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Volumn 582, Issue 18, 2008, Pages 2685-2688

Phosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic protein (MBP) in multiple sclerosis

Author keywords

Kinase; Mimicry; Myelin; Phosphorylation; U24

Indexed keywords

MYELIN BASIC PROTEIN; PROTEIN; PROTEIN U24;

EID: 47849114837     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.06.050     Document Type: Article
Times cited : (24)

References (31)
  • 1
    • 17644396349 scopus 로고    scopus 로고
    • Immunology of multiple sclerosis
    • Sospedra M., and Martin R. Immunology of multiple sclerosis. Annu. Rev. Immunol. 23 (2005) 683-747
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 683-747
    • Sospedra, M.1    Martin, R.2
  • 2
    • 34547236023 scopus 로고    scopus 로고
    • Environment-gene interaction in multiple sclerosis: human herpesvirus 6 and MHC2TA
    • Martinez A., et al. Environment-gene interaction in multiple sclerosis: human herpesvirus 6 and MHC2TA. Hum. Immunol. 68 (2007) 685-689
    • (2007) Hum. Immunol. , vol.68 , pp. 685-689
    • Martinez, A.1
  • 3
    • 0028926223 scopus 로고
    • Molecular mimicry in T cell-mediated autoimmunity: viral peptides activate human T cell clones specific for myelin basic protein
    • Wucherpfennig K.W., and Strominger J.L. Molecular mimicry in T cell-mediated autoimmunity: viral peptides activate human T cell clones specific for myelin basic protein. Cell 80 (1995) 695-705
    • (1995) Cell , vol.80 , pp. 695-705
    • Wucherpfennig, K.W.1    Strominger, J.L.2
  • 4
    • 0037309220 scopus 로고    scopus 로고
    • Cross-reactivity with myelin basic protein and human herpesvirus-6 in multiple sclerosis
    • Tejada-Simon M.V., Zang Y.C., Hong J., Rivera V.M., and Zhang J.Z. Cross-reactivity with myelin basic protein and human herpesvirus-6 in multiple sclerosis. Ann. Neurol. 53 (2003) 189-197
    • (2003) Ann. Neurol. , vol.53 , pp. 189-197
    • Tejada-Simon, M.V.1    Zang, Y.C.2    Hong, J.3    Rivera, V.M.4    Zhang, J.Z.5
  • 5
    • 0142234077 scopus 로고    scopus 로고
    • Multiple sclerosis: an important role for post-translational modifications of myelin basic protein in pathogenesis
    • Kim J.K., Mastronardi F.G., Wood D.D., Lubman D.M., Zand R., and Moscarello M.A. Multiple sclerosis: an important role for post-translational modifications of myelin basic protein in pathogenesis. Mol. Cell Proteomics 2 (2003) 453-462
    • (2003) Mol. Cell Proteomics , vol.2 , pp. 453-462
    • Kim, J.K.1    Mastronardi, F.G.2    Wood, D.D.3    Lubman, D.M.4    Zand, R.5    Moscarello, M.A.6
  • 6
    • 0016272941 scopus 로고
    • Phosphorylation of myelin basic protein
    • Steck A.J., and Appel S.H. Phosphorylation of myelin basic protein. J. Biol. Chem. 249 (1974) 5416-5420
    • (1974) J. Biol. Chem. , vol.249 , pp. 5416-5420
    • Steck, A.J.1    Appel, S.H.2
  • 7
    • 0020805751 scopus 로고
    • Phosphate groups modifying myelin basic proteins are metabolically labile; methyl groups are stable
    • DesJardins K.C., and Morell P. Phosphate groups modifying myelin basic proteins are metabolically labile; methyl groups are stable. J. Cell Biol. 97 (1983) 438-446
    • (1983) J. Cell Biol. , vol.97 , pp. 438-446
    • DesJardins, K.C.1    Morell, P.2
  • 8
    • 0032840879 scopus 로고    scopus 로고
    • Regulation of myelin basic protein phosphorylation by mitogen-activated protein kinase during increased action potential firing in the hippocampus
    • Atkins C.M., Yon M., Groome N.P., and Sweatt J.D. Regulation of myelin basic protein phosphorylation by mitogen-activated protein kinase during increased action potential firing in the hippocampus. J. Neurochem. 73 (1999) 1090-1097
    • (1999) J. Neurochem. , vol.73 , pp. 1090-1097
    • Atkins, C.M.1    Yon, M.2    Groome, N.P.3    Sweatt, J.D.4
  • 9
    • 30744479193 scopus 로고    scopus 로고
    • Effect of phosphorylation of myelin basic protein by MAPK on its interactions with actin and actin binding to a lipid membrane in vitro
    • Boggs J.M., Rangaraj G., Gao W., and Heng Y.M. Effect of phosphorylation of myelin basic protein by MAPK on its interactions with actin and actin binding to a lipid membrane in vitro. Biochemistry 45 (2006) 391-401
    • (2006) Biochemistry , vol.45 , pp. 391-401
    • Boggs, J.M.1    Rangaraj, G.2    Gao, W.3    Heng, Y.M.4
  • 10
    • 0024334338 scopus 로고
    • Secondary structure of charge isomers of myelin basic protein before and after phosphorylation
    • Ramwani J.J., Epand R.M., and Moscarello M.A. Secondary structure of charge isomers of myelin basic protein before and after phosphorylation. Biochemistry 28 (1989) 6538-6543
    • (1989) Biochemistry , vol.28 , pp. 6538-6543
    • Ramwani, J.J.1    Epand, R.M.2    Moscarello, M.A.3
  • 11
    • 0025258896 scopus 로고
    • Identification by mass spectrometry of threonine 97 in bovine myelin basic protein as a specific phosphorylation site for mitogen-activated protein kinase
    • Erickson A.K., Payne D.M., Martino P.A., Rossomando A.J., Shabanowitz J., Weber M.J., Hunt D.F., and Sturgill T.W. Identification by mass spectrometry of threonine 97 in bovine myelin basic protein as a specific phosphorylation site for mitogen-activated protein kinase. J. Biol. Chem. 265 (1990) 19728-19735
    • (1990) J. Biol. Chem. , vol.265 , pp. 19728-19735
    • Erickson, A.K.1    Payne, D.M.2    Martino, P.A.3    Rossomando, A.J.4    Shabanowitz, J.5    Weber, M.J.6    Hunt, D.F.7    Sturgill, T.W.8
  • 12
    • 33947371742 scopus 로고    scopus 로고
    • Partitioning of myelin basic protein into membrane microdomains in a spontaneously demyelinating mouse model for multiple sclerosis
    • DeBruin L.S., Haines J.D., Bienzle D., and Harauz G. Partitioning of myelin basic protein into membrane microdomains in a spontaneously demyelinating mouse model for multiple sclerosis. Biochem. Cell Biol. 84 (2006) 993-1005
    • (2006) Biochem. Cell Biol. , vol.84 , pp. 993-1005
    • DeBruin, L.S.1    Haines, J.D.2    Bienzle, D.3    Harauz, G.4
  • 14
    • 0029969271 scopus 로고    scopus 로고
    • Identification of a mitogen-activated protein kinase site in human myelin basic protein in situ
    • Yon M., Ackerley C.A., Mastronardi F.G., Groome N., and Moscarello M.A. Identification of a mitogen-activated protein kinase site in human myelin basic protein in situ. J. Neuroimmunol. 65 (1996) 55-59
    • (1996) J. Neuroimmunol. , vol.65 , pp. 55-59
    • Yon, M.1    Ackerley, C.A.2    Mastronardi, F.G.3    Groome, N.4    Moscarello, M.A.5
  • 15
    • 30644473886 scopus 로고    scopus 로고
    • Myelin basic protein, an autoantigen in multiple sclerosis, is selectively processed by human trypsin 4
    • Medveczky P., Antal J., Patthy A., Kekesi K., Juhasz G., Szilagyi L., and Graf L. Myelin basic protein, an autoantigen in multiple sclerosis, is selectively processed by human trypsin 4. FEBS Lett. 580 (2006) 545-552
    • (2006) FEBS Lett. , vol.580 , pp. 545-552
    • Medveczky, P.1    Antal, J.2    Patthy, A.3    Kekesi, K.4    Juhasz, G.5    Szilagyi, L.6    Graf, L.7
  • 16
    • 0031214792 scopus 로고    scopus 로고
    • High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose-binding-protein double-affinity fusion system
    • Pryor K.D., and Leiting B. High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose-binding-protein double-affinity fusion system. Protein Expr. Purif. 10 (1997) 309-319
    • (1997) Protein Expr. Purif. , vol.10 , pp. 309-319
    • Pryor, K.D.1    Leiting, B.2
  • 17
    • 47849106101 scopus 로고    scopus 로고
    • Tait, A.R. and Straus, S.K. (in preparation) Purification and characterization of U24 - a membrane protein from human herpesvirus type-6. Protein Expr. Purif.
    • Tait, A.R. and Straus, S.K. (in preparation) Purification and characterization of U24 - a membrane protein from human herpesvirus type-6. Protein Expr. Purif.
  • 18
    • 0024411870 scopus 로고
    • Protein measurement using bicinchoninic acid: elimination of interfering substances
    • Brown R.E., Jarvis K.L., and Hyland K.J. Protein measurement using bicinchoninic acid: elimination of interfering substances. Anal. Biochem. 180 (1989) 136-139
    • (1989) Anal. Biochem. , vol.180 , pp. 136-139
    • Brown, R.E.1    Jarvis, K.L.2    Hyland, K.J.3
  • 19
    • 0016770567 scopus 로고
    • Solution behavior, circular dichroism and 22 HMz PMR studies of the bovine myelin basic protein
    • Liebes L.F., Zand R., and Phillips W.D. Solution behavior, circular dichroism and 22 HMz PMR studies of the bovine myelin basic protein. Biochim. Biophys. Acta 405 (1975) 27-39
    • (1975) Biochim. Biophys. Acta , vol.405 , pp. 27-39
    • Liebes, L.F.1    Zand, R.2    Phillips, W.D.3
  • 20
    • 0037325818 scopus 로고    scopus 로고
    • A quantitative method for measuring protein phosphorylation
    • McKenzie J.A., and Strauss P.R. A quantitative method for measuring protein phosphorylation. Anal. Biochem. 313 (2003) 9-16
    • (2003) Anal. Biochem. , vol.313 , pp. 9-16
    • McKenzie, J.A.1    Strauss, P.R.2
  • 21
    • 0025133304 scopus 로고
    • An alternative method for a fast separation of phosphotyrosine
    • Munoz G., and Marshall S.H. An alternative method for a fast separation of phosphotyrosine. Anal. Biochem. 190 (1990) 233-237
    • (1990) Anal. Biochem. , vol.190 , pp. 233-237
    • Munoz, G.1    Marshall, S.H.2
  • 22
    • 0346079910 scopus 로고    scopus 로고
    • Thr94 in bovine myelin basic protein is a second phosphorylation site for 42-kDa mitogen-activated protein kinase (ERK2)
    • Hirschberg D., Radmark O., Jornvall H., and Bergman T. Thr94 in bovine myelin basic protein is a second phosphorylation site for 42-kDa mitogen-activated protein kinase (ERK2). J. Protein Chem. 22 (2003) 177-181
    • (2003) J. Protein Chem. , vol.22 , pp. 177-181
    • Hirschberg, D.1    Radmark, O.2    Jornvall, H.3    Bergman, T.4
  • 23
    • 0027165150 scopus 로고
    • The mitogen-activated protein kinase signal transduction pathway
    • Davis R.J. The mitogen-activated protein kinase signal transduction pathway. J. Biol. Chem. 268 (1993) 14553-14556
    • (1993) J. Biol. Chem. , vol.268 , pp. 14553-14556
    • Davis, R.J.1
  • 24
    • 0022506190 scopus 로고
    • Immunocytochemical search for JC papovavirus large T-antigen in multiple sclerosis brain tissue
    • Stoner G.L., Ryschkewitsch C.F., Walker D.L., Soffer D., and Webster H.D. Immunocytochemical search for JC papovavirus large T-antigen in multiple sclerosis brain tissue. Acta Neuropathol. 70 (1986) 345-347
    • (1986) Acta Neuropathol. , vol.70 , pp. 345-347
    • Stoner, G.L.1    Ryschkewitsch, C.F.2    Walker, D.L.3    Soffer, D.4    Webster, H.D.5
  • 27
    • 15044359537 scopus 로고    scopus 로고
    • Early and late HHV-6 gene transcripts in multiple sclerosis lesions and normal appearing white matter
    • Opsahl M.L., and Kennedy P.G. Early and late HHV-6 gene transcripts in multiple sclerosis lesions and normal appearing white matter. Brain 128 (2005) 516-527
    • (2005) Brain , vol.128 , pp. 516-527
    • Opsahl, M.L.1    Kennedy, P.G.2
  • 28
    • 37849017715 scopus 로고    scopus 로고
    • Downregulation of the T-cell receptor complex and impairment of T-cell activation by human herpesvirus 6 u24 protein
    • Sullivan B.M., and Coscoy L. Downregulation of the T-cell receptor complex and impairment of T-cell activation by human herpesvirus 6 u24 protein. J. Virol. 82 (2008) 602-608
    • (2008) J. Virol. , vol.82 , pp. 602-608
    • Sullivan, B.M.1    Coscoy, L.2
  • 29
    • 33748487414 scopus 로고    scopus 로고
    • Myelin basic protein: a multifunctional protein
    • Boggs J.M. Myelin basic protein: a multifunctional protein. Cell Mol. Life Sci. 63 (2006) 1945-1961
    • (2006) Cell Mol. Life Sci. , vol.63 , pp. 1945-1961
    • Boggs, J.M.1
  • 30
    • 37849026077 scopus 로고    scopus 로고
    • Binding of the proline-rich segment of myelin basic protein to SH3 domains: spectroscopic, microarray, and modeling studies of ligand conformation and effects of posttranslational modifications
    • Polverini E., Rangaraj G., Libich D.S., Boggs J.M., and Harauz G. Binding of the proline-rich segment of myelin basic protein to SH3 domains: spectroscopic, microarray, and modeling studies of ligand conformation and effects of posttranslational modifications. Biochemistry 47 (2008) 267-282
    • (2008) Biochemistry , vol.47 , pp. 267-282
    • Polverini, E.1    Rangaraj, G.2    Libich, D.S.3    Boggs, J.M.4    Harauz, G.5
  • 31
    • 0033922393 scopus 로고    scopus 로고
    • Phosphorylation of tau alters its association with the plasma membrane
    • Ekinci F.J., and Shea T.B. Phosphorylation of tau alters its association with the plasma membrane. Cell Mol. Neurobiol. 20 (2000) 497-508
    • (2000) Cell Mol. Neurobiol. , vol.20 , pp. 497-508
    • Ekinci, F.J.1    Shea, T.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.