. 2003. Alterations in desmosome size and number coincide with the loss of keratinocyte cohesion in skin with homozygous and heterozygous defects in the desmosomal protein plakophilin 1. J. Invest. Dermatol. 121:96-103. http://dx.doi.org/10.1046/j.1523-1747.2003 .12324.x.
    • (2003) J. Invest. Dermatol , vol.121 , pp. 96-103
    • McMillan, J.R.1    Haftek, M.2    Akiyama, M.3    South, A.P.4    Perrot, H.5    McGrath, J.A.6    Eady, R.A.7    Shimizu, H.8
  • 10
    • 84859242550 scopus 로고    scopus 로고
    • Functions of p120ctn isoforms in cell-cell adhesion and intracellular signaling
    • Pieters T, van Roy F, van Hengel J. 2012. Functions of p120ctn isoforms in cell-cell adhesion and intracellular signaling. Front. Biosci. 17:1669- 1694. http://dx.doi.org/10.2741/4012.
    • (2012) Front. Biosci , vol.17 , pp. 1669- 1694
    • Pieters, T.1    van Roy, F.2    van Hengel, J.3
  • 12
    • 0034009710 scopus 로고    scopus 로고
    • ARVCF localizes to the nucleus and adherens junction and is mutually exclusive with p120(ctn) in Ecadherin complexes
    • Mariner DJ, Wang J, Reynolds AB. 2000. ARVCF localizes to the nucleus and adherens junction and is mutually exclusive with p120(ctn) in Ecadherin complexes. J. Cell Sci. 113:1481-1490.
    • (2000) J. Cell Sci. , vol.113 , pp. 1481-1490
    • Mariner, D.J.1    Wang, J.2    Reynolds, A.B.3
  • 13
    • 70349333829 scopus 로고    scopus 로고
    • Plakophilins: multifunctional scaffolds for adhesion and signaling
    • Bass-Zubek AE, Godsel LM, Delmar M, Green KJ. 2009. Plakophilins: multifunctional scaffolds for adhesion and signaling. Curr. Opin. Cell Biol. 21:708-716. http://dx.doi.org/10.1016/j.ceb.2009.07.002.
    • (2009) Curr. Opin. Cell Biol , vol.21 , pp. 708-716
    • Bass-Zubek, A.E.1    Godsel, L.M.2    Delmar, M.3    Green, K.J.4
  • 15
    • 77149147440 scopus 로고    scopus 로고
    • The catenin family at a glance
    • McCrea PD, Gu D. 2010. The catenin family at a glance. J. Cell Sci. 123:637-642. http://dx.doi.org/10.1242/jcs.039842.
    • (2010) J. Cell Sci , vol.123 , pp. 637-642
    • McCrea, P.D.1    Gu, D.2
  • 16
    • 0030856140 scopus 로고    scopus 로고
    • Plakophilins 1a and 1b: widespread nuclear proteins recruited in specific epithelial cells as desmosomal plaque components
    • Schmidt A, Langbein L, Rode M, Pratzel S, Zimbelmann R, Franke WW. 1997. Plakophilins 1a and 1b: widespread nuclear proteins recruited in specific epithelial cells as desmosomal plaque components. Cell Tissue Res. 290:481-499. http://dx.doi.org/10.1007/s004410050956.
    • (1997) Cell Tissue Res , vol.290 , pp. 481-499
    • Schmidt, A.1    Langbein, L.2    Rode, M.3    Pratzel, S.4    Zimbelmann, R.5    Franke, W.W.6
  • 18
    • 0034932143 scopus 로고    scopus 로고
    • Nuclear particles containing RNA polymerase III complexes associated with the junctional plaque protein plakophilin 2
    • Mertens C, Hofmann I, Wang Z, Teichmann M, Sepehri Chong S, Schnolzer M, Franke WW. 2001. Nuclear particles containing RNA polymerase III complexes associated with the junctional plaque protein plakophilin 2. Proc. Natl. Acad. Sci. U. S. A. 98:7795-7800. http://dx.doi.org/10 .1073/pnas.141219498.
    • (2001) Proc. Natl. Acad. Sci. U. S. A , vol.98 , pp. 7795-7800
    • Mertens, C.1    Hofmann, I.2    Wang, Z.3    Teichmann, M.4    Sepehri Chong, S.5    Schnolzer, M.6    Franke, W.W.7
  • 19
    • 0029825414 scopus 로고    scopus 로고
    • Plakophilins 2a and 2b: constitutive proteins of dual location in the karyoplasm and the desmosomal plaque
    • Mertens C, Kuhn C, Franke WW. 1996. Plakophilins 2a and 2b: constitutive proteins of dual location in the karyoplasm and the desmosomal plaque. J. Cell Biol. 135:1009-1025. http://dx.doi.org/10.1083/jcb.135.4 .1009.
    • (1996) J. Cell Biol , vol.135 , pp. 1009-1025
    • Mertens, C.1    Kuhn, C.2    Franke, W.W.3
  • 20
    • 33644854767 scopus 로고    scopus 로고
    • Identification of the junctional plaque protein plakophilin 3 in cytoplasmic particles containing RNA-binding proteins and the recruitment of plakophilins 1 and 3 to stress granules
    • Hofmann I, Casella M, Schnolzer M, Schlechter T, Spring H, Franke WW.2006. Identification of the junctional plaque protein plakophilin 3 in cytoplasmic particles containing RNA-binding proteins and the recruitment of plakophilins 1 and 3 to stress granules. Mol. Biol. Cell 17:1388- 1398. http://dx.doi.org/10.1091/mbc.E05-08-0708.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1388-1398
    • Hofmann, I.1    Casella, M.2    Schnolzer, M.3    Schlechter, T.4    Spring, H.5    Franke, W.W.6
  • 21
    • 84884155152 scopus 로고    scopus 로고
    • Plakophilin-associated RNA-binding proteins in prostate cancer and their implications in tumor progression and metastasis
    • Yang C, Strobel P, Marx A, Hofmann I. 2013. Plakophilin-associated RNA-binding proteins in prostate cancer and their implications in tumor progression and metastasis. Virchows Arch. 463:379-390. http://dx.doi .org/10.1007/s00428-013-1452-y.
    • (2013) Virchows Arch , vol.463 , pp. 379-390
    • Yang, C.1    Strobel, P.2    Marx, A.3    Hofmann, I.4
  • 22
    • 38449123517 scopus 로고    scopus 로고
    • Mammalian stress granules and processing bodies
    • Kedersha N, Anderson P. 2007. Mammalian stress granules and processing bodies. Methods Enzymol. 431:61-81. http://dx.doi.org/10.1016 /S0076-6879(07)31005-7.
    • (2007) Methods Enzymol , vol.431 , pp. 61-81
    • Kedersha, N.1    Anderson, P.2
  • 23
    • 33947262696 scopus 로고    scopus 로고
    • AU-rich-element-mediated upregulation of translation by FXR1 and Argonaute 2
    • Vasudevan S, Steitz JA. 2007. AU-rich-element-mediated upregulation of translation by FXR1 and Argonaute 2. Cell 128:1105-1118. http://dx .doi.org/10.1016/j.cell.2007.01.038.
    • (2007) Cell , vol.128 , pp. 1105-1118
    • Vasudevan, S.1    Steitz, J.A.2
  • 24
    • 14044275840 scopus 로고    scopus 로고
    • Fragile X-related protein FXR1P regulates proinflammatory cytokine tumor necrosis factor expression at the post-transcriptional level
    • Garnon J, Lachance C, Di Marco S, Hel Z, Marion D, Ruiz MC, Newkirk MM, Khandjian EW, Radzioch D. 2005. Fragile X-related protein FXR1P regulates proinflammatory cytokine tumor necrosis factor expression at the post-transcriptional level. J. Biol. Chem. 280:5750-5763. http://dx.doi.org/10.1074/jbc.M401988200.
    • (2005) J. Biol. Chem , vol.280 , pp. 5750-5763
    • Garnon, J.1    Lachance, C.2    Di Marco, S.3    Hel, Z.4    Marion, D.5    Ruiz, M.C.6    Newkirk, M.M.7    Khandjian, E.W.8    Radzioch, D.9
  • 25
    • 35148892615 scopus 로고    scopus 로고
    • Posttranscriptional gene expression regulation in CpG-activated macrophages depends on FXR1P RNA-binding protein
    • Lachance C, Thuraisingam T, Garnon J, Roter E, Radzioch D. 2007. Posttranscriptional gene expression regulation in CpG-activated macrophages depends on FXR1P RNA-binding protein. FEMS Immunol. Med. Microbiol. 51:422- 430. http://dx.doi.org/10.1111/j.1574-695X .2007.00317.x.
    • (2007) FEMS Immunol. Med. Microbiol , vol.51 , pp. 422- 430
    • Lachance, C.1    Thuraisingam, T.2    Garnon, J.3    Roter, E.4    Radzioch, D.5
  • 26
    • 77953550540 scopus 로고    scopus 로고
    • Fragile X-related protein FXR1 controls post-transcriptional suppression of lipopolysaccharide-induced tumour necrosis factor-alpha production by transforming growth factorbeta1
    • Khera TK, Dick AD, Nicholson LB. 2010. Fragile X-related protein FXR1 controls post-transcriptional suppression of lipopolysaccharide-induced tumour necrosis factor-alpha production by transforming growth factorbeta1. FEBS J. 277:2754-2765. http://dx.doi.org/10.1111/j.1742-4658 .2010.07692.x.
    • (2010) FEBS J , vol.277 , pp. 2754-2765
    • Khera, T.K.1    Dick, A.D.2    Nicholson, L.B.3
  • 27
    • 13144276292 scopus 로고    scopus 로고
    • Rasputin, more promiscuous than ever: a review of G3BP
    • Irvine K, Stirling R, Hume D, Kennedy D. 2004. Rasputin, more promiscuous than ever: a review of G3BP. Int. J. Dev. Biol. 48:1065-1077. http://dx.doi.org/10.1387/ijdb.041893ki.
    • (2004) Int. J. Dev. Biol , vol.48 , pp. 1065-1077
    • Irvine, K.1    Stirling, R.2    Hume, D.3    Kennedy, D.4
  • 28
    • 75149146546 scopus 로고    scopus 로고
    • Endoribonucleases-enzymes gaining spotlight in mRNA metabolism
    • Li WM, Barnes T, Lee CH. 2010. Endoribonucleases-enzymes gaining spotlight in mRNA metabolism. FEBS J. 277:627-641. http://dx.doi.org /10.1111/j.1742-4658.2009.07488.x.
    • (2010) FEBS J , vol.277 , pp. 627-641
    • Li, W.M.1    Barnes, T.2    Lee, C.H.3
  • 29
    • 77955994655 scopus 로고    scopus 로고
    • Human G3BP1 interacts with beta-F1-ATPase mRNA and inhibits its translation
    • Ortega AD, Willers IM, Sala S, Cuezva JM. 2010. Human G3BP1 interacts with beta-F1-ATPase mRNA and inhibits its translation. J. Cell Sci. 123:2685-2696. http://dx.doi.org/10.1242/jcs.065920.
    • (2010) J. Cell Sci , vol.123 , pp. 2685-2696
    • Ortega, A.D.1    Willers, I.M.2    Sala, S.3    Cuezva, J.M.4
  • 30
    • 0038487811 scopus 로고    scopus 로고
    • Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression
    • Mangus DA, Evans MC, Jacobson A. 2003. Poly(A)-binding proteins: multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol. 4:223. http://dx.doi.org/10.1186/gb-2003-4-7 -223.
    • (2003) Genome Biol , vol.4 , pp. 223
    • Mangus, D.A.1    Evans, M.C.2    Jacobson, A.3
  • 31
    • 46249091565 scopus 로고    scopus 로고
    • Translation factors promote the formation of two states of the closed-loop mRNP
    • Amrani N, Ghosh S, Mangus DA, Jacobson A. 2008. Translation factors promote the formation of two states of the closed-loop mRNP. Nature 453:1276-1280. http://dx.doi.org/10.1038/nature06974.
    • (2008) Nature , vol.453 , pp. 1276-1280
    • Amrani, N.1    Ghosh, S.2    Mangus, D.A.3    Jacobson, A.4
  • 32
    • 0344758983 scopus 로고    scopus 로고
    • Starting the protein synthesis machine: eukaryotic translation initiation
    • Preiss T, Hentze MW. 2003. Starting the protein synthesis machine: eukaryotic translation initiation. Bioessays 25:1201-1211. http://dx.doi .org/10.1002/bies.10362.
    • (2003) Bioessays , vol.25 , pp. 1201-1211
    • Preiss, T.1    Hentze, M.W.2
  • 33
    • 55449106579 scopus 로고    scopus 로고
    • Poly(A)-binding proteininteracting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation
    • Martineau Y, Derry MC, Wang X, Yanagiya A, Berlanga JJ, Shyu AB, Imataka H, Gehring K, Sonenberg N. 2008. Poly(A)-binding proteininteracting protein 1 binds to eukaryotic translation initiation factor 3 to stimulate translation. Mol. Cell. Biol. 28:6658-6667. http://dx.doi.org/10 .1128/MCB.00738-08.
    • (2008) Mol. Cell. Biol , vol.28 , pp. 6658-6667
    • Martineau, Y.1    Derry, M.C.2    Wang, X.3    Yanagiya, A.4    Berlanga, J.J.5    Shyu, A.B.6    Imataka, H.7    Gehring, K.8    Sonenberg, N.9
  • 34
    • 0034282752 scopus 로고    scopus 로고
    • Multiple portions of poly(A)-binding protein stimulate translation in vivo
    • Gray NK, Coller JM, Dickson KS, Wickens M. 2000. Multiple portions of poly(A)-binding protein stimulate translation in vivo. EMBO J. 19: 4723-4733. http://dx.doi.org/10.1093/emboj/19.17.4723.
    • (2000) EMBO J , vol.19 , pp. 4723-4733
    • Gray, N.K.1    Coller, J.M.2    Dickson, K.S.3    Wickens, M.4
  • 35
    • 77951622022 scopus 로고    scopus 로고
    • Role of GW182 proteins and PABPC1 in the miRNA pathway: a sense of deja vu
    • Tritschler F, Huntzinger E, Izaurralde E. 2010. Role of GW182 proteins and PABPC1 in the miRNA pathway: a sense of deja vu. Nat. Rev. Mol. Cell Biol. 11:379-384. http://dx.doi.org/10.1038/nrm2885.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 379-384
    • Tritschler, F.1    Huntzinger, E.2    Izaurralde, E.3
  • 37
    • 71949121493 scopus 로고    scopus 로고
    • The silencing domain of GW182 interacts with PABPC1 to promote translational repression and degradation of microRNA targets and is required for target release
    • Zekri L, Huntzinger E, Heimstadt S, Izaurralde E. 2009. The silencing domain of GW182 interacts with PABPC1 to promote translational repression and degradation of microRNA targets and is required for target release. Mol. Cell. Biol. 29:6220-6231. http://dx.doi.org/10.1128/MCB .01081-09.
    • (2009) Mol. Cell. Biol , vol.29 , pp. 6220-6231
    • Zekri, L.1    Huntzinger, E.2    Heimstadt, S.3    Izaurralde, E.4
  • 38
    • 78650258635 scopus 로고    scopus 로고
    • Two PABPC1-binding sites in GW182 proteins promote miRNA-mediated gene silencing
    • Huntzinger E, Braun JE, Heimstadt S, Zekri L, Izaurralde E. 2010. Two PABPC1-binding sites in GW182 proteins promote miRNA-mediated gene silencing. EMBO J. 29:4146-4160. http://dx.doi.org/10.1038/emboj .2010.274.
    • (2010) EMBO J , vol.29 , pp. 4146-4160
    • Huntzinger, E.1    Braun, J.E.2    Heimstadt, S.3    Zekri, L.4    Izaurralde, E.5
  • 39
    • 0036759339 scopus 로고    scopus 로고
    • Poly(A)-binding protein and eRF3 are associated in vivo in human and Xenopus cells
    • Cosson B, Berkova N, Couturier A, Chabelskaya S, Philippe M, Zhouravleva G. 2002. Poly(A)-binding protein and eRF3 are associated in vivo in human and Xenopus cells. Biol. Cell 94:205-216. http://dx.doi.org /10.1016/S0248-4900(02)01194-2.
    • (2002) Biol. Cell , vol.94 , pp. 205-216
    • Cosson, B.1    Berkova, N.2    Couturier, A.3    Chabelskaya, S.4    Philippe, M.5    Zhouravleva, G.6
  • 40
    • 40949148553 scopus 로고    scopus 로고
    • Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways
    • Ivanov PV, Gehring NH, Kunz JB, Hentze MW, Kulozik AE. 2008. Interactions between UPF1, eRFs, PABP and the exon junction complex suggest an integrated model for mammalian NMD pathways. EMBO J. 27:736-747. http://dx.doi.org/10.1038/emboj.2008.17.
    • (2008) EMBO J , vol.27 , pp. 736-747
    • Ivanov, P.V.1    Gehring, N.H.2    Kunz, J.B.3    Hentze, M.W.4    Kulozik, A.E.5
  • 41
    • 77958459763 scopus 로고    scopus 로고
    • Upf1 senses 3'UTR length to potentiate mRNA decay
    • Hogg JR, Goff SP. 2010. Upf1 senses 3'UTR length to potentiate mRNA decay. Cell 143:379-389. http://dx.doi.org/10.1016/j.cell.2010.10.005.
    • (2010) Cell , vol.143 , pp. 379-389
    • Hogg, J.R.1    Goff, S.P.2
  • 42
    • 77949904260 scopus 로고    scopus 로고
    • Nonsense-mediated mRNA decay in human cells: mechanistic insights, functions beyond quality control and the double-life of NMD factors
    • Nicholson P, Yepiskoposyan H, Metze S, Zamudio Orozco R, Kleinschmidt N, Muhlemann O. 2010. Nonsense-mediated mRNA decay in human cells: mechanistic insights, functions beyond quality control and the double-life of NMD factors. Cell. Mol. Life Sci. 67:677-700. http://dx .doi.org/10.1007/s00018-009-0177-1.
    • (2010) Cell. Mol. Life Sci , vol.67 , pp. 677-700
    • Nicholson, P.1    Yepiskoposyan, H.2    Metze, S.3    Zamudio Orozco, R.4    Kleinschmidt, N.5    Muhlemann, O.6
  • 43
    • 84867850145 scopus 로고    scopus 로고
    • NMD: a multifaceted response to premature translational termination
    • Kervestin S, Jacobson A. 2012. NMD: a multifaceted response to premature translational termination. Nat. Rev. Mol. Cell Biol. 13:700-712. http: //dx.doi.org/10.1038/nrm3454.
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 700-712
    • Kervestin, S.1    Jacobson, A.2
  • 44
    • 0029348072 scopus 로고
    • Purification and characterization of the Upf1 protein: a factor involved in translation and mRNA degradation
    • Czaplinski K, Weng Y, Hagan KW, Peltz SW. 1995. Purification and characterization of the Upf1 protein: a factor involved in translation and mRNA degradation. RNA 1:610-623.
    • (1995) RNA , vol.1 , pp. 610-623
    • Czaplinski, K.1    Weng, Y.2    Hagan, K.W.3    Peltz, S.W.4
  • 45
    • 46049110089 scopus 로고    scopus 로고
    • The meaning of nonsense
    • Stalder L, Muhlemann O. 2008. The meaning of nonsense. Trends Cell Biol. 18:315-321. http://dx.doi.org/10.1016/j.tcb.2008.04.005.
    • (2008) Trends Cell Biol , vol.18 , pp. 315-321
    • Stalder, L.1    Muhlemann, O.2
  • 46
    • 69249215256 scopus 로고    scopus 로고
    • The modern RNP world of eukaryotes
    • Collins LJ, Kurland CG, Biggs P, Penny D. 2009. The modern RNP world of eukaryotes. J. Hered. 100:597-604. http://dx.doi.org/10.1093 /jhered/esp064.
    • (2009) J. Hered , vol.100 , pp. 597-604
    • Collins, L.J.1    Kurland, C.G.2    Biggs, P.3    Penny, D.4
  • 47
    • 44449166478 scopus 로고    scopus 로고
    • RNA-binding proteins and post-transcriptional gene regulation
    • Glisovic T, Bachorik JL, Yong J, Dreyfuss G. 2008. RNA-binding proteins and post-transcriptional gene regulation. FEBS Lett. 582:1977-1986. http://dx.doi.org/10.1016/j.febslet.2008.03.004.
    • (2008) FEBS Lett , vol.582 , pp. 1977-1986
    • Glisovic, T.1    Bachorik, J.L.2    Yong, J.3    Dreyfuss, G.4
  • 48
    • 0036289532 scopus 로고    scopus 로고
    • Eukaryotic mRNPs may represent posttranscriptional operons
    • Keene JD, Tenenbaum SA. 2002. Eukaryotic mRNPs may represent posttranscriptional operons. Mol. Cell 9:1161-1167. http://dx.doi.org/10 .1016/S1097-2765(02)00559-2.
    • (2002) Mol. Cell , vol.9 , pp. 1161-1167
    • Keene, J.D.1    Tenenbaum, S.A.2
  • 49
    • 77952015221 scopus 로고    scopus 로고
    • Desmosomal plakophilins in the prostate and prostatic adenocarcinomas: implications for diagnosis and tumor progression
    • Breuninger S, Reidenbach S, Sauer CG, Strobel P, Pfitzenmaier J, Trojan L, Hofmann I. 2010. Desmosomal plakophilins in the prostate and prostatic adenocarcinomas: implications for diagnosis and tumor progression. Am. J. Pathol. 176:2509-2519. http://dx.doi.org/10.2353 /ajpath.2010.090737.
    • (2010) Am. J. Pathol , vol.176 , pp. 2509-2519
    • Breuninger, S.1    Reidenbach, S.2    Sauer, C.G.3    Strobel, P.4    Pfitzenmaier, J.5    Trojan, L.6    Hofmann, I.7
  • 51
    • 0036773207 scopus 로고    scopus 로고
    • Optimizing radiation-responsive gene promoters for radiogenetic cancer therapy
    • Scott SD, Joiner MC, Marples B. 2002. Optimizing radiation-responsive gene promoters for radiogenetic cancer therapy. Gene Ther. 9:1396-1402. http://dx.doi.org/10.1038/sj.gt.3301822.
    • (2002) Gene Ther , vol.9 , pp. 1396-1402
    • Scott, S.D.1    Joiner, M.C.2    Marples, B.3
  • 52
    • 80052979901 scopus 로고    scopus 로고
    • RNA homeostasis governed by cell typespecific and branched feedback loops acting on NMD
    • Huang L, Lou CH, Chan W, Shum EY, Shao A, Stone E, Karam R, Song HW, Wilkinson MF. 2011. RNA homeostasis governed by cell typespecific and branched feedback loops acting on NMD. Mol. Cell 43:950- 961. http://dx.doi.org/10.1016/j.molcel.2011.06.031.
    • (2011) Mol. Cell , vol.43 , pp. 950- 961
    • Huang, L.1    Lou, C.H.2    Chan, W.3    Shum, E.Y.4    Shao, A.5    Stone, E.6    Karam, R.7    Song, H.W.8    Wilkinson, M.F.9
  • 53
    • 77955339642 scopus 로고    scopus 로고
    • UPF1 association with the cap-binding protein, CBP80, promotes nonsense-mediated mRNA decay at two distinct steps
    • Hwang J, Sato H, Tang Y, Matsuda D, Maquat LE. 2010. UPF1 association with the cap-binding protein, CBP80, promotes nonsense-mediated mRNA decay at two distinct steps. Mol. Cell 39:396-409. http://dx.doi .org/10.1016/j.molcel.2010.07.004.
    • (2010) Mol. Cell , vol.39 , pp. 396-409
    • Hwang, J.1    Sato, H.2    Tang, Y.3    Matsuda, D.4    Maquat, L.E.5
  • 54
    • 12944327374 scopus 로고    scopus 로고
    • Mammalian Staufen1 recruits Upf1 to specific mRNA 3'UTRs so as to elicit mRNA decay
    • Kim YK, Furic L, Desgroseillers L, Maquat LE. 2005. Mammalian Staufen1 recruits Upf1 to specific mRNA 3'UTRs so as to elicit mRNA decay. Cell 120:195-208. http://dx.doi.org/10.1016/j.cell.2004.11.050.
    • (2005) Cell , vol.120 , pp. 195-208
    • Kim, Y.K.1    Furic, L.2    Desgroseillers, L.3    Maquat, L.E.4
  • 55
    • 79961032285 scopus 로고    scopus 로고
    • Desmoplakin and talin2 are novel mRNA targets of fragile x-related protein-1 in cardiac muscle
    • Whitman SA, Cover C, Yu L, Nelson DL, Zarnescu DC, Gregorio CC. Desmoplakin and talin2 are novel mRNA targets of fragile x-related protein-1 in cardiac muscle. Circ. Res. 109:262-271. http://dx.doi.org/10 .1161/CIRCRESAHA.111.244244.
    • Circ. Res. , vol.109 , pp. 262-271
    • Whitman, S.A.1    Cover, C.2    Yu, L.3    Nelson, D.L.4    Zarnescu, D.C.5    Gregorio, C.C.6
  • 56
    • 0033868312 scopus 로고    scopus 로고
    • Interaction of plakophilins with desmoplakin and intermediate filament proteins: an in vitro analysis
    • Hofmann I, Mertens C, Brettel M, Nimmrich V, Schnolzer M, Herrmann H. 2000. Interaction of plakophilins with desmoplakin and intermediate filament proteins: an in vitro analysis. J. Cell Sci. 113:2471- 2483.
    • (2000) J. Cell Sci. , vol.113 , pp. 2471- 2483
    • Hofmann, I.1    Mertens, C.2    Brettel, M.3    Nimmrich, V.4    Schnolzer, M.5    Herrmann, H.6
  • 57
    • 0029972935 scopus 로고    scopus 로고
    • Specific sequences in the fragile X syndrome protein FMR1 and the FXR proteins mediate their binding to 60S ribosomal subunits and the interactions among them
    • Siomi MC, Zhang Y, Siomi H, Dreyfuss G. 1996. Specific sequences in the fragile X syndrome protein FMR1 and the FXR proteins mediate their binding to 60S ribosomal subunits and the interactions among them. Mol. Cell. Biol. 16:3825-3832.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3825-3832
    • Siomi, M.C.1    Zhang, Y.2    Siomi, H.3    Dreyfuss, G.4
  • 58
    • 0033612248 scopus 로고    scopus 로고
    • Reduced mRNA for G3BP in fragile X cells: evidence of FMR1 gene regulation
    • Zhong N, Ju W, Nelson D, Dobkin C, Brown WT. 1999. Reduced mRNA for G3BP in fragile X cells: evidence of FMR1 gene regulation. Am. J. Med. Genet. 84:268-271. http://dx.doi.org/10.1002/(SICI)1096-8628 (19990528)84:3<268::AID-AJMG20>3.0.CO;2-#.
    • (1999) Am. J. Med. Genet , vol.84 , pp. 268-271
    • Zhong, N.1    Ju, W.2    Nelson, D.3    Dobkin, C.4    Brown, W.T.5
  • 62
    • 0035199158 scopus 로고    scopus 로고
    • Desmoplakin is essential in epidermal sheet formation
    • Vasioukhin V, Bowers E, Bauer C, Degenstein L, Fuchs E. 2001. Desmoplakin is essential in epidermal sheet formation. Nat. Cell Biol. 3:1076- 1085. http://dx.doi.org/10.1038/ncb1201-1076.
    • (2001) Nat. Cell Biol , vol.3 , pp. 1076- 1085
    • Vasioukhin, V.1    Bowers, E.2    Bauer, C.3    Degenstein, L.4    Fuchs, E.5
  • 63
    • 0031005659 scopus 로고    scopus 로고
    • The zinc-finger protein slug causes desmosome dissociation, an initial and necessary step for growth factor-induced epithelial-mesenchymal transition
    • Savagner P, Yamada KM, Thiery JP. 1997. The zinc-finger protein slug causes desmosome dissociation, an initial and necessary step for growth factor-induced epithelial-mesenchymal transition. J. Cell Biol. 137:1403- 1419. http://dx.doi.org/10.1083/jcb.137.6.1403.
    • (1997) J. Cell Biol , vol.137 , pp. 1403- 1419
    • Savagner, P.1    Yamada, K.M.2    Thiery, J.P.3
  • 65
    • 0042738101 scopus 로고    scopus 로고
    • Functional analysis of C-TAK1 substrate binding and identification of PKP2 as a new C-TAK1 substrate
    • Muller J, Ritt DA, Copeland TD, Morrison DK. 2003. Functional analysis of C-TAK1 substrate binding and identification of PKP2 as a new C-TAK1 substrate. EMBO J. 22:4431-4442. http://dx.doi.org/10.1093 /emboj/cdg426.
    • (2003) EMBO J , vol.22 , pp. 4431-4442
    • Muller, J.1    Ritt, D.A.2    Copeland, T.D.3    Morrison, D.K.4
  • 66
    • 0023864445 scopus 로고
    • Kinetics of desmosome assembly in Madin- Darby canine kidney epithelial cells: temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact
    • Pasdar M, Nelson WJ. 1988. Kinetics of desmosome assembly in Madin- Darby canine kidney epithelial cells: temporal and spatial regulation of desmoplakin organization and stabilization upon cell-cell contact. I. Biochemical analysis. J. Cell Biol. 106:677-685.
    • (1988) I. Biochemical analysis. J. Cell Biol. , vol.106 , pp. 677-685
    • Pasdar, M.1    Nelson, W.J.2
  • 67
    • 33845411513 scopus 로고    scopus 로고
    • p120-catenin: past and present
    • Reynolds AB. 2007. p120-catenin: past and present. Biochim. Biophys. Acta 1773:2-7. http://dx.doi.org/10.1016/j.bbamcr.2006.09.019.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 2-7
    • Reynolds, A.B.1
  • 68
    • 33845400338 scopus 로고    scopus 로고
    • Diverse functions of p120ctn in tumors
    • van Hengel J, van Roy F. 2007. Diverse functions of p120ctn in tumors. Biochim. Biophys. Acta 1773:78-88. http://dx.doi.org/10.1016/j.bbamcr .2006.08.033.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 78-88
    • van Hengel, J.1    van Roy, F.2
  • 69
    • 7944227353 scopus 로고    scopus 로고
    • Emerging roles for p120-catenin in cell adhesion and cancer
    • Reynolds AB, Roczniak-Ferguson A. 2004. Emerging roles for p120-catenin in cell adhesion and cancer. Oncogene 23:7947-7956. http://dx .doi.org/10.1038/sj.onc.1208161.
    • (2004) Oncogene , vol.23 , pp. 7947-7956
    • Reynolds, A.B.1    Roczniak-Ferguson, A.2
  • 70
    • 33746808398 scopus 로고    scopus 로고
    • Wnt/beta-catenin signaling in development and disease
    • Clevers H. 2006. Wnt/beta-catenin signaling in development and disease. Cell 127:469-480. http://dx.doi.org/10.1016/j.cell.2006.10.018.
    • (2006) Cell , vol.127 , pp. 469-480
    • Clevers, H.1
  • 71
    • 77954112841 scopus 로고    scopus 로고
    • Epigenetic disruption of the WNT/beta-catenin signaling pathway in human cancers
    • Ying Y, Tao Q. 2009. Epigenetic disruption of the WNT/beta-catenin signaling pathway in human cancers. Epigenetics 4:307-312. http://dx.doi .org/10.4161/epi.4.5.9371.
    • (2009) Epigenetics , vol.4 , pp. 307-312
    • Ying, Y.1    Tao, Q.2
  • 72
    • 37849005006 scopus 로고    scopus 로고
    • NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity
    • Chamieh H, Ballut L, Bonneau F, Le Hir H. 2008. NMD factors UPF2 and UPF3 bridge UPF1 to the exon junction complex and stimulate its RNA helicase activity. Nat. Struct. Mol. Biol. 15:85-93. http://dx.doi.org /10.1038/nsmb1330.
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 85-93
    • Chamieh, H.1    Ballut, L.2    Bonneau, F.3    Le Hir, H.4
  • 73
    • 0037112805 scopus 로고    scopus 로고
    • Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression
    • Mazroui R, Huot ME, Tremblay S, Filion C, Labelle Y, Khandjian EW. Trapping of messenger RNA by Fragile X Mental Retardation protein into cytoplasmic granules induces translation repression. Hum. Mol. Genet. 11:3007-3017. http://dx.doi.org/10.1093/hmg/11.24.3007.
    • Hum. Mol. Genet. , vol.11 , pp. 3007-3017
    • Mazroui, R.1    Huot, M.E.2    Tremblay, S.3    Filion, C.4    Labelle, Y.5    Khandjian, E.W.6
  • 74
    • 34249316905 scopus 로고    scopus 로고
    • RNA-binding proteins: modular design for efficient function
    • Lunde BM, Moore C, Varani G. 2007. RNA-binding proteins: modular design for efficient function. Nat. Rev. Mol. Cell Biol. 8:479-490. http: //dx.doi.org/10.1038/nrm2178.
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 479-490
    • Lunde, B.M.1    Moore, C.2    Varani, G.3
  • 78
    • 12344281930 scopus 로고    scopus 로고
    • Structure of the armadillo repeat domain of plakophilin 1
    • Choi HJ, Weis WI. 2005. Structure of the armadillo repeat domain of plakophilin 1. J. Mol. Biol. 346:367-376. http://dx.doi.org/10.1016/j.jmb .2004.11.048.
    • (2005) J. Mol. Biol , vol.346 , pp. 367-376
    • Choi, H.J.1    Weis, W.I.2
  • 79
    • 84876011845 scopus 로고    scopus 로고
    • A novel role for the RNA-binding protein FXR1P in myoblasts cell-cycle progression by modulating p21/ Cdkn1a/Cip1/Waf1 mRNA stability
    • Davidovic L, Durand N, Khalfallah O, Tabet R, Barbry P, Mari B, Sacconi S, Moine H, Bardoni B. 2013. A novel role for the RNA-binding protein FXR1P in myoblasts cell-cycle progression by modulating p21/ Cdkn1a/Cip1/Waf1 mRNA stability. PLoS Genet. 9:e1003367. http://dx .doi.org/10.1371/journal.pgen.1003367.
    • (2013) PLoS Genet , vol.9 , pp. e1003367
    • Davidovic, L.1    Durand, N.2    Khalfallah, O.3    Tabet, R.4    Barbry, P.5    Mari, B.6    Sacconi, S.7    Moine, H.8    Bardoni, B.9
  • 80
    • 84858446579 scopus 로고    scopus 로고
    • MicroRNAs and their targets: recognition, regulation and an emerging reciprocal relationship
    • Pasquinelli AE. 2012. MicroRNAs and their targets: recognition, regulation and an emerging reciprocal relationship. Nat. Rev. Genet. 13:271- 282. http://dx.doi.org/10.1038/nrg3162.
    • (2012) Nat. Rev. Genet , vol.13 , pp. 271- 282
    • Pasquinelli, A.E.1
  • 82
    • 53849124668 scopus 로고    scopus 로고
    • Diverse molecular functions of Hu proteins
    • Hinman MN, Lou H. 2008. Diverse molecular functions of Hu proteins. Cell. Mol. Life Sci. 65:3168-3181. http://dx.doi.org/10.1007/s00018-008 -8252-6.
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 3168-3181
    • Hinman, M.N.1    Lou, H.2
  • 83
    • 0141889091 scopus 로고    scopus 로고
    • Regulation of eotaxin gene expression by TNF-alpha and IL-4 through mRNA stabilization: involvement of the RNA-binding protein HuR
    • Atasoy U, Curry SL, Lopez de Silanes I, Shyu AB, Casolaro V, Gorospe M, Stellato C. 2003. Regulation of eotaxin gene expression by TNF-alpha and IL-4 through mRNA stabilization: involvement of the RNA-binding protein HuR. J. Immunol. 171:4369-4378. http://dx.doi.org/10.4049 /jimmunol.171.8.4369.
    • (2003) J. Immunol , vol.171 , pp. 4369-4378
    • Atasoy, U.1    Curry, S.L.2    Lopez de Silanes, I.3    Shyu, A.B.4    Casolaro, V.5    Gorospe, M.6    Stellato, C.7
  • 84
    • 0035099573 scopus 로고    scopus 로고
    • HuR and mRNA stability
    • Brennan CM, Steitz JA. 2001. HuR and mRNA stability. Cell. Mol. Life Sci. 58:266-277. http://dx.doi.org/10.1007/PL00000854.
    • (2001) Cell. Mol. Life Sci , vol.58 , pp. 266-277
    • Brennan, C.M.1    Steitz, J.A.2
  • 85
    • 0032513043 scopus 로고    scopus 로고
    • Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR
    • Levy NS, Chung S, Furneaux H, Levy AP. 1998. Hypoxic stabilization of vascular endothelial growth factor mRNA by the RNA-binding protein HuR. J. Biol. Chem. 273:6417-6423. http://dx.doi.org/10.1074/jbc.273.11 .6417.
    • (1998) J. Biol. Chem , vol.273 , pp. 6417-6423
    • Levy, N.S.1    Chung, S.2    Furneaux, H.3    Levy, A.P.4
  • 88
    • 79952759375 scopus 로고    scopus 로고
    • Posttranscriptional regulation of cancer traits by HuR
    • Abdelmohsen K, Gorospe M. 2010. Posttranscriptional regulation of cancer traits by HuR. Wiley Interdiscip. Rev. RNA 1:214-229. http://dx .doi.org/10.1002/wrna.4.
    • (2010) Wiley Interdiscip. Rev. RNA , vol.1 , pp. 214-229
    • Abdelmohsen, K.1    Gorospe, M.2
  • 89
    • 0033566226 scopus 로고    scopus 로고
    • Alternative splicing in the murine and human FXR1 genes
    • Kirkpatrick LL, McIlwain KA, Nelson DL. 1999. Alternative splicing in the murine and human FXR1 genes. Genomics 59:193-202. http://dx.doi .org/10.1006/geno.1999.5868.
    • (1999) Genomics , vol.59 , pp. 193-202
    • Kirkpatrick, L.L.1    McIlwain, K.A.2    Nelson, D.L.3
  • 90
    • 2942591953 scopus 로고    scopus 로고
    • Muscle specific fragile X related protein 1 isoforms are sequestered in the nucleus of undifferentiated myoblast
    • Dube M, Huot ME, Khandjian EW. 2000. Muscle specific fragile X related protein 1 isoforms are sequestered in the nucleus of undifferentiated myoblast. BMC Genet. 1:4. http://dx.doi.org/10.1186/1471-2156-1-4.
    • (2000) BMC Genet. , vol.1 , pp. 4
    • Dube, M.1    Huot, M.E.2    Khandjian, E.W.3


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