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Volumn 1830, Issue 4, 2013, Pages 2938-2945

CK2 phosphorylation of human Sec63 regulates its interaction with Sec62

Author keywords

Phosphorylation; Protein kinase; Protein translocation; Protein protein interaction

Indexed keywords

CASEIN KINASE II; FUNGAL PROTEIN; PHOSPHOPROTEIN; PROTEIN SEC62; PROTEIN SEC63; SERINE; TRANSLOCON; UNCLASSIFIED DRUG;

EID: 84873710465     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2012.12.020     Document Type: Article
Times cited : (20)

References (44)
  • 2
    • 0025970051 scopus 로고
    • Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex
    • R.J. Deshaies, S.L. Sanders, D.A. Feldheim, and R. Schekman Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex Nature 349 1991 806 808
    • (1991) Nature , vol.349 , pp. 806-808
    • Deshaies, R.J.1    Sanders, S.L.2    Feldheim, D.A.3    Schekman, R.4
  • 3
    • 84863934536 scopus 로고    scopus 로고
    • Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation
    • A.K. Lakkaraju, R. Thankappan, C. Mary, J.L. Garrison, J. Taunton, and K. Strub Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation Mol. Biol. Cell 23 2012 2712 2722
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2712-2722
    • Lakkaraju, A.K.1    Thankappan, R.2    Mary, C.3    Garrison, J.L.4    Taunton, J.5    Strub, K.6
  • 5
    • 0032871620 scopus 로고    scopus 로고
    • Molecular characterization of a novel mammalian DnaJ-like Sec63p homolog
    • M.H. Skowronek, M. Rotter, and I.G. Haas Molecular characterization of a novel mammalian DnaJ-like Sec63p homolog Biol. Chem. 380 1999 1133 1138
    • (1999) Biol. Chem. , vol.380 , pp. 1133-1138
    • Skowronek, M.H.1    Rotter, M.2    Haas, I.G.3
  • 6
    • 0035670403 scopus 로고    scopus 로고
    • Localization of individual subunits of protein kinase CK2 to the endoplasmic reticulum and to the Golgi apparatus
    • M. Faust, M. Jung, J. Günther, R. Zimmermann, and M. Montenarh Localization of individual subunits of protein kinase CK2 to the endoplasmic reticulum and to the Golgi apparatus Mol. Cell. Biochem. 227 2001 73 80
    • (2001) Mol. Cell. Biochem. , vol.227 , pp. 73-80
    • Faust, M.1    Jung, M.2    Günther, J.3    Zimmermann, R.4    Montenarh, M.5
  • 8
    • 0037334895 scopus 로고    scopus 로고
    • One-thousand-and-one substrates of protein kinase CK2?
    • F. Meggio, and L.A. Pinna One-thousand-and-one substrates of protein kinase CK2? FASEB J. 17 2003 349 368
    • (2003) FASEB J. , vol.17 , pp. 349-368
    • Meggio, F.1    Pinna, L.A.2
  • 11
    • 1642524204 scopus 로고    scopus 로고
    • The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity
    • B. Kroczynska, C.M. Evangelista, S.S. Samant, E.C. Elguindi, and S.Y. Blond The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity J. Biol. Chem. 279 2004 11432 11443
    • (2004) J. Biol. Chem. , vol.279 , pp. 11432-11443
    • Kroczynska, B.1    Evangelista, C.M.2    Samant, S.S.3    Elguindi, E.C.4    Blond, S.Y.5
  • 12
    • 0033559231 scopus 로고    scopus 로고
    • Phosphorylation of components of the ER translocation site
    • O.J. Gruss, P. Feick, R. Frank, and B. Dobberstein Phosphorylation of components of the ER translocation site Eur. J. Biochem. 260 1999 785 793
    • (1999) Eur. J. Biochem. , vol.260 , pp. 785-793
    • Gruss, O.J.1    Feick, P.2    Frank, R.3    Dobberstein, B.4
  • 13
    • 14944361914 scopus 로고    scopus 로고
    • Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the endoplasmic reticulum protein translocation apparatus
    • X. Wang, and N. Johnsson Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the endoplasmic reticulum protein translocation apparatus J. Cell Sci. 118 2005 723 732
    • (2005) J. Cell Sci. , vol.118 , pp. 723-732
    • Wang, X.1    Johnsson, N.2
  • 14
    • 79951576536 scopus 로고    scopus 로고
    • An interaction between human Sec63 and nucleoredoxin may provide the missing link between the SEC63 gene and polycystic liver disease
    • L. Müller, Y. Funato, H. Miki, and R. Zimmermann An interaction between human Sec63 and nucleoredoxin may provide the missing link between the SEC63 gene and polycystic liver disease FEBS Lett. 585 2011 596 600
    • (2011) FEBS Lett. , vol.585 , pp. 596-600
    • Müller, L.1    Funato, Y.2    Miki, H.3    Zimmermann, R.4
  • 17
    • 0029146173 scopus 로고
    • Isolation and characterization of a monoclonal anti-protein kinase CK2 β-subunit antibody of the IgG class for the direct detection of CK2 β-subunit in tissue cultures of various mammalian species and human tumors
    • W. Nastainczyk, I. Schmidt-Spaniol, B. Boldyreff, and O.-G. Issinger Isolation and characterization of a monoclonal anti-protein kinase CK2 β-subunit antibody of the IgG class for the direct detection of CK2 β-subunit in tissue cultures of various mammalian species and human tumors Hybridoma 14 1995 335 339
    • (1995) Hybridoma , vol.14 , pp. 335-339
    • Nastainczyk, W.1    Schmidt-Spaniol, I.2    Boldyreff, B.3    Issinger, O.-G.4
  • 19
    • 69149090973 scopus 로고    scopus 로고
    • Common design principles in the spliceosomal RNA helicase Brr2 and in the Hel308 DNA helicase
    • V. Pena, S.M. Jovin, P. Fabrizio, J. Orlowski, J.M. Bujnicki, R. Luhrmann, and M.C. Wahl Common design principles in the spliceosomal RNA helicase Brr2 and in the Hel308 DNA helicase Mol. Cell 35 2009 454 466
    • (2009) Mol. Cell , vol.35 , pp. 454-466
    • Pena, V.1    Jovin, S.M.2    Fabrizio, P.3    Orlowski, J.4    Bujnicki, J.M.5    Luhrmann, R.6    Wahl, M.C.7
  • 21
    • 78649335829 scopus 로고    scopus 로고
    • Cellular regulators of protein kinase CK2
    • M. Montenarh Cellular regulators of protein kinase CK2 Cell Tissue Res. 342 2010 139 146
    • (2010) Cell Tissue Res. , vol.342 , pp. 139-146
    • Montenarh, M.1
  • 23
    • 0033738377 scopus 로고    scopus 로고
    • Sec62p, a component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the Sec-complex
    • S. Wittke, M. Dunnwald, and N. Johnsson Sec62p, a component of the endoplasmic reticulum protein translocation machinery, contains multiple binding sites for the Sec-complex Mol. Biol. Cell 11 2000 3859 3871
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3859-3871
    • Wittke, S.1    Dunnwald, M.2    Johnsson, N.3
  • 24
    • 70349186117 scopus 로고    scopus 로고
    • From birth to death: The role of protein kinase CK2 in the regulation of cell proliferation and survival
    • N.A. St-Denis, and D.W. Litchfield From birth to death: the role of protein kinase CK2 in the regulation of cell proliferation and survival Cell. Mol. Life Sci. 66 2009 1817 1829
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1817-1829
    • St-Denis, N.A.1    Litchfield, D.W.2
  • 25
    • 0033837291 scopus 로고    scopus 로고
    • Subcellular localization of protein kinase CK2: A key to its function?
    • M. Faust, and M. Montenarh Subcellular localization of protein kinase CK2: a key to its function? Cell Tissue Res. 301 2000 329 340
    • (2000) Cell Tissue Res. , vol.301 , pp. 329-340
    • Faust, M.1    Montenarh, M.2
  • 26
    • 0027057336 scopus 로고
    • Casein kinase II phosphorylation of signal sequence receptor α and the associated membrane chaperone calnexin
    • W.-J. Ou, D.Y. Thomas, A.W. Bell, and J.J.M. Bergeron Casein kinase II phosphorylation of signal sequence receptor α and the associated membrane chaperone calnexin J. Biol. Chem. 267 1992 23789 23796
    • (1992) J. Biol. Chem. , vol.267 , pp. 23789-23796
    • Ou, W.-J.1    Thomas, D.Y.2    Bell, A.W.3    Bergeron, J.J.M.4
  • 27
    • 0023645087 scopus 로고
    • Substrat specificity determinants for casein kinase II as deduced from studies with synthetic peptides
    • E.A. Kuenzel, J.A. Mulligan, J. Sommercorn, and E.G. Krebs Substrat specificity determinants for casein kinase II as deduced from studies with synthetic peptides J. Biol. Chem. 262 1987 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
  • 28
  • 29
    • 42049118391 scopus 로고    scopus 로고
    • Protein kinase CK2 interacts with the splicing factor hPrp3p
    • S. Lehnert, C. Götz, and M. Montenarh Protein kinase CK2 interacts with the splicing factor hPrp3p Oncogene 27 2008 2390 2400
    • (2008) Oncogene , vol.27 , pp. 2390-2400
    • Lehnert, S.1    Götz, C.2    Montenarh, M.3
  • 30
    • 33845386375 scopus 로고    scopus 로고
    • CD5-CK2 binding/activation-deficient mice are resistant to experimental autoimmune encephalomyelitis: Protection is associated with diminished populations of IL-17-expressing T cells in the central nervous system
    • R.C. Axtell, L. Xu, S.R. Barnum, and C. Raman CD5-CK2 binding/activation-deficient mice are resistant to experimental autoimmune encephalomyelitis: protection is associated with diminished populations of IL-17-expressing T cells in the central nervous system J. Immunol. 177 2006 8542 8549
    • (2006) J. Immunol. , vol.177 , pp. 8542-8549
    • Axtell, R.C.1    Xu, L.2    Barnum, S.R.3    Raman, C.4
  • 31
    • 0035054435 scopus 로고    scopus 로고
    • Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C
    • M. Ritter, C. Buechler, M. Kapinsky, and G. Schmitz Interaction of CD163 with the regulatory subunit of casein kinase II (CKII) and dependence of CD163 signaling on CKII and protein kinase C Eur. J. Immunol. 31 2001 999 1009
    • (2001) Eur. J. Immunol. , vol.31 , pp. 999-1009
    • Ritter, M.1    Buechler, C.2    Kapinsky, M.3    Schmitz, G.4
  • 32
    • 4744338740 scopus 로고    scopus 로고
    • The pleckstrin homology domain of CK2 interacting protein-1 is required for interactions and recruitment of protein kinase CK2 to the plasma membrane
    • M.E.K. Olsten, D.A. Canton, C.J. Zhang, P.A. Walton, and D.W. Litchfield The pleckstrin homology domain of CK2 interacting protein-1 is required for interactions and recruitment of protein kinase CK2 to the plasma membrane J. Biol. Chem. 279 2004 42114 42127
    • (2004) J. Biol. Chem. , vol.279 , pp. 42114-42127
    • Olsten, M.E.K.1    Canton, D.A.2    Zhang, C.J.3    Walton, P.A.4    Litchfield, D.W.5
  • 33
    • 0034041537 scopus 로고    scopus 로고
    • Nuclear targeting signal recognition: A key control point in nuclear transport?
    • D.A. Jans, C.Y. Xiao, and M.H. Lam Nuclear targeting signal recognition: a key control point in nuclear transport? Bioessays 22 2000 532 544
    • (2000) Bioessays , vol.22 , pp. 532-544
    • Jans, D.A.1    Xiao, C.Y.2    Lam, M.H.3
  • 34
    • 2942556504 scopus 로고    scopus 로고
    • Mutation of a CK2 phosphorylation site in cdc25C impairs importin α/β binding and results in cytoplasmic retention
    • S.L. Schwindling, A. Noll, M. Montenarh, and C. Götz Mutation of a CK2 phosphorylation site in cdc25C impairs importin α/β binding and results in cytoplasmic retention Oncogene 23 2004 4155 4165
    • (2004) Oncogene , vol.23 , pp. 4155-4165
    • Schwindling, S.L.1    Noll, A.2    Montenarh, M.3    Götz, C.4
  • 35
    • 0030973394 scopus 로고    scopus 로고
    • Casein kinase II-mediated phosphorylation of the C terminus of spl decreases its DNA binding activity
    • S.A. Armstrong, D.A. Barry, R.W. Leggett, and C.R. Mueller Casein kinase II-mediated phosphorylation of the C terminus of spl decreases its DNA binding activity J. Biol. Chem. 272 1997 13489 13495
    • (1997) J. Biol. Chem. , vol.272 , pp. 13489-13495
    • Armstrong, S.A.1    Barry, D.A.2    Leggett, R.W.3    Mueller, C.R.4
  • 36
    • 0033281074 scopus 로고    scopus 로고
    • The translocon: A dynamic gateway at the ER membrane
    • A.E. Johnson, and M.A. van Waes The translocon: a dynamic gateway at the ER membrane Annu. Rev. Cell Dev. Biol. 15 1999 799 842
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 799-842
    • Johnson, A.E.1    Van Waes, M.A.2
  • 37
    • 0030051440 scopus 로고    scopus 로고
    • ER membrane protein complex required for nuclear fusion
    • D.T. Ng, and P. Walter ER membrane protein complex required for nuclear fusion J. Cell Biol. 132 1996 499 509
    • (1996) J. Cell Biol. , vol.132 , pp. 499-509
    • Ng, D.T.1    Walter, P.2
  • 38
    • 0035862963 scopus 로고    scopus 로고
    • Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo
    • B.P. Young, R.A. Craven, P.J. Reid, M. Willer, and C.J. Stirling Sec63p and Kar2p are required for the translocation of SRP-dependent precursors into the yeast endoplasmic reticulum in vivo EMBO J. 20 2001 262 271
    • (2001) EMBO J. , vol.20 , pp. 262-271
    • Young, B.P.1    Craven, R.A.2    Reid, P.J.3    Willer, M.4    Stirling, C.J.5
  • 41
    • 84871856283 scopus 로고    scopus 로고
    • Functional interaction of protein kinase CK2 and activating transcription factor 4 (ATF4), a key player in the cellular stress response
    • E. Ampofo, T. Sokolowsky, C. Götz, and M. Montenarh Functional interaction of protein kinase CK2 and activating transcription factor 4 (ATF4), a key player in the cellular stress response Biochim. Biophys. Acta Mol. Cell Res. 1833 2013 439 451
    • (2013) Biochim. Biophys. Acta Mol. Cell Res. , vol.1833 , pp. 439-451
    • Ampofo, E.1    Sokolowsky, T.2    Götz, C.3    Montenarh, M.4
  • 42
    • 84862660266 scopus 로고    scopus 로고
    • CK2 regulates ATF4 and CHOP transcription within the cellular stress response signalling pathway
    • C.C. Schneider, E. Ampofo, and M. Montenarh CK2 regulates ATF4 and CHOP transcription within the cellular stress response signalling pathway Cell. Signal. 24 2012 1797 1802
    • (2012) Cell. Signal. , vol.24 , pp. 1797-1802
    • Schneider, C.C.1    Ampofo, E.2    Montenarh, M.3


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