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Volumn 31, Issue 7, 2006, Pages 366-373

A role for zinc in postsynaptic density asSAMbly and plasticity?

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; CYTOSKELETON PROTEIN; GLUTAMIC ACID; IONOTROPIC RECEPTOR; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEIN SHANK3; SCAFFOLD PROTEIN; SHANK PROTEIN; UNCLASSIFIED DRUG; ZINC ION;

EID: 33745958293     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2006.05.007     Document Type: Article
Times cited : (91)

References (55)
  • 1
    • 0031442806 scopus 로고    scopus 로고
    • Enlightening the postsynaptic density
    • Ziff E. Enlightening the postsynaptic density. Neuron 19 (1997) 1163-1174
    • (1997) Neuron , vol.19 , pp. 1163-1174
    • Ziff, E.1
  • 2
    • 0035865546 scopus 로고    scopus 로고
    • Laminar organization of the NMDA receptor complex within the postsynaptic density
    • Valtschanoff J.G., and Weinberg R.J. Laminar organization of the NMDA receptor complex within the postsynaptic density. J. Neurosci. 21 (2001) 1211-1217
    • (2001) J. Neurosci. , vol.21 , pp. 1211-1217
    • Valtschanoff, J.G.1    Weinberg, R.J.2
  • 3
    • 0036568565 scopus 로고    scopus 로고
    • Molecular mechanisms of CNS synaptogenesis
    • Garner C.C., et al. Molecular mechanisms of CNS synaptogenesis. Trends Neurosci. 25 (2002) 243-251
    • (2002) Trends Neurosci. , vol.25 , pp. 243-251
    • Garner, C.C.1
  • 4
    • 5044224260 scopus 로고    scopus 로고
    • PDZ domain proteins of synapses
    • Kim E., and Sheng M. PDZ domain proteins of synapses. Nat. Rev. Neurosci. 5 (2004) 771-781
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 771-781
    • Kim, E.1    Sheng, M.2
  • 5
    • 0036467761 scopus 로고    scopus 로고
    • Molecular morphogens for dendritic spines
    • Ehlers M.D. Molecular morphogens for dendritic spines. Trends Neurosci. 25 (2002) 64-67
    • (2002) Trends Neurosci. , vol.25 , pp. 64-67
    • Ehlers, M.D.1
  • 6
    • 17044378032 scopus 로고    scopus 로고
    • Shank expression is sufficient to induce functional dendritic spine synapses in aspiny neurons
    • Roussignol G., et al. Shank expression is sufficient to induce functional dendritic spine synapses in aspiny neurons. J. Neurosci. 25 (2005) 3560-3570
    • (2005) J. Neurosci. , vol.25 , pp. 3560-3570
    • Roussignol, G.1
  • 7
    • 0036316727 scopus 로고    scopus 로고
    • ProSAP/Shank proteins - a family of higher order organizing molecules of the postsynaptic density with an emerging role in human neurological disease
    • Boeckers T.M., et al. ProSAP/Shank proteins - a family of higher order organizing molecules of the postsynaptic density with an emerging role in human neurological disease. J. Neurochem. 81 (2002) 903-910
    • (2002) J. Neurochem. , vol.81 , pp. 903-910
    • Boeckers, T.M.1
  • 8
    • 0034721678 scopus 로고    scopus 로고
    • Signal-processing machines at the postsynaptic density
    • Kennedy M.B. Signal-processing machines at the postsynaptic density. Science 290 (2000) 750-754
    • (2000) Science , vol.290 , pp. 750-754
    • Kennedy, M.B.1
  • 9
    • 31544482776 scopus 로고    scopus 로고
    • An architectural framework that may lie at the core of the postsynaptic density
    • Baron M.K., et al. An architectural framework that may lie at the core of the postsynaptic density. Science 311 (2006) 531-535
    • (2006) Science , vol.311 , pp. 531-535
    • Baron, M.K.1
  • 10
    • 13244277917 scopus 로고    scopus 로고
    • Zinc-specific autometallographic in vivo selenium methods: tracing of zinc-enriched (ZEN) terminals, ZEN pathways, and pools of zinc ions in a multitude of other ZEN cells
    • Danscher G., and Stoltenberg M. Zinc-specific autometallographic in vivo selenium methods: tracing of zinc-enriched (ZEN) terminals, ZEN pathways, and pools of zinc ions in a multitude of other ZEN cells. J. Histochem. Cytochem. 53 (2005) 141-153
    • (2005) J. Histochem. Cytochem. , vol.53 , pp. 141-153
    • Danscher, G.1    Stoltenberg, M.2
  • 11
    • 20144377557 scopus 로고    scopus 로고
    • The neurobiology of zinc in health and disease
    • Fredericksen C.J., et al. The neurobiology of zinc in health and disease. Nat. Rev. Neurosci. 6 (2005) 449-462
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 449-462
    • Fredericksen, C.J.1
  • 12
    • 0034044563 scopus 로고    scopus 로고
    • The Shank family of scaffold proteins
    • Sheng M., and Kim E. The Shank family of scaffold proteins. J. Cell Sci. 113 (2000) 1851-1856
    • (2000) J. Cell Sci. , vol.113 , pp. 1851-1856
    • Sheng, M.1    Kim, E.2
  • 13
    • 13244272115 scopus 로고    scopus 로고
    • C-terminal synaptic targeting elements for postsynaptic density proteins ProSAP1/Shank2 and ProSAP2/Shank3
    • Boeckers T.M., et al. C-terminal synaptic targeting elements for postsynaptic density proteins ProSAP1/Shank2 and ProSAP2/Shank3. J. Neurochem. 92 (2005) 519-524
    • (2005) J. Neurochem. , vol.92 , pp. 519-524
    • Boeckers, T.M.1
  • 14
    • 0034879863 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphology and synaptic function by Shank and Homer
    • Sala C., et al. Regulation of dendritic spine morphology and synaptic function by Shank and Homer. Neuron 31 (2001) 115-130
    • (2001) Neuron , vol.31 , pp. 115-130
    • Sala, C.1
  • 15
    • 0034927366 scopus 로고    scopus 로고
    • Disruption of the ProSAP2 gene in a t(12;22)(q24.1;q13.3) is associated with the 22q13.3 deletion syndrome
    • Bonaglia M.C., et al. Disruption of the ProSAP2 gene in a t(12;22)(q24.1;q13.3) is associated with the 22q13.3 deletion syndrome. Am. J. Hum. Genet. 69 (2001) 261-268
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 261-268
    • Bonaglia, M.C.1
  • 16
    • 0042828948 scopus 로고    scopus 로고
    • Molecular characterization of the 22q13 deletion syndrome supports the role of haploinsufficiency of SHANK3/PROSAP2 in the major neurological symptoms
    • Wilson H.L., et al. Molecular characterization of the 22q13 deletion syndrome supports the role of haploinsufficiency of SHANK3/PROSAP2 in the major neurological symptoms. J. Med. Genet. 40 (2003) 575-584
    • (2003) J. Med. Genet. , vol.40 , pp. 575-584
    • Wilson, H.L.1
  • 17
    • 30344442873 scopus 로고    scopus 로고
    • Qiao, F. and Bowie, J.U. (2005) The many faces of SAM. Sci. STKE 2005, re7
  • 18
    • 30344433269 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction
    • Kwan J.J., et al. Saccharomyces cerevisiae Ste50 binds the MAPKKK Ste11 through a head-to-tail SAM domain interaction. J. Mol. Biol. 356 (2006) 142-154
    • (2006) J. Mol. Biol. , vol.356 , pp. 142-154
    • Kwan, J.J.1
  • 19
    • 14144255403 scopus 로고    scopus 로고
    • Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast: implications for efficient signaling through the MAPK cascades
    • Bhattacharjya S., et al. Polymerization of the SAM domain of MAPKKK Ste11 from the budding yeast: implications for efficient signaling through the MAPK cascades. Protein Sci. 14 (2005) 828-835
    • (2005) Protein Sci. , vol.14 , pp. 828-835
    • Bhattacharjya, S.1
  • 20
    • 23044476138 scopus 로고    scopus 로고
    • Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer
    • Kim C.A., et al. Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer. J. Biol. Chem. 280 (2005) 27769-27775
    • (2005) J. Biol. Chem. , vol.280 , pp. 27769-27775
    • Kim, C.A.1
  • 21
    • 3242688256 scopus 로고    scopus 로고
    • Derepression by depolymerization; structural insights into the regulation of Yan by Mae
    • Qiao F., et al. Derepression by depolymerization; structural insights into the regulation of Yan by Mae. Cell 118 (2004) 163-173
    • (2004) Cell , vol.118 , pp. 163-173
    • Qiao, F.1
  • 22
    • 7644226406 scopus 로고    scopus 로고
    • Tankyrase polymerization is controlled by its sterile α motif and poly(ADP-ribose) polymerase domains
    • De Rycker M., and Price C.M. Tankyrase polymerization is controlled by its sterile α motif and poly(ADP-ribose) polymerase domains. Mol. Cell. Biol. 24 (2004) 9802-9812
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9802-9812
    • De Rycker, M.1    Price, C.M.2
  • 23
    • 30444442307 scopus 로고    scopus 로고
    • Mae inhibits Pointed-P2 transcriptional activity by blocking its MAPK docking site
    • Qiao F., et al. Mae inhibits Pointed-P2 transcriptional activity by blocking its MAPK docking site. EMBO J. 25 (2006) 70-79
    • (2006) EMBO J. , vol.25 , pp. 70-79
    • Qiao, F.1
  • 24
    • 23744450036 scopus 로고    scopus 로고
    • Antagonistic regulation of Yan nuclear export by Mae and Crm1 may increase the stringency of the Ras response
    • Song H., et al. Antagonistic regulation of Yan nuclear export by Mae and Crm1 may increase the stringency of the Ras response. Genes Dev. 19 (2005) 1767-1772
    • (2005) Genes Dev. , vol.19 , pp. 1767-1772
    • Song, H.1
  • 25
    • 32244436130 scopus 로고    scopus 로고
    • Sequence-specific recognition of RNA hairpins by the SAM domain of Vts1p
    • Aviv T., et al. Sequence-specific recognition of RNA hairpins by the SAM domain of Vts1p. Nat. Struct. Mol. Biol. 13 (2006) 168-176
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 168-176
    • Aviv, T.1
  • 26
    • 32244447225 scopus 로고    scopus 로고
    • Shape-specific recognition in the structure of the Vts1p SAM domain with RNA
    • Oberstrass F.C., et al. Shape-specific recognition in the structure of the Vts1p SAM domain with RNA. Nat. Struct. Mol. Biol. 13 (2006) 160-167
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 160-167
    • Oberstrass, F.C.1
  • 27
    • 0033165926 scopus 로고    scopus 로고
    • Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin
    • Naisbitt S., et al. Shank, a novel family of postsynaptic density proteins that binds to the NMDA receptor/PSD-95/GKAP complex and cortactin. Neuron 23 (1999) 569-582
    • (1999) Neuron , vol.23 , pp. 569-582
    • Naisbitt, S.1
  • 28
    • 0036828330 scopus 로고    scopus 로고
    • Structural role of zinc ions bound to postsynaptic densities
    • Jan H.H., et al. Structural role of zinc ions bound to postsynaptic densities. J. Neurochem. 83 (2002) 525-534
    • (2002) J. Neurochem. , vol.83 , pp. 525-534
    • Jan, H.H.1
  • 29
    • 30044448338 scopus 로고    scopus 로고
    • The mammalian central nervous synaptic cleft contains a high density of periodically organized complexes
    • Zuber B., et al. The mammalian central nervous synaptic cleft contains a high density of periodically organized complexes. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 19192-19197
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 19192-19197
    • Zuber, B.1
  • 30
    • 0041672236 scopus 로고    scopus 로고
    • Boutons containing vesicular zinc define a subpopulation of synapses with low AMPAR content in rat hippocampus
    • Sindreu C.B., et al. Boutons containing vesicular zinc define a subpopulation of synapses with low AMPAR content in rat hippocampus. Cereb. Cortex 13 (2003) 823-829
    • (2003) Cereb. Cortex , vol.13 , pp. 823-829
    • Sindreu, C.B.1
  • 32
    • 0035657358 scopus 로고    scopus 로고
    • 2+ from presynaptic terminals into postsynaptic hippocampal neurons after physiological stimulation
    • 2+ from presynaptic terminals into postsynaptic hippocampal neurons after physiological stimulation. J. Neurophysiol. 86 (2001) 2597-2604
    • (2001) J. Neurophysiol. , vol.86 , pp. 2597-2604
    • Li, Y.1
  • 33
    • 0035887735 scopus 로고    scopus 로고
    • 2+
    • 2+. J. Neurosci. 21 (2001) 8015-8025
    • (2001) J. Neurosci. , vol.21 , pp. 8015-8025
    • Li, Y.1
  • 34
    • 0037101907 scopus 로고    scopus 로고
    • 2+ currents are mediated by calcium-permeable AMPA/kainate channels in cultured murine hippocampal neurons
    • 2+ currents are mediated by calcium-permeable AMPA/kainate channels in cultured murine hippocampal neurons. J. Physiol. 543 (2002) 35-48
    • (2002) J. Physiol. , vol.543 , pp. 35-48
    • Jia, Y.1
  • 35
    • 17144466355 scopus 로고    scopus 로고
    • Differential expression and dendritic transcript localization of Shank family members: Identification of a dendritic targeting element in the 3′ untranslated region of Shank1 mRNA
    • Bockers T.M., et al. Differential expression and dendritic transcript localization of Shank family members: Identification of a dendritic targeting element in the 3′ untranslated region of Shank1 mRNA. Mol. Cell. Neurosci. 26 (2004) 182-190
    • (2004) Mol. Cell. Neurosci. , vol.26 , pp. 182-190
    • Bockers, T.M.1
  • 36
    • 14644421469 scopus 로고    scopus 로고
    • Surface trafficking of receptors between synaptic and extrasynaptic membranes: and yet they do move!
    • Triller A., and Choquet D. Surface trafficking of receptors between synaptic and extrasynaptic membranes: and yet they do move!. Trends Neurosci. 28 (2005) 133-139
    • (2005) Trends Neurosci. , vol.28 , pp. 133-139
    • Triller, A.1    Choquet, D.2
  • 37
    • 0034721711 scopus 로고    scopus 로고
    • Actin-based plasticity in dendritic spines
    • Matus A. Actin-based plasticity in dendritic spines. Science 290 (2000) 754-758
    • (2000) Science , vol.290 , pp. 754-758
    • Matus, A.1
  • 38
    • 23244440196 scopus 로고    scopus 로고
    • The actin cytoskeleton: integrating form and function at the synapse
    • Dillon C., and Goda Y. The actin cytoskeleton: integrating form and function at the synapse. Annu. Rev. Neurosci. 28 (2005) 25-55
    • (2005) Annu. Rev. Neurosci. , vol.28 , pp. 25-55
    • Dillon, C.1    Goda, Y.2
  • 39
    • 1542620777 scopus 로고    scopus 로고
    • Linkage of the actin cytoskeleton to the postsynaptic density via direct interactions of Abp1 with the ProSAP/Shank family
    • Qualmann B., et al. Linkage of the actin cytoskeleton to the postsynaptic density via direct interactions of Abp1 with the ProSAP/Shank family. J. Neurosci. 24 (2004) 2481-2495
    • (2004) J. Neurosci. , vol.24 , pp. 2481-2495
    • Qualmann, B.1
  • 40
    • 0029798061 scopus 로고    scopus 로고
    • Induction of long-term potentiation is associated with major ultrastructural changes of activated synapses
    • Buchs P.A., and Muller D. Induction of long-term potentiation is associated with major ultrastructural changes of activated synapses. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 8040-8045
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 8040-8045
    • Buchs, P.A.1    Muller, D.2
  • 41
    • 33646476118 scopus 로고    scopus 로고
    • Imaging synaptic zinc: promises and perils
    • Kay A.R. Imaging synaptic zinc: promises and perils. Trends Neurosci. 29 (2006) 200-206
    • (2006) Trends Neurosci. , vol.29 , pp. 200-206
    • Kay, A.R.1
  • 42
    • 0036846301 scopus 로고    scopus 로고
    • ProSAP/Shank postsynaptic density proteins interact with insulin receptor tyrosine kinase substrate IRSp53
    • Bockmann J., et al. ProSAP/Shank postsynaptic density proteins interact with insulin receptor tyrosine kinase substrate IRSp53. J. Neurochem. 83 (2002) 1013-1017
    • (2002) J. Neurochem. , vol.83 , pp. 1013-1017
    • Bockmann, J.1
  • 43
    • 0036944697 scopus 로고    scopus 로고
    • The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein CDC42
    • Soltau M., et al. The insulin receptor substrate IRSp53 links postsynaptic shank1 to the small G-protein CDC42. Mol. Cell. Neurosci. 21 (2002) 575-583
    • (2002) Mol. Cell. Neurosci. , vol.21 , pp. 575-583
    • Soltau, M.1
  • 44
    • 12144249931 scopus 로고    scopus 로고
    • Postsynaptic Shank antagonizes dendrite branching induced by leucine-rich repeat protein Densin 180
    • Quitsch A., et al. Postsynaptic Shank antagonizes dendrite branching induced by leucine-rich repeat protein Densin 180. J. Neurosci. 25 (2005) 479-487
    • (2005) J. Neurosci. , vol.25 , pp. 479-487
    • Quitsch, A.1
  • 45
    • 0141918783 scopus 로고    scopus 로고
    • AMPA receptor trafficking at excitatory synapses
    • Bredt D.S., and Nicoll R.A. AMPA receptor trafficking at excitatory synapses. Neuron 40 (2003) 361-379
    • (2003) Neuron , vol.40 , pp. 361-379
    • Bredt, D.S.1    Nicoll, R.A.2
  • 46
    • 2942689457 scopus 로고    scopus 로고
    • Direct interaction of GluRδ2 with Shank scaffold proteins in cerebellar Purkinje cells
    • Uemura T., et al. Direct interaction of GluRδ2 with Shank scaffold proteins in cerebellar Purkinje cells. Mol. Cell. Neurosci. 26 (2004) 330-341
    • (2004) Mol. Cell. Neurosci. , vol.26 , pp. 330-341
    • Uemura, T.1
  • 47
    • 25444500447 scopus 로고    scopus 로고
    • Shank 2E binds NaPi cotransporter at the apical membrane of proximal tubule cells
    • Mc Williams R.R., et al. Shank 2E binds NaPi cotransporter at the apical membrane of proximal tubule cells. Am. J. Physiol. Cell Physiol. 289 (2005) C1042-C1051
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289
    • Mc Williams, R.R.1
  • 48
    • 13944262462 scopus 로고    scopus 로고
    • 2+ channels is dependent on a Shank-binding domain
    • 2+ channels is dependent on a Shank-binding domain. J. Neurosci. 25 (2005) 1050-1062
    • (2005) J. Neurosci. , vol.25 , pp. 1050-1062
    • Olson, P.A.1
  • 49
    • 13944250584 scopus 로고    scopus 로고
    • v1.3 L-type calcium channels with Shank
    • v1.3 L-type calcium channels with Shank. J. Neurosci. 25 (2005) 1037-1049
    • (2005) J. Neurosci. , vol.25 , pp. 1037-1049
    • Zhang, H.1
  • 50
    • 1642328118 scopus 로고    scopus 로고
    • Inhibitory regulation of cystic fibrosis transmembrane conductance regulator anion-transporting activities by Shank2
    • Kim J.Y., et al. Inhibitory regulation of cystic fibrosis transmembrane conductance regulator anion-transporting activities by Shank2. J. Biol. Chem. 279 (2004) 10389-10396
    • (2004) J. Biol. Chem. , vol.279 , pp. 10389-10396
    • Kim, J.Y.1
  • 51
    • 0037805671 scopus 로고    scopus 로고
    • The Shank family of postsynaptic density proteins interacts with and promotes synaptic accumulation of the βPix guanine nucleotide exchange factor for Rac1 and CDC42
    • Park E., et al. The Shank family of postsynaptic density proteins interacts with and promotes synaptic accumulation of the βPix guanine nucleotide exchange factor for Rac1 and CDC42. J. Biol. Chem. 278 (2003) 19220-19229
    • (2003) J. Biol. Chem. , vol.278 , pp. 19220-19229
    • Park, E.1
  • 52
    • 16844362568 scopus 로고    scopus 로고
    • The interaction of phospholipase Cβ3 with Shank2 regulates mGluR-mediated calcium signal
    • Hwang J.I., et al. The interaction of phospholipase Cβ3 with Shank2 regulates mGluR-mediated calcium signal. J. Biol. Chem. 280 (2005) 12467-12473
    • (2005) J. Biol. Chem. , vol.280 , pp. 12467-12473
    • Hwang, J.I.1
  • 53
    • 10344230447 scopus 로고    scopus 로고
    • The neuronal scaffold protein, Shank, mediates receptor tyrosine kinase signalling and biological function
    • Schuetz G., et al. The neuronal scaffold protein, Shank, mediates receptor tyrosine kinase signalling and biological function. J. Cell Biol. 167 (2004) 945-952
    • (2004) J. Cell Biol. , vol.167 , pp. 945-952
    • Schuetz, G.1
  • 54
    • 33745954665 scopus 로고    scopus 로고
    • Wendhold, D. et al. ProSAP interacting protein 1 (ProSAPiP1), a novel protein of the postsynaptic density that links the spine associated Rap-GAP (SPAR) to the scaffolding protein ProSAP2/Shank3. J. Biol. Chem. (in press)
  • 55
    • 1542351670 scopus 로고    scopus 로고
    • Bright fluorescent chemosensor platforms for imaging endogenous pools of neuronal zinc
    • Chang C.J., et al. Bright fluorescent chemosensor platforms for imaging endogenous pools of neuronal zinc. Chem. Biol. 11 (2004) 203-210
    • (2004) Chem. Biol. , vol.11 , pp. 203-210
    • Chang, C.J.1


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