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Volumn 14, Issue 4, 2012, Pages 297-310

The ezrin metastatic phenotype is associated with the initiation of protein Translation

Author keywords

[No Author keywords available]

Indexed keywords

EZRIN; INITIATION FACTOR 4E; MESSENGER RNA; POLYADENYLIC ACID BINDING PROTEIN; RECEPTOR FOR ACTIVATED C KINASE 1; RIBONUCLEOPROTEIN; RNA 18S; RNA 28S; RNA 5S; S6 KINASE; Y BOX BINDING PROTEIN 1;

EID: 84860635862     PISSN: 15228002     EISSN: 14765586     Source Type: Journal    
DOI: 10.1593/neo.111518     Document Type: Article
Times cited : (22)

References (56)
  • 2
    • 1442304609 scopus 로고    scopus 로고
    • Expression profiling identifies the cytoskeletal organizer ezrin and the developmental homeoprotein Six-1 as key metastatic regulators
    • Yu Y, Khan J, Khanna C, Helman L, Meltzer PS, and Merlino G (2004). Expression profiling identifies the cytoskeletal organizer ezrin and the developmental homeoprotein Six-1 as key metastatic regulators. Nat Med 10, 175-181.
    • (2004) Nat Med , vol.10 , pp. 175-181
    • Yu, Y.1    Khan, J.2    Khanna, C.3    Helman, L.4    Meltzer, P.S.5    Merlino, G.6
  • 4
    • 0032708603 scopus 로고    scopus 로고
    • Ezrin, a membrane-cytoskeletal linking protein, is involved in the process of invasion of endometrial cancer cells
    • Ohtani K, Sakamoto H, Rutherford T, Chen Z, Satoh K, and Naftolin F (1999). Ezrin, a membrane-cytoskeletal linking protein, is involved in the process of invasion of endometrial cancer cells. Cancer Lett 147, 31-38.
    • (1999) Cancer Lett , vol.147 , pp. 31-38
    • Ohtani, K.1    Sakamoto, H.2    Rutherford, T.3    Chen, Z.4    Satoh, K.5    Naftolin, F.6
  • 8
    • 24344464300 scopus 로고    scopus 로고
    • Prognostic impact of immunohistochemical expression of ezrin in highly malignant soft tissue sarcomas
    • Weng WH, Ahlen J, Astrom K, Lui WO, and Larsson C (2005). Prognostic impact of immunohistochemical expression of ezrin in highly malignant soft tissue sarcomas. Clin Cancer Res 11, 6198-6204.
    • (2005) Clin Cancer Res , vol.11 , pp. 6198-6204
    • Weng, W.H.1    Ahlen, J.2    Astrom, K.3    Lui, W.O.4    Larsson, C.5
  • 10
    • 0030608877 scopus 로고    scopus 로고
    • Identification of EBP50: A PDZcontaining phosphoprotein that associates with members of the ezrin-radixinmoesin family
    • Reczek D, Berryman M, and Bretscher A (1997). Identification of EBP50: a PDZcontaining phosphoprotein that associates with members of the ezrin-radixinmoesin family. J Cell Biol 139, 169-179.
    • (1997) J Cell Biol , vol.139 , pp. 169-179
    • Reczek, D.1    Berryman, M.2    Bretscher, A.3
  • 11
    • 0028229539 scopus 로고
    • ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actinbased cytoskeletons
    • Tsukita S, Oishi K, Sato N, Sagara J, and Kawai A (1994). ERM family members as molecular linkers between the cell surface glycoprotein CD44 and actinbased cytoskeletons. J Cell Biol 126, 391-401.
    • (1994) J Cell Biol , vol.126 , pp. 391-401
    • Tsukita, S.1    Oishi, K.2    Sato, N.3    Sagara, J.4    Kawai, A.5
  • 12
    • 0027183643 scopus 로고
    • Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells
    • Berryman M, Franck Z, and Bretscher A (1993). Ezrin is concentrated in the apical microvilli of a wide variety of epithelial cells whereas moesin is found primarily in endothelial cells. J Cell Sci 105(pt 4), 1025-1043.
    • (1993) J Cell Sci , vol.105 , Issue.4 PART , pp. 1025-1043
    • Berryman, M.1    Franck, Z.2    Bretscher, A.3
  • 13
    • 0034524664 scopus 로고    scopus 로고
    • ERM-Merlin and EBP50 protein families in plasma membrane organization and function
    • Bretscher A, Chambers D, Nguyen R, and Reczek D (2000). ERM-Merlin and EBP50 protein families in plasma membrane organization and function. Annu Rev Cell Dev Biol 16, 113-143.
    • (2000) Annu Rev Cell Dev Biol , vol.16 , pp. 113-143
    • Bretscher, A.1    Chambers, D.2    Nguyen, R.3    Reczek, D.4
  • 15
    • 0036346708 scopus 로고    scopus 로고
    • ERM proteins and merlin: Integrators at the cell cortex
    • Bretscher A, Edwards K, and Fehon RG (2002). ERM proteins and merlin: integrators at the cell cortex. Nat Rev Mol Cell Biol 3, 586-599.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 586-599
    • Bretscher, A.1    Edwards, K.2    Fehon, R.G.3
  • 17
    • 0033019133 scopus 로고    scopus 로고
    • Cytoskeletal rearrangement during migration and activation of T lymphocytes
    • Serrador JM, Nieto M, and Sanchez-Madrid F (1999). Cytoskeletal rearrangement during migration and activation of T lymphocytes. Trends Cell Biol 9, 228-233.
    • (1999) Trends Cell Biol , vol.9 , pp. 228-233
    • Serrador, J.M.1    Nieto, M.2    Sanchez-Madrid, F.3
  • 21
    • 0031471375 scopus 로고    scopus 로고
    • Ezrin: A protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures
    • Bretscher A, Reczek D, and Berryman M (1997). Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J Cell Sci 110(pt 24), 3011-3018.
    • (1997) J Cell Sci , vol.110 , Issue.24 PATT , pp. 3011-3018
    • Bretscher, A.1    Reczek, D.2    Berryman, M.3
  • 22
    • 1942453838 scopus 로고    scopus 로고
    • A novel function of the MA-3 domains in transformation and translation suppressor Pdcd4 is essential for its binding to eukaryotic translation initiation factor 4A
    • Yang HS, Cho MH, Zakowicz H, Hegamyer G, Sonenberg N, and Colburn NH (2004). A novel function of the MA-3 domains in transformation and translation suppressor Pdcd4 is essential for its binding to eukaryotic translation initiation factor 4A. Mol Cell Biol 24, 3894-3906.
    • (2004) Mol Cell Biol , vol.24 , pp. 3894-3906
    • Yang, H.S.1    Cho, M.H.2    Zakowicz, H.3    Hegamyer, G.4    Sonenberg, N.5    Colburn, N.H.6
  • 27
    • 0032541057 scopus 로고    scopus 로고
    • The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule
    • Reczek D and Bretscher A (1998). The carboxyl-terminal region of EBP50 binds to a site in the amino-terminal domain of ezrin that is masked in the dormant molecule. J Biol Chem 273, 18452-18458.
    • (1998) J Biol Chem , vol.273 , pp. 18452-18458
    • Reczek, D.1    Bretscher, A.2
  • 28
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm M, Shevchenko A, Houthaeve T, Breit S, Schweigerer L, Fotsis T, and Mann M (1996). Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 379, 466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7
  • 29
    • 0037273324 scopus 로고    scopus 로고
    • Translational control and metastatic progression: Enhanced activity of the mRNA cap-binding protein eIF-4E selectively enhances translation of metastasis-related mRNAs
    • Graff JR and Zimmer SG (2003). Translational control and metastatic progression: enhanced activity of the mRNA cap-binding protein eIF-4E selectively enhances translation of metastasis-related mRNAs. Clin Exp Metastasis 20, 265-273.
    • (2003) Clin Exp Metastasis , vol.20 , pp. 265-273
    • Graff, J.R.1    Zimmer, S.G.2
  • 31
    • 0034212658 scopus 로고    scopus 로고
    • The chicken c-Jun 5′ untranslated region directs translation by internal initiation
    • Sehgal A, Briggs J, Rinehart-Kim J, Basso J, and Bos TJ (2000). The chicken c-Jun 5′ untranslated region directs translation by internal initiation. Oncogene 19, 2836-2845.
    • (2000) Oncogene , vol.19 , pp. 2836-2845
    • Sehgal, A.1    Briggs, J.2    Rinehart-Kim, J.3    Basso, J.4    Bos, T.J.5
  • 32
    • 0141919444 scopus 로고    scopus 로고
    • Aberrant regulation of translation initiation in tumorigenesis
    • Stoneley M and Willis AE (2003). Aberrant regulation of translation initiation in tumorigenesis. Curr Mol Med 3, 597-603.
    • (2003) Curr Mol Med , vol.3 , pp. 597-603
    • Stoneley, M.1    Willis, A.E.2
  • 33
    • 62849093964 scopus 로고    scopus 로고
    • Direct link between RACK1 function and localization at the ribosome in vivo
    • Coyle SM, Gilbert WV, and Doudna JA (2009). Direct link between RACK1 function and localization at the ribosome in vivo. Mol Cell Biol 29, 1626-1634.
    • (2009) Mol Cell Biol , vol.29 , pp. 1626-1634
    • Coyle, S.M.1    Gilbert, W.V.2    Doudna, J.A.3
  • 34
    • 12144253782 scopus 로고    scopus 로고
    • Regulation of eukaryotic translation by the RACK1 protein: A platform for signalling molecules on the ribosome
    • Nilsson J, Sengupta J, Frank J, and Nissen P (2004). Regulation of eukaryotic translation by the RACK1 protein: a platform for signalling molecules on the ribosome. EMBO Rep 5, 1137-1141.
    • (2004) EMBO Rep , vol.5 , pp. 1137-1141
    • Nilsson, J.1    Sengupta, J.2    Frank, J.3    Nissen, P.4
  • 36
    • 77956211588 scopus 로고    scopus 로고
    • Prognostic implications of ezrin expression in human hepatocellular carcinoma
    • Kang YK, Hong SW, Lee H, and Kim WH (2010). Prognostic implications of ezrin expression in human hepatocellular carcinoma. Mol Carcinog 49, 798-804.
    • (2010) Mol Carcinog , vol.49 , pp. 798-804
    • Kang, Y.K.1    Hong, S.W.2    Lee, H.3    Kim, W.H.4
  • 37
    • 70349673599 scopus 로고    scopus 로고
    • Ezrin overexpression in gastrointestinal stromal tumors: An independent adverse prognosticator associated with the non-gastric location
    • Wei YC, Li CF, Yu SC, Chou FF, Fang FM, Eng HL, Uen YH, Tian YF, Wu JM, Li SH, et al. (2009). Ezrin overexpression in gastrointestinal stromal tumors: an independent adverse prognosticator associated with the non-gastric location. Mod Pathol 22, 1351-1360.
    • (2009) Mod Pathol , vol.22 , pp. 1351-1360
    • Wei, Y.C.1    Li, C.F.2    Yu, S.C.3    Chou, F.F.4    Fang, F.M.5    Eng, H.L.6    Uen, Y.H.7    Tian, Y.F.8    Wu, J.M.9    Li, S.H.10
  • 39
    • 33750375071 scopus 로고    scopus 로고
    • Differential tissue and subcellular expression of ERM proteins in normal and malignant tissues: Cytoplasmic ezrin expression has prognostic significance for head and neck squamous cell carcinoma
    • Madan R, Brandwein-Gensler M, Schlecht NF, Elias K, Gorbovitsky E, Belbin TJ, Mahmood R, Breining D, Qian H, Childs G, et al. (2006). Differential tissue and subcellular expression of ERM proteins in normal and malignant tissues: cytoplasmic ezrin expression has prognostic significance for head and neck squamous cell carcinoma. Head Neck 28, 1018-1027.
    • (2006) Head Neck , vol.28 , pp. 1018-1027
    • Madan, R.1    Brandwein-Gensler, M.2    Schlecht, N.F.3    Elias, K.4    Gorbovitsky, E.5    Belbin, T.J.6    Mahmood, R.7    Breining, D.8    Qian, H.9    Childs, G.10
  • 42
    • 0032537124 scopus 로고    scopus 로고
    • Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions
    • Chicurel ME, Singer RH, Meyer CJ, and Ingber DE (1998). Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions. Nature 392, 730-733.
    • (1998) Nature , vol.392 , pp. 730-733
    • Chicurel, M.E.1    Singer, R.H.2    Meyer, C.J.3    Ingber, D.E.4
  • 43
    • 72949113853 scopus 로고    scopus 로고
    • Emerging role for the cytoskeleton as an organizer and regulator of translation
    • Kim S and Coulombe PA (2010). Emerging role for the cytoskeleton as an organizer and regulator of translation. Nat Rev Mol Cell Biol 11, 75-81.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 75-81
    • Kim, S.1    Coulombe, P.A.2
  • 45
    • 46549088342 scopus 로고    scopus 로고
    • A Cytoskeletal Platform For Local Translation In Axons
    • Van Horck FP and Holt CE (2008). A cytoskeletal platform for local translation in axons. Sci Signal 1, pe11.
    • (2008) Sci Signal , vol.1 , pp. 11
    • van Horck, F.P.1    Holt, C.E.2
  • 46
    • 33747358541 scopus 로고    scopus 로고
    • Compartmentalisation and localisation of the translation initiation factor (eIF) 4F complex in normally growing fibroblasts
    • Willett M, Flint SA, Morley SJ, and Pain VM (2006). Compartmentalisation and localisation of the translation initiation factor (eIF) 4F complex in normally growing fibroblasts. Exp Cell Res 312, 2942-2953.
    • (2006) Exp Cell Res , vol.312 , pp. 2942-2953
    • Willett, M.1    Flint, S.A.2    Morley, S.J.3    Pain, V.M.4
  • 47
    • 2342489456 scopus 로고    scopus 로고
    • eIF-4E expression and its role in malignancies and metastases
    • De Benedetti A and Graff JR (2004). eIF-4E expression and its role in malignancies and metastases. Oncogene 23, 3189-3199.
    • (2004) Oncogene , vol.23 , pp. 3189
    • de Benedetti, A.1    Graff, J.R.2
  • 48
    • 77952393003 scopus 로고    scopus 로고
    • Mechanisms governing the control of mRNA translation
    • Livingstone M, Atas E, Meller A, and Sonenberg N (2010). Mechanisms governing the control of mRNA translation. Phys Biol 7, 021001.
    • (2010) Phys Biol , vol.7 , pp. 021001
    • Livingstone, M.1    Atas, E.2    Meller, A.3    Sonenberg, N.4
  • 49
    • 77958027783 scopus 로고    scopus 로고
    • Targeting eukaryotic translation initiation factor 4E (eIF4E) in cancer
    • Hsieh AC and Ruggero D (2010). Targeting eukaryotic translation initiation factor 4E (eIF4E) in cancer. Clin Cancer Res 16, 4914-4920.
    • (2010) Clin Cancer Res , vol.16 , pp. 4914-4920
    • Hsieh, A.C.1    Ruggero, D.2
  • 51
    • 17644391054 scopus 로고    scopus 로고
    • Interaction of paxillin with poly(A)-binding protein 1 and its role in focal adhesion turnover and cell migration
    • Woods AJ, Kantidakis T, Sabe H, Critchley DR, and Norman JC (2005). Interaction of paxillin with poly(A)-binding protein 1 and its role in focal adhesion turnover and cell migration. Mol Cell Biol 25, 3763-3773.
    • (2005) Mol Cell Biol , vol.25 , pp. 3763-3773
    • Woods, A.J.1    Kantidakis, T.2    Sabe, H.3    Critchley, D.R.4    Norman, J.C.5
  • 53
    • 2442513975 scopus 로고    scopus 로고
    • Nuclear ERM (ezrin, radixin, moesin) proteins: Regulation by cell density and nuclear import
    • Batchelor CL, Woodward AM, and Crouch DH (2004). Nuclear ERM (ezrin, radixin, moesin) proteins: regulation by cell density and nuclear import. Exp Cell Res 296, 208-222.
    • (2004) Exp Cell Res , vol.296 , pp. 208-222
    • Batchelor, C.L.1    Woodward, A.M.2    Crouch, D.H.3
  • 54
    • 79951510534 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1
    • Rabl J, Leibundgut M, Ataide SF, Haag A, and Ban N (2011). Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. Science 331, 730-736.
    • (2011) Science , vol.331 , pp. 730-736
    • Rabl, J.1    Leibundgut, M.2    Ataide, S.F.3    Haag, A.4    Ban, N.5
  • 55
    • 4744350970 scopus 로고    scopus 로고
    • Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM
    • Sengupta J, Nilsson J, Gursky R, Spahn CM, Nissen P, and Frank J (2004). Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM. Nat Struct Mol Biol 11, 957-962.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 957-962
    • Sengupta, J.1    Nilsson, J.2    Gursky, R.3    Spahn, C.M.4    Nissen, P.5    Frank, J.6


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