메뉴 건너뛰기




Volumn 53, Issue 38, 2014, Pages 6092-6102

Probing the interaction between U24 and the SH3 domain of Fyn tyrosine kinase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; ENZYMES; VIRUSES;

EID: 84907462408     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500945x     Document Type: Article
Times cited : (7)

References (47)
  • 1
    • 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. (2003) Cross-reactivity with myelin basic protein and human herpesvirus-6 in multiple sclerosis Ann. Neurol. 53, 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
  • 2
    • 84890842607 scopus 로고    scopus 로고
    • Oligoclonal bands in multiple sclerosis reactive against two herpesviruses and association with magnetic resonance imaging findings
    • Virtanen, J., Wohler, J., Fenton, K., Reich, D., and Jacobson, S. (2014) Oligoclonal bands in multiple sclerosis reactive against two herpesviruses and association with magnetic resonance imaging findings Mult. Scler. 20, 27-34
    • (2014) Mult. Scler. , vol.20 , pp. 27-34
    • Virtanen, J.1    Wohler, J.2    Fenton, K.3    Reich, D.4    Jacobson, S.5
  • 3
    • 73949102660 scopus 로고    scopus 로고
    • The U24 protein from human herpesvirus 6 and 7 affects endocytic recycling
    • Sullivan, B. M. and Coscoy, L. (2010) The U24 protein from human herpesvirus 6 and 7 affects endocytic recycling J. Virol. 84, 1265-1275
    • (2010) J. Virol. , vol.84 , pp. 1265-1275
    • Sullivan, B.M.1    Coscoy, L.2
  • 6
    • 47849114837 scopus 로고    scopus 로고
    • Phosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic protein (MBP) in multiple sclerosis
    • Tait, A. R. and Straus, S. K. (2008) Phosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic protein (MBP) in multiple sclerosis FEBS Lett. 582, 2685-2688
    • (2008) FEBS Lett. , vol.582 , pp. 2685-2688
    • Tait, A.R.1    Straus, S.K.2
  • 7
    • 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. (2008) 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, 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
  • 8
    • 84862851788 scopus 로고    scopus 로고
    • Classic 18.5- and 21.5-kDa Myelin Basic Protein Isoforms Associate with Cytoskeletal and SH3-Domain Proteins in the Immortalized N19-Oligodendroglial Cell Line Stimulated by Phorbol Ester and IGF-1
    • Smith, G. S., Homchaudhuri, L., Boggs, J. M., and Harauz, G. (2012) Classic 18.5- and 21.5-kDa Myelin Basic Protein Isoforms Associate with Cytoskeletal and SH3-Domain Proteins in the Immortalized N19-Oligodendroglial Cell Line Stimulated by Phorbol Ester and IGF-1 Neurochem. Res. 37, 1277-1295
    • (2012) Neurochem. Res. , vol.37 , pp. 1277-1295
    • Smith, G.S.1    Homchaudhuri, L.2    Boggs, J.M.3    Harauz, G.4
  • 9
    • 79958252836 scopus 로고    scopus 로고
    • From axon-glial signalling to myelination: The integrating role of oligodendroglial Fyn kinase
    • Kramer-Albers, E. M. and White, R. (2011) From axon-glial signalling to myelination: The integrating role of oligodendroglial Fyn kinase Cell. Mol. Life Sci. 68, 2003-2012
    • (2011) Cell. Mol. Life Sci. , vol.68 , pp. 2003-2012
    • Kramer-Albers, E.M.1    White, R.2
  • 10
    • 0034307614 scopus 로고    scopus 로고
    • Severe hypomyelination of the murine CNS in the absence of myelin-associated glycoprotein and fyn tyrosine kinase
    • Biffiger, K., Bartsch, S., Montag, D., Aguzzi, A., Schachner, M., and Bartsch, U. (2000) Severe hypomyelination of the murine CNS in the absence of myelin-associated glycoprotein and fyn tyrosine kinase J. Neurosci. 20, 7430-7437
    • (2000) J. Neurosci. , vol.20 , pp. 7430-7437
    • Biffiger, K.1    Bartsch, S.2    Montag, D.3    Aguzzi, A.4    Schachner, M.5    Bartsch, U.6
  • 11
    • 0027976632 scopus 로고
    • Initial events of myelination involve Fyn tyrosine kinase signalling
    • Umemori, H., Sato, S., Yagi, T., Aizawa, S., and Yamamoto, T. (1994) Initial events of myelination involve Fyn tyrosine kinase signalling Nature 367, 572-576
    • (1994) Nature , vol.367 , pp. 572-576
    • Umemori, H.1    Sato, S.2    Yagi, T.3    Aizawa, S.4    Yamamoto, T.5
  • 13
    • 0033553885 scopus 로고    scopus 로고
    • Morphological differentiation of oligodendrocytes requires activation of Fyn tyrosine kinase
    • Osterhout, D. J., Wolven, A., Wolf, R. M., Resh, M. D., and Chao, M. V. (1999) Morphological differentiation of oligodendrocytes requires activation of Fyn tyrosine kinase J. Cell Biol. 145, 1209-1218
    • (1999) J. Cell Biol. , vol.145 , pp. 1209-1218
    • Osterhout, D.J.1    Wolven, A.2    Wolf, R.M.3    Resh, M.D.4    Chao, M.V.5
  • 15
    • 80052434381 scopus 로고    scopus 로고
    • Proline substitutions and threonine pseudophosphorylation of the SH3 ligand of 18.5-kDa myelin basic protein decrease its affinity for the Fyn-SH3 domain and alter process development and protein localization in oligodendrocytes
    • Smith, G. S., De Avila, M., Paez, P. M., Spreuer, V., Wills, M. K., Jones, N., Boggs, J. M., and Harauz, G. (2012) Proline substitutions and threonine pseudophosphorylation of the SH3 ligand of 18.5-kDa myelin basic protein decrease its affinity for the Fyn-SH3 domain and alter process development and protein localization in oligodendrocytes J. Neurosci. Res. 90, 28-47
    • (2012) J. Neurosci. Res. , vol.90 , pp. 28-47
    • Smith, G.S.1    De Avila, M.2    Paez, P.M.3    Spreuer, V.4    Wills, M.K.5    Jones, N.6    Boggs, J.M.7    Harauz, G.8
  • 16
    • 69249131573 scopus 로고    scopus 로고
    • The classic basic protein of myelin: Conserved structural motifs and the dynamic molecular barcode involved in membrane adhesion and protein-protein interactions
    • Harauz, G. and Libich, D. S. (2009) The classic basic protein of myelin: Conserved structural motifs and the dynamic molecular barcode involved in membrane adhesion and protein-protein interactions Curr. Protein Pept. Sci. 10, 196-215
    • (2009) Curr. Protein Pept. Sci. , vol.10 , pp. 196-215
    • Harauz, G.1    Libich, D.S.2
  • 17
    • 84866640683 scopus 로고    scopus 로고
    • Solution nuclear magnetic resonance structure and molecular dynamics simulations of a murine 18.5 kDa myelin basic protein segment (S72-S107) in association with dodecylphosphocholine micelles
    • Ahmed, M. A., De Avila, M., Polverini, E., Bessonov, K., Bamm, V. V., and Harauz, G. (2012) Solution nuclear magnetic resonance structure and molecular dynamics simulations of a murine 18.5 kDa myelin basic protein segment (S72-S107) in association with dodecylphosphocholine micelles Biochemistry 51, 7475-7487
    • (2012) Biochemistry , vol.51 , pp. 7475-7487
    • Ahmed, M.A.1    De Avila, M.2    Polverini, E.3    Bessonov, K.4    Bamm, V.V.5    Harauz, G.6
  • 18
    • 40149102826 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A protein binds the SH3 domain of the Fyn tyrosine kinase with high affinity: Mutagenic analysis of residues within the SH3 domain that contribute to the interaction
    • Shelton, H. and Harris, M. (2008) Hepatitis C virus NS5A protein binds the SH3 domain of the Fyn tyrosine kinase with high affinity: Mutagenic analysis of residues within the SH3 domain that contribute to the interaction Virol. J. 5, 24
    • (2008) Virol. J. , vol.5 , pp. 24
    • Shelton, H.1    Harris, M.2
  • 19
    • 80051577496 scopus 로고    scopus 로고
    • Overexpression and purification of U24 from human herpesvirus type-6 in E. Coli: Unconventional use of oxidizing environments with a maltose binding protein-hexahistine dual tag to enhance membrane protein yield
    • Tait, A. R. and Straus, S. K. (2011) Overexpression and purification of U24 from human herpesvirus type-6 in E. coli: Unconventional use of oxidizing environments with a maltose binding protein-hexahistine dual tag to enhance membrane protein yield Microb. Cell Fact. 10, 51
    • (2011) Microb. Cell Fact. , vol.10 , pp. 51
    • Tait, A.R.1    Straus, S.K.2
  • 20
    • 42549119962 scopus 로고    scopus 로고
    • Distinct endocytic recycling of myelin proteins promotes oligodendroglial membrane remodeling
    • Winterstein, C., Trotter, J., and Kramer-Albers, E. M. (2008) Distinct endocytic recycling of myelin proteins promotes oligodendroglial membrane remodeling J. Cell Sci. 121, 834-842
    • (2008) J. Cell Sci. , vol.121 , pp. 834-842
    • Winterstein, C.1    Trotter, J.2    Kramer-Albers, E.M.3
  • 21
    • 0027208292 scopus 로고
    • Identification of cellular proteins that bind to the human immunodeficiency virus type 1 nef gene product in vitro: A role for myristylation
    • Harris, M. and Coates, K. (1993) Identification of cellular proteins that bind to the human immunodeficiency virus type 1 nef gene product in vitro: A role for myristylation J. Gen. Virol. 74 (Part 8) 1581-1589
    • (1993) J. Gen. Virol. , vol.74 , Issue.PART 8 , pp. 1581-1589
    • Harris, M.1    Coates, K.2
  • 22
    • 78349238929 scopus 로고    scopus 로고
    • Importance of residue 13 and the C-terminus for the structure and activity of the antimicrobial peptide aurein 2.2
    • Cheng, J. T., Hale, J. D., Kindrachuk, J., Jenssen, H., Elliott, M., Hancock, R. E., and Straus, S. K. (2010) Importance of residue 13 and the C-terminus for the structure and activity of the antimicrobial peptide aurein 2.2 Biophys. J. 99, 2926-2935
    • (2010) Biophys. J. , vol.99 , pp. 2926-2935
    • Cheng, J.T.1    Hale, J.D.2    Kindrachuk, J.3    Jenssen, H.4    Elliott, M.5    Hancock, R.E.6    Straus, S.K.7
  • 23
    • 78650624171 scopus 로고    scopus 로고
    • The importance of bacterial membrane composition in the structure and function of aurein 2.2 and selected variants
    • Cheng, J. T., Hale, J. D., Elliott, M., Hancock, R. E., and Straus, S. K. (2011) The importance of bacterial membrane composition in the structure and function of aurein 2.2 and selected variants Biochim. Biophys. Acta 1808, 622-633
    • (2011) Biochim. Biophys. Acta , vol.1808 , pp. 622-633
    • Cheng, J.T.1    Hale, J.D.2    Elliott, M.3    Hancock, R.E.4    Straus, S.K.5
  • 25
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • Edelhoch, H. (1967) Spectroscopic determination of tryptophan and tyrosine in proteins Biochemistry 6, 1948-1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 26
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4, 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 28
    • 29344434301 scopus 로고    scopus 로고
    • Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain
    • Zarrine-Afsar, A., Mittermaier, A., Kay, L. E., and Davidson, A. R. (2006) Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain Protein Sci. 15, 162-170
    • (2006) Protein Sci. , vol.15 , pp. 162-170
    • Zarrine-Afsar, A.1    Mittermaier, A.2    Kay, L.E.3    Davidson, A.R.4
  • 29
    • 0029753011 scopus 로고    scopus 로고
    • Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase
    • Renzoni, D. A., Pugh, D. J., Siligardi, G., Das, P., Morton, C. J., Rossi, C., Waterfield, M. D., Campbell, I. D., and Ladbury, J. E. (1996) Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase Biochemistry 35, 15646-15653
    • (1996) Biochemistry , vol.35 , pp. 15646-15653
    • Renzoni, D.A.1    Pugh, D.J.2    Siligardi, G.3    Das, P.4    Morton, C.J.5    Rossi, C.6    Waterfield, M.D.7    Campbell, I.D.8    Ladbury, J.E.9
  • 36
    • 33646940952 scopus 로고
    • Numerical-Integration of Cartesian Equations of Motion of a System with Constraints: Molecular-Dynamics of N-Alkanes
    • Ryckaert, J. P., Ciccotti, G., and Berendsen, H. J. C. (1977) Numerical-Integration of Cartesian Equations of Motion of a System with Constraints: Molecular-Dynamics of N-Alkanes J. Comput. Phys. 23, 327-341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 37
    • 4544369164 scopus 로고
    • A generalized reaction field method for molecular-dynamics simulations
    • Tironi, I. G., Sperb, R., Smith, P. E., and van Gunsteren, W. F. (1995) A Generalized Reaction Field Method for Molecular-Dynamics Simulations J. Chem. Phys. 102, 5451-5459
    • (1995) J. Chem. Phys. , vol.102 , pp. 5451-5459
    • Tironi, I.G.1    Sperb, R.2    Smith, P.E.3    Van Gunsteren, W.F.4
  • 38
    • 24044465136 scopus 로고    scopus 로고
    • Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region
    • Jia, C. Y., Nie, J., Wu, C., Li, C., and Li, S. S. (2005) Novel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich region Mol. Cell. Proteomics 4, 1155-1166
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1155-1166
    • Jia, C.Y.1    Nie, J.2    Wu, C.3    Li, C.4    Li, S.S.5
  • 39
    • 0346850829 scopus 로고    scopus 로고
    • Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain
    • Kaneko, T., Kumasaka, T., Ganbe, T., Sato, T., Miyazawa, K., Kitamura, N., and Tanaka, N. (2003) Structural insight into modest binding of a non-PXXP ligand to the signal transducing adaptor molecule-2 Src homology 3 domain J. Biol. Chem. 278, 48162-48168
    • (2003) J. Biol. Chem. , vol.278 , pp. 48162-48168
    • Kaneko, T.1    Kumasaka, T.2    Ganbe, T.3    Sato, T.4    Miyazawa, K.5    Kitamura, N.6    Tanaka, N.7
  • 40
    • 0032553012 scopus 로고    scopus 로고
    • RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef
    • Arold, S., OBrien, R., Franken, P., Strub, M. P., Hoh, F., Dumas, C., and Ladbury, J. E. (1998) RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef Biochemistry 37, 14683-14691
    • (1998) Biochemistry , vol.37 , pp. 14683-14691
    • Arold, S.1    Obrien, R.2    Franken, P.3    Strub, M.P.4    Hoh, F.5    Dumas, C.6    Ladbury, J.E.7
  • 41
    • 0036035968 scopus 로고    scopus 로고
    • Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions
    • Bochicchio, B. and Tamburro, A. M. (2002) Polyproline II structure in proteins: Identification by chiroptical spectroscopies, stability, and functions Chirality 14, 782-792
    • (2002) Chirality , vol.14 , pp. 782-792
    • Bochicchio, B.1    Tamburro, A.M.2
  • 42
    • 2442522724 scopus 로고    scopus 로고
    • Short sequences of non-proline residues can adopt the polyproline II helical conformation
    • Chellgren, B. W. and Creamer, T. P. (2004) Short sequences of non-proline residues can adopt the polyproline II helical conformation Biochemistry 43, 5864-5869
    • (2004) Biochemistry , vol.43 , pp. 5864-5869
    • Chellgren, B.W.1    Creamer, T.P.2
  • 43
    • 0030941828 scopus 로고    scopus 로고
    • Regulation of integrin-mediated p130(Cas) tyrosine phosphorylation in human B cells. A role for p59(Fyn) and SHP2
    • Manie, S. N., Astier, A., Haghayeghi, N., Canty, T., Druker, B. J., Hirai, H., and Freedman, A. S. (1997) Regulation of integrin-mediated p130(Cas) tyrosine phosphorylation in human B cells. A role for p59(Fyn) and SHP2 J. Biol. Chem. 272, 15636-15641
    • (1997) J. Biol. Chem. , vol.272 , pp. 15636-15641
    • Manie, S.N.1    Astier, A.2    Haghayeghi, N.3    Canty, T.4    Druker, B.J.5    Hirai, H.6    Freedman, A.S.7
  • 44
    • 0032211806 scopus 로고    scopus 로고
    • Fyn, a Src family tyrosine kinase
    • Resh, M. D. (1998) Fyn, a Src family tyrosine kinase Int. J. Biochem. Cell Biol. 30, 1159-1162
    • (1998) Int. J. Biochem. Cell Biol. , vol.30 , pp. 1159-1162
    • Resh, M.D.1
  • 45
    • 0029959928 scopus 로고    scopus 로고
    • Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLC, Crk, and Grb2
    • Sparks, A. B., Rider, J. E., Hoffman, N. G., Fowlkes, D. M., Quilliam, L. A., and Kay, B. K. (1996) Distinct ligand preferences of Src homology 3 domains from Src, Yes, Abl, Cortactin, p53bp2, PLC, Crk, and Grb2 Proc. Natl. Acad. Sci. U.S.A. 93, 1540-1544
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 1540-1544
    • Sparks, A.B.1    Rider, J.E.2    Hoffman, N.G.3    Fowlkes, D.M.4    Quilliam, L.A.5    Kay, B.K.6
  • 46
    • 13944249955 scopus 로고    scopus 로고
    • Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility
    • Vaynberg, J., Fukuda, T., Chen, K., Vinogradova, O., Velyvis, A., Tu, Y. Z., Ng, L., Wu, C. Y., and Qin, J. (2005) Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility Mol. Cell 17, 513-523
    • (2005) Mol. Cell , vol.17 , pp. 513-523
    • Vaynberg, J.1    Fukuda, T.2    Chen, K.3    Vinogradova, O.4    Velyvis, A.5    Tu, Y.Z.6    Ng, L.7    Wu, C.Y.8    Qin, J.9
  • 47
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W. and Sander, C. (1983) Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22, 2577-2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.