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Volumn 44, Issue 9, 2005, Pages 3159-3165

Zn7metallothionein-3 and the synaptic vesicle cycle: Interaction of metallothionein-3 with the small GTPase Rab3A

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; ENZYME KINETICS; PRECIPITATION (CHEMICAL); PROTEINS; SURFACE PLASMON RESONANCE;

EID: 14644397252     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi047636d     Document Type: Article
Times cited : (55)

References (50)
  • 1
    • 0024779411 scopus 로고
    • Neurobiology of zinc and zinc-containing neurons
    • Frederickson, C. J. (1989) Neurobiology of zinc and zinc-containing neurons, Int. Rev. Neurobiol. 31, 145-238.
    • (1989) Int. Rev. Neurobiol. , vol.31 , pp. 145-238
    • Frederickson, C.J.1
  • 2
    • 0035696287 scopus 로고    scopus 로고
    • Synaptically released zinc: Physiological functions and pathological effects
    • Frederickson, C. J., and Bush, A. I. (2001) Synaptically released zinc: Physiological functions and pathological effects, BioMetals 14, 353-366.
    • (2001) BioMetals , vol.14 , pp. 353-366
    • Frederickson, C.J.1    Bush, A.I.2
  • 3
    • 3242741010 scopus 로고    scopus 로고
    • Mammalian zinc transporters
    • Liuzzi, J. P., and Cousins, R. J. (2004) Mammalian zinc transporters, Annu. Rev. Nutr. 24, 151-172.
    • (2004) Annu. Rev. Nutr. , vol.24 , pp. 151-172
    • Liuzzi, J.P.1    Cousins, R.J.2
  • 5
    • 0033574071 scopus 로고    scopus 로고
    • Elimination of zinc from synaptic vesicles in the intact mouse brain by disruption of the ZnT3 gene
    • Cole, T. B., Wenzel, H. J., Kafer, K. E., Schwartzkroin, P. A., and Palmiter, R. D. (1999) Elimination of zinc from synaptic vesicles in the intact mouse brain by disruption of the ZnT3 gene, Proc. Natl. Acad. Sci. U.S.A. 96, 1716-1721.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1716-1721
    • Cole, T.B.1    Wenzel, H.J.2    Kafer, K.E.3    Schwartzkroin, P.A.4    Palmiter, R.D.5
  • 6
    • 0032555204 scopus 로고    scopus 로고
    • The elusive function of metallothioneins
    • Palmiter, R. D. (1998) The elusive function of metallothioneins, Proc. Natl. Acad. Sci. U.S.A. 95, 8428-8430.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 8428-8430
    • Palmiter, R.D.1
  • 7
    • 0038406726 scopus 로고    scopus 로고
    • Metallothioneins: New functional and structural insights
    • Vašák, M., and Hasler, D. W. (2000) Metallothioneins: New functional and structural insights, Curr. Opin. Chem. Biol. 4, 177-183.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 177-183
    • Vašák, M.1    Hasler, D.W.2
  • 8
    • 0035872463 scopus 로고    scopus 로고
    • Roles of the metallothionein family of proteins in the central nervous system
    • Hidalgo, J., Aschner, M., Zatta, P., and Vašák, M. (2001) Roles of the metallothionein family of proteins in the central nervous system, Brain Res. Bull. 55, 133-145.
    • (2001) Brain Res. Bull. , vol.55 , pp. 133-145
    • Hidalgo, J.1    Aschner, M.2    Zatta, P.3    Vašák, M.4
  • 9
    • 0035968001 scopus 로고    scopus 로고
    • Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis
    • Outten, C. E., and O'Halloran, T. V. (2001) Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis, Science 292, 2488-2492.
    • (2001) Science , vol.292 , pp. 2488-2492
    • Outten, C.E.1    O'Halloran, T.V.2
  • 10
    • 0037993832 scopus 로고    scopus 로고
    • Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors
    • Finney, L. A., and O'Halloran, T. V. (2003) Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors, Science 300, 931-936.
    • (2003) Science , vol.300 , pp. 931-936
    • Finney, L.A.1    O'Halloran, T.V.2
  • 11
    • 0027394031 scopus 로고
    • The biochemical basis of zinc physiology
    • Vallee, B. L., and Falchuk, K. H. (1993) The biochemical basis of zinc physiology, Physiol. Rev. 73, 79-118.
    • (1993) Physiol. Rev. , vol.73 , pp. 79-118
    • Vallee, B.L.1    Falchuk, K.H.2
  • 12
    • 0031016825 scopus 로고    scopus 로고
    • Disruption of the metallothionein-III gene in mice: Analysis of brain zinc, behavior, and neuron vulnerability to metals, aging, and seizures
    • Erickson, J. C., Hollopeter, G., Thomas, S. A., Froelick, G. J., and Palmiter, R. D. (1997) Disruption of the metallothionein-III gene in mice: Analysis of brain zinc, behavior, and neuron vulnerability to metals, aging, and seizures, J. Neurosci. 17, 1271-1281.
    • (1997) J. Neurosci. , vol.17 , pp. 1271-1281
    • Erickson, J.C.1    Hollopeter, G.2    Thomas, S.A.3    Froelick, G.J.4    Palmiter, R.D.5
  • 13
    • 0025768860 scopus 로고
    • The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein
    • Uchida, Y., Takio, K., Titani, K., Ihara, Y., and Tomonaga, M. (1991) The growth inhibitory factor that is deficient in the Alzheimer's disease brain is a 68 amino acid metallothionein-like protein, Neuron 7, 337-347.
    • (1991) Neuron , vol.7 , pp. 337-347
    • Uchida, Y.1    Takio, K.2    Titani, K.3    Ihara, Y.4    Tomonaga, M.5
  • 14
    • 0037200013 scopus 로고    scopus 로고
    • Growth inhibitory factor prevents neurite extension and death of cortical neurons caused by high oxygen exposure through hydroxyl radical scavenging
    • Uchida, Y., Gomi, F., Masumizu, T., and Miura, Y. (2002) Growth inhibitory factor prevents neurite extension and death of cortical neurons caused by high oxygen exposure through hydroxyl radical scavenging, J. Biol. Chem. 277, 32353-32359.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32353-32359
    • Uchida, Y.1    Gomi, F.2    Masumizu, T.3    Miura, Y.4
  • 17
    • 0344394903 scopus 로고    scopus 로고
    • Zinc released from metallothionein-III may contribute to hippocampal CA1 and thalamic neuronal death following acute brain injury
    • Lee, J.-Y., Kim, J.-H., Palmiter, R. D., and Koh, J.-Y. (2003) Zinc released from metallothionein-III may contribute to hippocampal CA1 and thalamic neuronal death following acute brain injury, Exp. Neurol. 184, 337-347.
    • (2003) Exp. Neurol. , vol.184 , pp. 337-347
    • Lee, J.-Y.1    Kim, J.-H.2    Palmiter, R.D.3    Koh, J.-Y.4
  • 18
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Südhof, T. C. (2004) The synaptic vesicle cycle, Annu. Rev. Neurosci. 27, 509-547.
    • (2004) Annu. Rev. Neurosci. , vol.27 , pp. 509-547
    • Südhof, T.C.1
  • 19
    • 22244464935 scopus 로고    scopus 로고
    • Growth inhibitory factor (GIF) directly interacts with G-protein Rab3a
    • Kang, Q. H., Chen, Q. L., Ren, H. W., and Ru, B. G. (2001) Growth inhibitory factor (GIF) directly interacts with G-protein Rab3a, Prog. Biochem. Biophys. 28, 880-884.
    • (2001) Prog. Biochem. Biophys. , vol.28 , pp. 880-884
    • Kang, Q.H.1    Chen, Q.L.2    Ren, H.W.3    Ru, B.G.4
  • 21
    • 0024328734 scopus 로고
    • The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion
    • Zahraoui, A., Touchot, N., Chardin, P., and Tavitian, A. (1989) The human Rab genes encode a family of GTP-binding proteins related to yeast YPT1 and SEC4 products involved in secretion, J. Biol. Chem. 264, 12394-12401.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12394-12401
    • Zahraoui, A.1    Touchot, N.2    Chardin, P.3    Tavitian, A.4
  • 22
    • 0033520117 scopus 로고    scopus 로고
    • Evidence for a dynamic structure of human neuronal growth inhibitory factor and for major rearrangements of its metal-thiolate clusters
    • Faller, P., Hasler, D. W., Zerbe, O., Klauser, S., Winge, D. R., and Vašák, M. (1999) Evidence for a dynamic structure of human neuronal growth inhibitory factor and for major rearrangements of its metal-thiolate clusters, Biochemistry 38, 10158-10167.
    • (1999) Biochemistry , vol.38 , pp. 10158-10167
    • Faller, P.1    Hasler, D.W.2    Zerbe, O.3    Klauser, S.4    Winge, D.R.5    Vašák, M.6
  • 24
    • 0026318278 scopus 로고
    • Metal removal and substitution in vertebrate and invertebrate metallothioneins
    • Vašák, M. (1991) Metal removal and substitution in vertebrate and invertebrate metallothioneins, Methods Enzymol. 205, 452-458.
    • (1991) Methods Enzymol. , vol.205 , pp. 452-458
    • Vašák, M.1
  • 25
    • 17444437606 scopus 로고    scopus 로고
    • Distinct metal-thiolate clusters in the N-terminal domain of neuronal growth inhibitory factor
    • Faller, P., and Vašák, M. (1997) Distinct metal-thiolate clusters in the N-terminal domain of neuronal growth inhibitory factor, Biochemistry 36, 13341-13348.
    • (1997) Biochemistry , vol.36 , pp. 13341-13348
    • Faller, P.1    Vašák, M.2
  • 26
    • 0029919479 scopus 로고    scopus 로고
    • Distinct functional properties of Rab3A and Rab3B in PC12 neuroendocrine cells
    • Weber, E., Jilling, T., and Kirk, K. L. (1996) Distinct functional properties of Rab3A and Rab3B in PC12 neuroendocrine cells, J. Biol. Chem. 271, 6963-6971.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6963-6971
    • Weber, E.1    Jilling, T.2    Kirk, K.L.3
  • 27
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • Lanzetta, P. A., Alvarez, L. J., Reinach, P. S., and Candia, O. A. (1979) An improved assay for nanomole amounts of inorganic phosphate, Anal. Biochem. 100, 95-97.
    • (1979) Anal. Biochem. , vol.100 , pp. 95-97
    • Lanzetta, P.A.1    Alvarez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 28
    • 0026318277 scopus 로고
    • Cysteine modification of metallothionein
    • Hunziker, P. E. (1991) Cysteine modification of metallothionein, Methods Enzymol. 205, 399-400.
    • (1991) Methods Enzymol. , vol.205 , pp. 399-400
    • Hunziker, P.E.1
  • 29
    • 0036941677 scopus 로고    scopus 로고
    • 4-thiolate cluster of human metallothionein-3 is located in the N-terminal domain
    • 4-thiolate cluster of human metallothionein-3 is located in the N-terminal domain, J. Biol. Inorg. Chem. 7, 611-616.
    • (2002) J. Biol. Inorg. Chem. , vol.7 , pp. 611-616
    • Roschitzki, B.1    Vašák, M.2
  • 30
    • 0033561376 scopus 로고    scopus 로고
    • Structural basis of activation and GTP hydrolysis in Rab proteins
    • Dumas, J. J., Zhu, Z., Connolly, J. L., and Lambright, D. G. (1999) Structural basis of activation and GTP hydrolysis in Rab proteins, Structure 7, 413-423.
    • (1999) Structure , vol.7 , pp. 413-423
    • Dumas, J.J.1    Zhu, Z.2    Connolly, J.L.3    Lambright, D.G.4
  • 31
    • 0004608219 scopus 로고    scopus 로고
    • Importance of zinc in the central nervous system: The zinc-containing neuron
    • Frederickson, C. J., Suh, S. W., Silva, D., Frederickson, C. J., and Thompson, R. B. (2000) Importance of zinc in the central nervous system: The zinc-containing neuron, J. Nutr. 130, 1471S-1483S.
    • (2000) J. Nutr. , vol.130
    • Frederickson, C.J.1    Suh, S.W.2    Silva, D.3    Frederickson, C.J.4    Thompson, R.B.5
  • 32
    • 0032552960 scopus 로고    scopus 로고
    • Metal-thiolate clusters in the C-terminal domain of human neuronal growth inhibitory factor (GIF)
    • Hasler, D. W., Faller, P., and Vašák, M. (1998) Metal-thiolate clusters in the C-terminal domain of human neuronal growth inhibitory factor (GIF), Biochemistry 37, 14966-14973.
    • (1998) Biochemistry , vol.37 , pp. 14966-14973
    • Hasler, D.W.1    Faller, P.2    Vašák, M.3
  • 33
    • 0037076545 scopus 로고    scopus 로고
    • Brain-specific metallothionein-3 has higher metal-binding capacity than ubiquitous metallothioneins and binds metals noncooperatively
    • Palumaa, P., Eriste, E., Njunkova, O., Pokras, L., Jornvall, H., and Sillard, R. (2002) Brain-specific metallothionein-3 has higher metal-binding capacity than ubiquitous metallothioneins and binds metals noncooperatively, Biochemistry 41, 6158-6163.
    • (2002) Biochemistry , vol.41 , pp. 6158-6163
    • Palumaa, P.1    Eriste, E.2    Njunkova, O.3    Pokras, L.4    Jornvall, H.5    Sillard, R.6
  • 34
    • 0037020159 scopus 로고    scopus 로고
    • Engineering of metallothionein-3 neuroinhibitory activity into the inactive isoform metallothionein-1
    • Romero-Isart, N., Jensen, L. T., Zerbe, O., Winge, D. R., and Vašák, M. (2002) Engineering of metallothionein-3 neuroinhibitory activity into the inactive isoform metallothionein-1, J. Biol. Chem. 277, 37023-37028.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37023-37028
    • Romero-Isart, N.1    Jensen, L.T.2    Zerbe, O.3    Winge, D.R.4    Vašák, M.5
  • 35
    • 0030574080 scopus 로고    scopus 로고
    • Subcellular localization of growth inhibitory factor in rat brain: Light and electron microscopic immunohistochemical studies
    • Yamada, M., Hayashi, S., Hozumi, I., Inuzuka, T., Tsuji, S., and Takahashi, H. (1996) Subcellular localization of growth inhibitory factor in rat brain: Light and electron microscopic immunohistochemical studies, Brain Res. 735, 257-264.
    • (1996) Brain Res. , vol.735 , pp. 257-264
    • Yamada, M.1    Hayashi, S.2    Hozumi, I.3    Inuzuka, T.4    Tsuji, S.5    Takahashi, H.6
  • 36
    • 0035980002 scopus 로고    scopus 로고
    • Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants partially related through N-terminal α-helix motifs
    • Wang, X., Hu, B., Zimmermann, B., and Kilimann, M. W. (2001) Rim1 and rabphilin-3 bind Rab3-GTP by composite determinants partially related through N-terminal α-helix motifs, J. Biol. Chem. 276, 32480-32488.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32480-32488
    • Wang, X.1    Hu, B.2    Zimmermann, B.3    Kilimann, M.W.4
  • 37
    • 0037424351 scopus 로고    scopus 로고
    • Determinants of Rab5 interaction with the N terminus of early endosome antigen 1
    • Merithew, E., Stone, C., Eathiraj, S., and Lambright, D. G. (2003) Determinants of Rab5 interaction with the N terminus of early endosome antigen 1, J. Biol. Chem. 278, 8494-8500.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8494-8500
    • Merithew, E.1    Stone, C.2    Eathiraj, S.3    Lambright, D.G.4
  • 38
    • 0028243055 scopus 로고
    • Isolation, primary structures and metal binding properties of neuronal growth inhibitory factor (GIF) from bovine and equine brain
    • Pountney, D. L., Fundel, S. M., Faller, P., Birchler, N. E., Hunziker, P., and Vašák, M. (1994) Isolation, primary structures and metal binding properties of neuronal growth inhibitory factor (GIF) from bovine and equine brain, FEBS Lett. 345, 193-197.
    • (1994) FEBS Lett. , vol.345 , pp. 193-197
    • Pountney, D.L.1    Fundel, S.M.2    Faller, P.3    Birchler, N.E.4    Hunziker, P.5    Vašák, M.6
  • 39
    • 0033525215 scopus 로고    scopus 로고
    • Structural basis of Rab effector specificity: Crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A
    • Ostermeier, C., and Brunger, A. T. (1999) Structural basis of Rab effector specificity: Crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A, Cell 96, 363-374.
    • (1999) Cell , vol.96 , pp. 363-374
    • Ostermeier, C.1    Brunger, A.T.2
  • 40
    • 0035949634 scopus 로고    scopus 로고
    • Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: Metallothionein-3
    • Öz, G., Zangger, K., and Armitage, I. M. (2001) Three-dimensional structure and dynamics of a brain specific growth inhibitory factor: Metallothionein-3, Biochemistry 40, 11433-11441.
    • (2001) Biochemistry , vol.40 , pp. 11433-11441
    • Öz, G.1    Zangger, K.2    Armitage, I.M.3
  • 41
    • 2642563696 scopus 로고    scopus 로고
    • Structural principles for the multispecificity of small GTP-binding proteins
    • Biou, V., and Cherfils, J. (2004) Structural principles for the multispecificity of small GTP-binding proteins, Biochemistry 43, 6833-6840.
    • (2004) Biochemistry , vol.43 , pp. 6833-6840
    • Biou, V.1    Cherfils, J.2
  • 42
    • 0034737601 scopus 로고    scopus 로고
    • Binding of Rab3A to synaptic vesicles
    • Chou, J. H., and Jahn, R. (2000) Binding of Rab3A to synaptic vesicles, J. Biol. Chem. 275, 9433-9440.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9433-9440
    • Chou, J.H.1    Jahn, R.2
  • 45
    • 0033839040 scopus 로고    scopus 로고
    • Survey of mRNAs encoding zinc transporters and other metal complexing proteins in pancreatic islets of rats from birth to adulthood: Similar patterns in the Sprague-Dawley and Wistar BB strains
    • Clifford, K. S., and MacDonald, M. J. (2000) Survey of mRNAs encoding zinc transporters and other metal complexing proteins in pancreatic islets of rats from birth to adulthood: Similar patterns in the Sprague-Dawley and Wistar BB strains, Diabetes Res. Clin. Pract. 49, 77-85.
    • (2000) Diabetes Res. Clin. Pract. , vol.49 , pp. 77-85
    • Clifford, K.S.1    MacDonald, M.J.2
  • 47
    • 0017797285 scopus 로고
    • An improved Timm sulphide silver method for light and electron microscopic localization of heavy metals in biological tissues
    • Danscher, G., and Zimmer, J. (1978) An improved Timm sulphide silver method for light and electron microscopic localization of heavy metals in biological tissues, Histochemistry 55, 27-40.
    • (1978) Histochemistry , vol.55 , pp. 27-40
    • Danscher, G.1    Zimmer, J.2
  • 48
    • 0031818254 scopus 로고    scopus 로고
    • Expression of the gene encoding metallothionein-3 in organs of the reproductive system
    • Moffatt, P., and Seguin, C. (1998) Expression of the gene encoding metallothionein-3 in organs of the reproductive system, DNA Cell Biol. 17, 501-510.
    • (1998) DNA Cell Biol. , vol.17 , pp. 501-510
    • Moffatt, P.1    Seguin, C.2
  • 49
    • 0033168842 scopus 로고    scopus 로고
    • Identification of Rab3A GTPase as an acrosome-associated small GTP-binding protein in rat sperm
    • Iida, H., Yoshinaga, Y., Tanaka, S., Toshimori, K., and Mori, T. (1999) Identification of Rab3A GTPase as an acrosome-associated small GTP-binding protein in rat sperm, Dev. Biol. 211, 144-155.
    • (1999) Dev. Biol. , vol.211 , pp. 144-155
    • Iida, H.1    Yoshinaga, Y.2    Tanaka, S.3    Toshimori, K.4    Mori, T.5
  • 50
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling, Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2


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