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Volumn 31, Issue 17, 2011, Pages 3515-3530

Retraction: "Nuclear extracellular signal-regulated kinase 1 and 2 translocation is mediated by casein kinase 2 and accelerated by autophosphorylation" [Molecular and Cellular Biology, 31, 17, (2011) (3515-3530)] doi: 10.1128/MCB.05424-11;Nuclear extracellular signal-regulated kinase 1 and 2 translocation is mediated by casein kinase 2 and accelerated by autophosphorylation

Author keywords

[No Author keywords available]

Indexed keywords

CASEIN KINASE II; CYTOPLASM PROTEIN; KARYOPHERIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3;

EID: 80052332583     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.00106-18     Document Type: Erratum
Times cited : (69)

References (53)
  • 1
    • 77950413847 scopus 로고    scopus 로고
    • Extracellular-regulated kinase-mitogen-activated protein kinase cascade: unsolved issues
    • Bodart, J. F. 2010. Extracellular-regulated kinase-mitogen-activated protein kinase cascade: unsolved issues. J. Cell. Biochem. 109:850-857.
    • (2010) J. Cell. Biochem. , vol.109 , pp. 850-857
    • Bodart, J.F.1
  • 2
    • 0033081066 scopus 로고    scopus 로고
    • Nuclear translocation of p42/p44 mitogen-activated protein kinase is required for growth factor-induced gene expression and cell cycle entry
    • Brunet, A., et al. 1999. Nuclear translocation of p42/p44 mitogen-activated protein kinase is required for growth factor-induced gene expression and cell cycle entry. EMBO J. 18:664-674.
    • (1999) EMBO J , vol.18 , pp. 664-674
    • Brunet, A.1
  • 3
    • 33846590071 scopus 로고    scopus 로고
    • Interaction with MEK causes nuclear export and downregulation of peroxisome proliferator-activated receptor gamma
    • Burgermeister, E., et al. 2007. Interaction with MEK causes nuclear export and downregulation of peroxisome proliferator-activated receptor gamma. Mol. Cell. Biol. 27:803-817.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 803-817
    • Burgermeister, E.1
  • 4
    • 77951724799 scopus 로고    scopus 로고
    • The Ras-ERK pathway: understanding site-specific signaling provides hope of new anti-tumor therapies
    • Calvo, F., L. Agudo-Ibanez, and P. Crespo. 2010. The Ras-ERK pathway: understanding site-specific signaling provides hope of new anti-tumor therapies. Bioessays 32:412-421.
    • (2010) Bioessays , vol.32 , pp. 412-421
    • Calvo, F.1    Agudo-Ibanez, L.2    Crespo, P.3
  • 5
    • 50549083633 scopus 로고    scopus 로고
    • Essential role of ERK dimers in the activation of cytoplasmic but not nuclear substrates by ERK-scaffold complexes
    • Casar, B., A. Pinto, and P. Crespo. 2008. Essential role of ERK dimers in the activation of cytoplasmic but not nuclear substrates by ERK-scaffold complexes. Mol. Cell 31:708-721.
    • (2008) Mol. Cell , vol.31 , pp. 708-721
    • Casar, B.1    Pinto, A.2    Crespo, P.3
  • 6
    • 52049108218 scopus 로고    scopus 로고
    • Identification and characterization of a general nuclear translocation signal in signaling proteins
    • Chuderland, D., A. Konson, and R. Seger. 2008. Identification and characterization of a general nuclear translocation signal in signaling proteins. Mol. Cell 31:850-861.
    • (2008) Mol. Cell , vol.31 , pp. 850-861
    • Chuderland, D.1    Konson, A.2    Seger, R.3
  • 7
    • 21644449056 scopus 로고    scopus 로고
    • Protein-protein interactions in the regulation of the extracellular signal-regulated kinase
    • Chuderland, D., and R. Seger. 2005. Protein-protein interactions in the regulation of the extracellular signal-regulated kinase. Mol. Biotechnol. 29: 57-74.
    • (2005) Mol. Biotechnol. , vol.29 , pp. 57-74
    • Chuderland, D.1    Seger, R.2
  • 8
    • 38349116517 scopus 로고    scopus 로고
    • Too much of a good thing: the role of protein kinase CK2 in tumorigenesis and prospects for therapeutic inhibition of CK2
    • Duncan, J. S., and D. W. Litchfield. 2008. Too much of a good thing: the role of protein kinase CK2 in tumorigenesis and prospects for therapeutic inhibition of CK2. Biochim. Biophys. Acta 1784:33-47.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 33-47
    • Duncan, J.S.1    Litchfield, D.W.2
  • 10
    • 18044405015 scopus 로고    scopus 로고
    • PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase
    • Formstecher, E., et al. 2001. PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase. Dev. Cell 1:239-250.
    • (2001) Dev. Cell , vol.1 , pp. 239-250
    • Formstecher, E.1
  • 11
    • 0030972494 scopus 로고    scopus 로고
    • Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase
    • Fukuda, M., Y. Gotoh, and E. Nishida. 1997. Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase. EMBO J. 16:1901-1908.
    • (1997) EMBO J , vol.16 , pp. 1901-1908
    • Fukuda, M.1    Gotoh, Y.2    Nishida, E.3
  • 12
    • 70449591270 scopus 로고    scopus 로고
    • A new paradigm for MAPK: structural interactions of hERK1 with mitochondria in HeLa cells
    • Galli, S., et al. 2009. A new paradigm for MAPK: structural interactions of hERK1 with mitochondria in HeLa cells. PLoS One 4:e7541.
    • (2009) PLoS One , vol.4
    • Galli, S.1
  • 13
    • 0040182590 scopus 로고    scopus 로고
    • Nuclear protein import
    • Gorlich, D. 1997. Nuclear protein import. Curr. Opin. Cell Biol. 9:412-419.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 412-419
    • Gorlich, D.1
  • 14
    • 77957803826 scopus 로고    scopus 로고
    • CK2 inhibition induces apoptosis via the ER stress response
    • Hessenauer, A., C. C. Schneider, C. Gotz, and M. Montenarh. 2011. CK2 inhibition induces apoptosis via the ER stress response. Cell. Signal. 23:145-151.
    • (2011) Cell. Signal. , vol.23 , pp. 145-151
    • Hessenauer, A.1    Schneider, C.C.2    Gotz, C.3    Montenarh, M.4
  • 15
    • 76749088358 scopus 로고    scopus 로고
    • Pathological roles of MAPK signaling pathways in human diseases
    • Kim, E. K., and E. J. Choi. 2010. Pathological roles of MAPK signaling pathways in human diseases. Biochim. Biophys. Acta 1802:396-405.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 396-405
    • Kim, E.K.1    Choi, E.J.2
  • 16
    • 27644575157 scopus 로고    scopus 로고
    • Coordinating ERK/MAPK signalling through scaffolds and inhibitors
    • Kolch, W. 2005. Coordinating ERK/MAPK signalling through scaffolds and inhibitors. Nat. Rev. Mol. Cell Biol. 6:827-837.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 827-837
    • Kolch, W.1
  • 17
    • 77955942384 scopus 로고    scopus 로고
    • Functional proteomics to dissect tyrosine kinase signalling pathways in cancer
    • Kolch, W., and A. Pitt. 2010. Functional proteomics to dissect tyrosine kinase signalling pathways in cancer. Nat. Rev. Cancer 10:618-629.
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 618-629
    • Kolch, W.1    Pitt, A.2
  • 18
    • 0023645087 scopus 로고
    • Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides
    • Kuenzel, E. A., J. A. Mulligan, J. Sommercorn, and E. G. Krebs. 1987. Substrate specificity determinants for casein kinase II as deduced from studies with synthetic peptides. J. Biol. Chem. 262:9136-9140.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9136-9140
    • Kuenzel, E.A.1    Mulligan, J.A.2    Sommercorn, J.3    Krebs, E.G.4
  • 20
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: structure, regulation and role in cellular decisions of life and death
    • Litchfield, D. W. 2003. Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem. J. 369:1-15.
    • (2003) Biochem. J. , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 21
    • 0035036212 scopus 로고    scopus 로고
    • Nuclear import of activated D-ERK by DIM-7, an importin family member encoded by the gene moleskin
    • Lorenzen, J. A., et al. 2001. Nuclear import of activated D-ERK by DIM-7, an importin family member encoded by the gene moleskin. Development 128:1403-1414.
    • (2001) Development , vol.128 , pp. 1403-1414
    • Lorenzen, J.A.1
  • 22
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • Meggio, F., and L. A. Pinna. 2003. One-thousand-and-one substrates of protein kinase CK2? FASEB J. 17:349-368.
    • (2003) FASEB J , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 24
    • 34250166523 scopus 로고    scopus 로고
    • Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases
    • Niefind, K., C. W. Yde, I. Ermakova, and O. G. Issinger. 2007. Evolved to be active: sulfate ions define substrate recognition sites of CK2alpha and emphasise its exceptional role within the CMGC family of eukaryotic protein kinases. J. Mol. Biol. 370:427-438.
    • (2007) J. Mol. Biol. , vol.370 , pp. 427-438
    • Niefind, K.1    Yde, C.W.2    Ermakova, I.3    Issinger, O.G.4
  • 25
    • 0030964105 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: signals, mechanisms and regulation
    • Nigg, E. A. 1997. Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 386:779-787.
    • (1997) Nature , vol.386 , pp. 779-787
    • Nigg, E.A.1
  • 26
    • 0032516522 scopus 로고    scopus 로고
    • Protein kinase CK2alpha′ is induced by serum as a delayed early gene and cooperates with Ha-ras in fibroblast transformation
    • Orlandini, M., et al. 1998. Protein kinase CK2alpha′ is induced by serum as a delayed early gene and cooperates with Ha-ras in fibroblast transformation. J. Biol. Chem. 273:21291-21297.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21291-21297
    • Orlandini, M.1
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and W. Minor. 1997. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 28
    • 84872864632 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: CK2: an ugly duckling in the kinome pond
    • Pinna, L. A., and J. E. Allende. 2009. Protein kinase CK2 in health and disease: CK2: an ugly duckling in the kinome pond. Cell. Mol. Life Sci. 66:1795-1799.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1795-1799
    • Pinna, L.A.1    Allende, J.E.2
  • 29
    • 79955518288 scopus 로고    scopus 로고
    • The MAPK cascades: signaling components, nuclear roles and mechanisms of nuclear translocation
    • in press
    • Plotnikov, A., E. Zehorai, S. Procaccia, and R. Seger. The MAPK cascades: signaling components, nuclear roles and mechanisms of nuclear translocation. Biochim. Biophys. Acta, in press.
    • Biochim. Biophys. Acta
    • Plotnikov, A.1    Zehorai, E.2    Procaccia, S.3    Seger, R.4
  • 31
    • 34248597065 scopus 로고    scopus 로고
    • Differential regulation and properties of MAPKs
    • Raman, M., W. Chen, and M. H. Cobb. 2007. Differential regulation and properties of MAPKs. Oncogene 26:3100-3112.
    • (2007) Oncogene , vol.26 , pp. 3100-3112
    • Raman, M.1    Chen, W.2    Cobb, M.H.3
  • 32
    • 0030855766 scopus 로고    scopus 로고
    • Mitogenactivated protein kinase/extracellular signal-regulated kinase 2 regulates cytoskeletal organization and chemotaxis via catalytic and microtubule-specific interactions
    • Reszka, A. A., J. C. Bulinski, E. G. Krebs, and E. H. Fischer. 1997. Mitogenactivated protein kinase/extracellular signal-regulated kinase 2 regulates cytoskeletal organization and chemotaxis via catalytic and microtubule-specific interactions. Mol. Biol. Cell 8:1219-1232.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1219-1232
    • Reszka, A.A.1    Bulinski, J.C.2    Krebs, E.G.3    Fischer, E.H.4
  • 33
    • 0037112514 scopus 로고    scopus 로고
    • Protein kinase CK2 promotes aberrant activation of nuclear factor-kappaB, transformed phenotype, and survival of breast cancer cells
    • Romieu-Mourez, R., E. Landesman-Bollag, D. C. Seldin, and G. E. Sonenshein. 2002. Protein kinase CK2 promotes aberrant activation of nuclear factor-kappaB, transformed phenotype, and survival of breast cancer cells. Cancer Res. 62:6770-6778.
    • (2002) Cancer Res , vol.62 , pp. 6770-6778
    • Romieu-Mourez, R.1    Landesman-Bollag, E.2    Seldin, D.C.3    Sonenshein, G.E.4
  • 34
    • 0032749494 scopus 로고    scopus 로고
    • Identification of a cytoplasmic-retention sequence in ERK2
    • Rubinfeld, H., T. Hanoch, and R. Seger. 1999. Identification of a cytoplasmic-retention sequence in ERK2. J. Biol. Chem. 274:30349-30352.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30349-30352
    • Rubinfeld, H.1    Hanoch, T.2    Seger, R.3
  • 35
    • 75349084777 scopus 로고    scopus 로고
    • Addiction to protein kinase CK2: a common denominator of diverse cancer cells?
    • Ruzzene, M., and L. A. Pinna. 2010. Addiction to protein kinase CK2: a common denominator of diverse cancer cells? Biochim. Biophys. Acta 1804: 499-504.
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 499-504
    • Ruzzene, M.1    Pinna, L.A.2
  • 36
    • 27944499451 scopus 로고    scopus 로고
    • An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets
    • Schwartz, D., and S. P. Gygi. 2005. An iterative statistical approach to the identification of protein phosphorylation motifs from large-scale data sets. Nat. Biotechnol. 23:1391-1398.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1391-1398
    • Schwartz, D.1    Gygi, S.P.2
  • 37
    • 68149132138 scopus 로고    scopus 로고
    • Specific phosphorylation and activation of ERK1c by MEK1b: a unique route in the ERK cascade
    • Shaul, Y. D., G. Gibor, A. Plotnikov, and R. Seger. 2009. Specific phosphorylation and activation of ERK1c by MEK1b: a unique route in the ERK cascade. Genes Dev. 23:1779-1790.
    • (2009) Genes Dev , vol.23 , pp. 1779-1790
    • Shaul, Y.D.1    Gibor, G.2    Plotnikov, A.3    Seger, R.4
  • 38
    • 33644878839 scopus 로고    scopus 로고
    • ERK1c regulates Golgi fragmentation during mitosis
    • Shaul, Y. D., and R. Seger. 2006. ERK1c regulates Golgi fragmentation during mitosis. J. Cell Biol. 172:885-897.
    • (2006) J. Cell Biol. , vol.172 , pp. 885-897
    • Shaul, Y.D.1    Seger, R.2
  • 39
    • 34547204160 scopus 로고    scopus 로고
    • The MEK/ERK cascade: from signaling specificity to diverse functions
    • Shaul, Y. D., and R. Seger. 2007. The MEK/ERK cascade: from signaling specificity to diverse functions. Biochim. Biophys. Acta 1773:1213-1226.
    • (2007) Biochim. Biophys. Acta , vol.1773 , pp. 1213-1226
    • Shaul, Y.D.1    Seger, R.2
  • 40
    • 77957291965 scopus 로고    scopus 로고
    • Nuclear entry of activated MAPK is restricted in primary ovarian and mammary epithelial cells
    • Smith, E. R., et al. 2010. Nuclear entry of activated MAPK is restricted in primary ovarian and mammary epithelial cells. PLoS One 5:e9295.
    • (2010) PLoS One , vol.5
    • Smith, E.R.1
  • 41
    • 70349186117 scopus 로고    scopus 로고
    • Protein kinase CK2 in health and disease: from birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival
    • St-Denis, N. A., and D. W. Litchfield. 2009. Protein kinase CK2 in health and disease: from birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival. Cell. Mol. Life Sci. 66:1817-1829.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1817-1829
    • St-Denis, N.A.1    Litchfield, D.W.2
  • 42
    • 0026117693 scopus 로고
    • The streak seeding technique in protein crystallization
    • Stura, E. A., and I. A. Wilson. 1991. The streak seeding technique in protein crystallization. J. Cryst. Growth 110:270-282.
    • (1991) J. Cryst. Growth , vol.110 , pp. 270-282
    • Stura, E.A.1    Wilson, I.A.2
  • 43
    • 78049390388 scopus 로고    scopus 로고
    • Phosphorylation of the RNase III enzyme Drosha at serine300 or serine302 is required for its nuclear localization
    • Tang, X., Y. Zhang, L. Tucker, and B. Ramratnam. 2010. Phosphorylation of the RNase III enzyme Drosha at serine300 or serine302 is required for its nuclear localization. Nucleic Acids Res. 38:6610-6619.
    • (2010) Nucleic Acids Res , vol.38 , pp. 6610-6619
    • Tang, X.1    Zhang, Y.2    Tucker, L.3    Ramratnam, B.4
  • 44
    • 33947513279 scopus 로고    scopus 로고
    • Modulation of replicative senescence of diploid human cells by nuclear ERK signaling
    • Tresini, M., A. Lorenzini, C. Torres, and V. J. Cristofalo. 2007. Modulation of replicative senescence of diploid human cells by nuclear ERK signaling. J. Biol. Chem. 282:4136-4151.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4136-4151
    • Tresini, M.1    Lorenzini, A.2    Torres, C.3    Cristofalo, V.J.4
  • 45
    • 0035788131 scopus 로고    scopus 로고
    • Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps
    • Vagin, A. A., and M. N. Isupov. 2001. Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps. Acta Crystallogr. D Biol. Crystallogr. 57:1451- 1456.
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57
    • Vagin, A.A.1    Isupov, M.N.2
  • 46
    • 34948906397 scopus 로고    scopus 로고
    • Nuclear import of c-Jun is mediated by multiple transport receptors
    • Waldmann, I., S. Walde, and R. H. Kehlenbach. 2007. Nuclear import of c-Jun is mediated by multiple transport receptors. J. Biol. Chem. 282:27685- 27692.
    • (2007) J. Biol. Chem. , vol.282
    • Waldmann, I.1    Walde, S.2    Kehlenbach, R.H.3
  • 47
    • 0035816678 scopus 로고    scopus 로고
    • Involvement of the activation loop of ERK in the detachment from cytosolic anchoring
    • Wolf, I., et al. 2001. Involvement of the activation loop of ERK in the detachment from cytosolic anchoring. J. Biol. Chem. 276:24490-24497.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24490-24497
    • Wolf, I.1
  • 49
    • 53049104873 scopus 로고    scopus 로고
    • Preferential utilization of Imp7/8 in nuclear import of Smads
    • Yao, X., X. Chen, C. Cottonham, and L. Xu. 2008. Preferential utilization of Imp7/8 in nuclear import of Smads. J. Biol. Chem. 283:22867-22874.
    • (2008) J. Biol. Chem. , vol.283 , pp. 22867-22874
    • Yao, X.1    Chen, X.2    Cottonham, C.3    Xu, L.4
  • 50
    • 73249143291 scopus 로고    scopus 로고
    • The ERK signaling cascade-views from different subcellular compartments
    • Yao, Z., and R. Seger. 2009. The ERK signaling cascade-views from different subcellular compartments. Biofactors 35:407-416.
    • (2009) Biofactors , vol.35 , pp. 407-416
    • Yao, Z.1    Seger, R.2
  • 51
    • 35348957232 scopus 로고    scopus 로고
    • Mutations in ERK2 binding sites affect nuclear entry
    • Yazicioglu, M. N., et al. 2007. Mutations in ERK2 binding sites affect nuclear entry. J. Biol. Chem. 282:28759-28767.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28759-28767
    • Yazicioglu, M.N.1
  • 52
    • 30944447568 scopus 로고    scopus 로고
    • The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions
    • Yoon, S., and R. Seger. 2006. The extracellular signal-regulated kinase: multiple substrates regulate diverse cellular functions. Growth Factors 24: 21-44.
    • (2006) Growth Factors , vol.24 , pp. 21-44
    • Yoon, S.1    Seger, R.2
  • 53
    • 71849119627 scopus 로고    scopus 로고
    • The subcellular localization of MEK and ERK-a novel nuclear translocation signal (NTS) paves a way to the nucleus
    • Zehorai, E., Z. Yao, A. Plotnikov, and R. Seger. 2010. The subcellular localization of MEK and ERK-a novel nuclear translocation signal (NTS) paves a way to the nucleus. Mol. Cell. Endocrinol. 314:213-220.
    • (2010) Mol. Cell. Endocrinol. , vol.314 , pp. 213-220
    • Zehorai, E.1    Yao, Z.2    Plotnikov, A.3    Seger, R.4


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