메뉴 건너뛰기




Volumn 29, Issue 8, 2006, Pages 452-458

Synaptic plasticity: one STEP at a time

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PHOSPHATASE; PROTEIN KINASE FYN; STRIATAL ENRICHED TYROSINE PHOSPHATASE; UNCLASSIFIED DRUG;

EID: 33746366493     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tins.2006.06.007     Document Type: Review
Times cited : (105)

References (51)
  • 1
    • 0034142054 scopus 로고    scopus 로고
    • Postsynaptic protein phosphorylation and LTP
    • Soderling T.R., and Derkach V.A. Postsynaptic protein phosphorylation and LTP. Trends Neurosci. 23 (2000) 75-80
    • (2000) Trends Neurosci. , vol.23 , pp. 75-80
    • Soderling, T.R.1    Derkach, V.A.2
  • 2
    • 1842731881 scopus 로고    scopus 로고
    • Src kinases: a hub for NMDA receptor regulation
    • Salter M.W., and Kalia L.V. Src kinases: a hub for NMDA receptor regulation. Nat. Rev. Neurosci. 5 (2004) 317-328
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 317-328
    • Salter, M.W.1    Kalia, L.V.2
  • 3
    • 0344825108 scopus 로고    scopus 로고
    • Receptor and nonreceptor protein tyrosine phosphatases in the nervous system
    • Paul S., and Lombroso P.J. Receptor and nonreceptor protein tyrosine phosphatases in the nervous system. Cell. Mol. Life Sci. 60 (2003) 2465-2482
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2465-2482
    • Paul, S.1    Lombroso, P.J.2
  • 4
    • 2942550646 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in synaptic plasticity and memory
    • Sweatt J.D. Mitogen-activated protein kinases in synaptic plasticity and memory. Curr. Opin. Neurobiol. 14 (2004) 311-317
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 311-317
    • Sweatt, J.D.1
  • 5
    • 0038561177 scopus 로고    scopus 로고
    • Expression mechanisms underlying long-term potentiation: a postsynaptic view
    • Nicoll R.A. Expression mechanisms underlying long-term potentiation: a postsynaptic view. Philos. Trans. R. Soc. Lond. B Biol. Sci. 358 (2003) 721-726
    • (2003) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.358 , pp. 721-726
    • Nicoll, R.A.1
  • 6
    • 9944252377 scopus 로고    scopus 로고
    • Receptor trafficking and synaptic plasticity
    • Collingridge G.L., et al. Receptor trafficking and synaptic plasticity. Nat. Rev. Neurosci. 5 (2004) 952-962
    • (2004) Nat. Rev. Neurosci. , vol.5 , pp. 952-962
    • Collingridge, G.L.1
  • 7
    • 0025738171 scopus 로고
    • Molecular characterization of a protein tyrosine phosphatase enriched in striatum
    • Lombroso P.J., et al. Molecular characterization of a protein tyrosine phosphatase enriched in striatum. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 7242-7246
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 7242-7246
    • Lombroso, P.J.1
  • 8
    • 0027158376 scopus 로고
    • A protein tyrosine phosphatase expressed within dopaminoceptive neurons of the basal ganglia and related structures
    • Lombroso P.J., et al. A protein tyrosine phosphatase expressed within dopaminoceptive neurons of the basal ganglia and related structures. J. Neurosci. 13 (1993) 3064-3074
    • (1993) J. Neurosci. , vol.13 , pp. 3064-3074
    • Lombroso, P.J.1
  • 9
    • 0028899648 scopus 로고
    • Cellular and molecular characterization of a brain-enriched protein tyrosine phosphatase
    • Boulanger L.M., et al. Cellular and molecular characterization of a brain-enriched protein tyrosine phosphatase. J. Neurosci. 15 (1995) 1532-1544
    • (1995) J. Neurosci. , vol.15 , pp. 1532-1544
    • Boulanger, L.M.1
  • 10
    • 0037187645 scopus 로고    scopus 로고
    • Tyrosine phosphatase STEP is a tonic brake on induction of long-term potentiation
    • Pelkey K., et al. Tyrosine phosphatase STEP is a tonic brake on induction of long-term potentiation. Neuron 34 (2002) 127-138
    • (2002) Neuron , vol.34 , pp. 127-138
    • Pelkey, K.1
  • 11
    • 17844403782 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases and signalling
    • Stoker A.W. Protein tyrosine phosphatases and signalling. J. Endocrinol. 185 (2005) 19-33
    • (2005) J. Endocrinol. , vol.185 , pp. 19-33
    • Stoker, A.W.1
  • 12
    • 0347285350 scopus 로고    scopus 로고
    • A genomic perspective on protein tyrosine phosphatases: gene structure, pseudogenes, and genetic disease linkage
    • Andersen J.N., et al. A genomic perspective on protein tyrosine phosphatases: gene structure, pseudogenes, and genetic disease linkage. FASEB J. 18 (2004) 8-30
    • (2004) FASEB J. , vol.18 , pp. 8-30
    • Andersen, J.N.1
  • 13
    • 2942581416 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases in the human genome
    • Alonso A., et al. Protein tyrosine phosphatases in the human genome. Cell 117 (2004) 699-711
    • (2004) Cell , vol.117 , pp. 699-711
    • Alonso, A.1
  • 14
    • 0026593420 scopus 로고
    • Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase)
    • Zanke B., et al. Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase). Eur. J. Immunol. 22 (1992) 235-239
    • (1992) Eur. J. Immunol. , vol.22 , pp. 235-239
    • Zanke, B.1
  • 15
    • 0028840142 scopus 로고
    • A neuronal protein tyrosine phosphatase induced by nerve growth factor
    • Sharma E., and Lombroso P.J. A neuronal protein tyrosine phosphatase induced by nerve growth factor. J. Biol. Chem. 270 (1995) 49-53
    • (1995) J. Biol. Chem. , vol.270 , pp. 49-53
    • Sharma, E.1    Lombroso, P.J.2
  • 16
    • 0028850778 scopus 로고
    • A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain
    • Hendriks W., et al. A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain. Biochem. J. 305 (1995) 499-504
    • (1995) Biochem. J. , vol.305 , pp. 499-504
    • Hendriks, W.1
  • 17
    • 5644272856 scopus 로고    scopus 로고
    • Characterization of multiple transcripts and isoforms derived from the mouse protein tyrosine phosphatase gene Ptprr
    • Chirivi R.G., et al. Characterization of multiple transcripts and isoforms derived from the mouse protein tyrosine phosphatase gene Ptprr. Genes Cells 9 (2004) 919-933
    • (2004) Genes Cells , vol.9 , pp. 919-933
    • Chirivi, R.G.1
  • 18
    • 0029658737 scopus 로고    scopus 로고
    • STEP61: A new member of a family of brain-enriched PTPs is localized to the ER
    • Bult A., et al. STEP61: A new member of a family of brain-enriched PTPs is localized to the ER. J. Neurosci. 16 (1996) 7821-7831
    • (1996) J. Neurosci. , vol.16 , pp. 7821-7831
    • Bult, A.1
  • 19
    • 0028857858 scopus 로고
    • Immunocytochemical localization of the striatal enriched protein tyrosine phosphatase in the rat striatum: EM study
    • Oyama T., et al. Immunocytochemical localization of the striatal enriched protein tyrosine phosphatase in the rat striatum: EM study. Neuroscience 69 (1995) 869-880
    • (1995) Neuroscience , vol.69 , pp. 869-880
    • Oyama, T.1
  • 20
    • 0030932770 scopus 로고    scopus 로고
    • STEP: A family of brain enriched PTPs: Alternative splicing produces transmembrane, cytosolic and truncated isoforms
    • Bult A., et al. STEP: A family of brain enriched PTPs: Alternative splicing produces transmembrane, cytosolic and truncated isoforms. Eur. J. Cell Biol. 72 (1997) 337-344
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 337-344
    • Bult, A.1
  • 21
    • 0029045391 scopus 로고
    • Identification of two alternatively spliced transcripts of STEP: a subfamily of brain-enriched protein tyrosine phosphatases
    • Sharma E., et al. Identification of two alternatively spliced transcripts of STEP: a subfamily of brain-enriched protein tyrosine phosphatases. Mol. Brain Res. 32 (1995) 87-93
    • (1995) Mol. Brain Res. , vol.32 , pp. 87-93
    • Sharma, E.1
  • 22
    • 0037025303 scopus 로고    scopus 로고
    • Striatal enriched phosphatase 61 (STEP61) dephosphorylates Fyn at phosphotyrosine 420
    • Nguyen T.H., et al. Striatal enriched phosphatase 61 (STEP61) dephosphorylates Fyn at phosphotyrosine 420. J. Biol. Chem. 277 (2002) 24274-24279
    • (2002) J. Biol. Chem. , vol.277 , pp. 24274-24279
    • Nguyen, T.H.1
  • 23
    • 0032742620 scopus 로고    scopus 로고
    • Hypoxia-ischemia in perinatal rat brain induces the formation of a low molecular weight isoform of the protein tyrosine phosphatase, STEP
    • Gurd J., et al. Hypoxia-ischemia in perinatal rat brain induces the formation of a low molecular weight isoform of the protein tyrosine phosphatase, STEP. J. Neurochem. 73 (1999) 1990-1995
    • (1999) J. Neurochem. , vol.73 , pp. 1990-1995
    • Gurd, J.1
  • 24
    • 0032692172 scopus 로고    scopus 로고
    • Calcium-dependent cleavage of striatal enriched tyrosine phosphatase (STEP)
    • Nguyen T.H., et al. Calcium-dependent cleavage of striatal enriched tyrosine phosphatase (STEP). J. Neurochem. 73 (1999) 1995-2001
    • (1999) J. Neurochem. , vol.73 , pp. 1995-2001
    • Nguyen, T.H.1
  • 25
    • 0029869763 scopus 로고    scopus 로고
    • Neurotrophins stimulate phosphorylation of synapsin I by MAP kinase and regulate synapsin I-actin interactions
    • Jovanovic J.N., et al. Neurotrophins stimulate phosphorylation of synapsin I by MAP kinase and regulate synapsin I-actin interactions. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 3679-3683
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 3679-3683
    • Jovanovic, J.N.1
  • 26
    • 27144548450 scopus 로고    scopus 로고
    • Modulation of presynaptic plasticity and learning by the H-ras/extracellular signal-regulated kinase/synapsin I signaling pathway
    • Kushner S.A., et al. Modulation of presynaptic plasticity and learning by the H-ras/extracellular signal-regulated kinase/synapsin I signaling pathway. J. Neurosci. 25 (2005) 9721-9734
    • (2005) J. Neurosci. , vol.25 , pp. 9721-9734
    • Kushner, S.A.1
  • 27
    • 0036308524 scopus 로고    scopus 로고
    • Learning and memory functions of the basal ganglia
    • Packard M.G., and Knowlton B.J. Learning and memory functions of the basal ganglia. Annu. Rev. Neurosci. 25 (2002) 563-593
    • (2002) Annu. Rev. Neurosci. , vol.25 , pp. 563-593
    • Packard, M.G.1    Knowlton, B.J.2
  • 28
    • 0028101199 scopus 로고
    • Postsynaptic integration of glutamatergic and dopaminergic signals in the striatum
    • Kotter R. Postsynaptic integration of glutamatergic and dopaminergic signals in the striatum. Prog. Neurobiol. 44 (1994) 163-196
    • (1994) Prog. Neurobiol. , vol.44 , pp. 163-196
    • Kotter, R.1
  • 29
    • 0031939453 scopus 로고    scopus 로고
    • Dopamine and N-methyl-d-aspartate receptor interactions in the neostriatum
    • Cepeda C., and Levine M.S. Dopamine and N-methyl-d-aspartate receptor interactions in the neostriatum. Dev. Neurosci. 20 (1998) 1-18
    • (1998) Dev. Neurosci. , vol.20 , pp. 1-18
    • Cepeda, C.1    Levine, M.S.2
  • 30
    • 0037220735 scopus 로고    scopus 로고
    • NMDA-mediated activation of the protein tyrosine phosphatase, STEP, regulates the duration of ERK signaling
    • Paul S., et al. NMDA-mediated activation of the protein tyrosine phosphatase, STEP, regulates the duration of ERK signaling. Nat. Neurosci. 6 (2003) 34-42
    • (2003) Nat. Neurosci. , vol.6 , pp. 34-42
    • Paul, S.1
  • 31
    • 0034255148 scopus 로고    scopus 로고
    • Dopamine/D1 receptor mediates the phosphorylation and inactivation of the protein tyrosine phosphatase, STEP, through a PKA-mediated pathway
    • Paul S., et al. Dopamine/D1 receptor mediates the phosphorylation and inactivation of the protein tyrosine phosphatase, STEP, through a PKA-mediated pathway. J. Neurosci. 20 (2000) 5630-5638
    • (2000) J. Neurosci. , vol.20 , pp. 5630-5638
    • Paul, S.1
  • 32
    • 19944428022 scopus 로고    scopus 로고
    • Regulation of a protein phosphatase cascade allows convergent dopamine and glutamate signals to activate ERK in the striatum
    • Valjent E., et al. Regulation of a protein phosphatase cascade allows convergent dopamine and glutamate signals to activate ERK in the striatum. Proc. Natl. Acad. Sci. U. S. A. 102 (2004) 491-496
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 491-496
    • Valjent, E.1
  • 33
    • 1642414254 scopus 로고    scopus 로고
    • Hematopoietic protein tyrosine phosphatase (HePTP) phosphorylation by cAMP-dependent protein kinase in T cells: dynamics and subcellular location
    • Nika K., et al. Hematopoietic protein tyrosine phosphatase (HePTP) phosphorylation by cAMP-dependent protein kinase in T cells: dynamics and subcellular location. Biochem. J. 378 (2004) 335-342
    • (2004) Biochem. J. , vol.378 , pp. 335-342
    • Nika, K.1
  • 34
    • 0032534791 scopus 로고    scopus 로고
    • PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif
    • Pulido R., et al. PTP-SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal-regulated kinases ERK1 and ERK2 by association through a kinase interaction motif. EMBO J. 17 (1998) 7337-7350
    • (1998) EMBO J. , vol.17 , pp. 7337-7350
    • Pulido, R.1
  • 35
    • 0033597122 scopus 로고    scopus 로고
    • Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)
    • Saxena M., et al. Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP). J. Biol. Chem. 274 (1999) 11693-11700
    • (1999) J. Biol. Chem. , vol.274 , pp. 11693-11700
    • Saxena, M.1
  • 36
    • 0038845769 scopus 로고    scopus 로고
    • Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides specificity and retains ERK2 in the cytoplasm
    • Zuniga A., et al. Interaction of mitogen-activated protein kinases with the kinase interaction motif of the tyrosine phosphatase PTP-SL provides specificity and retains ERK2 in the cytoplasm. J. Biol. Chem. 274 (1999) 21900-21907
    • (1999) J. Biol. Chem. , vol.274 , pp. 21900-21907
    • Zuniga, A.1
  • 37
    • 33746337336 scopus 로고    scopus 로고
    • Paul, S. et al. (2004) Disruption of fear conditioning by STEP, a striatal enriched phosphatase, through the regulation of MAP kinase. In 2004 Abstract Viewer and Itinerary Planner, program number 632.11, Society for Neuroscience, online (http://sfn.scholarone.com/)
  • 38
    • 0034331242 scopus 로고    scopus 로고
    • Activation of ERK/MAP kinase in the amygdala is required for memory consolidation of Pavlovian fear conditioning
    • Schafe G.E., et al. Activation of ERK/MAP kinase in the amygdala is required for memory consolidation of Pavlovian fear conditioning. J. Neurosci. 20 (2000) 8177-8187
    • (2000) J. Neurosci. , vol.20 , pp. 8177-8187
    • Schafe, G.E.1
  • 39
    • 0031055324 scopus 로고    scopus 로고
    • Development of substrate trapping mutants to identify physiological substrates of PTPs
    • Flint A., et al. Development of substrate trapping mutants to identify physiological substrates of PTPs. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 1680-1685
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 1680-1685
    • Flint, A.1
  • 40
    • 0034666775 scopus 로고    scopus 로고
    • Memory consolidation of auditory pavlovian fear conditioning requires protein synthesis and protein kinase A in the amygdala
    • Schafe G.E., and LeDoux J.E. Memory consolidation of auditory pavlovian fear conditioning requires protein synthesis and protein kinase A in the amygdala. J. Neurosci. 20 (2000) RC96
    • (2000) J. Neurosci. , vol.20
    • Schafe, G.E.1    LeDoux, J.E.2
  • 41
    • 0034793235 scopus 로고    scopus 로고
    • Synaptic plasticity in the lateral amygdala: a cellular hypothesis of fear conditioning
    • Blair H.T., et al. Synaptic plasticity in the lateral amygdala: a cellular hypothesis of fear conditioning. Learn. Mem. 8 (2001) 229-242
    • (2001) Learn. Mem. , vol.8 , pp. 229-242
    • Blair, H.T.1
  • 42
    • 0026705734 scopus 로고
    • Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase
    • Zheng X.M., et al. Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase. Nature 359 (1992) 336-339
    • (1992) Nature , vol.359 , pp. 336-339
    • Zheng, X.M.1
  • 43
    • 2642710919 scopus 로고    scopus 로고
    • Physical and functional interactions between receptor-like protein-tyrosine phosphatase α and p59fyn
    • Bhandari V., et al. Physical and functional interactions between receptor-like protein-tyrosine phosphatase α and p59fyn. J. Biol. Chem. 273 (1998) 8691-8698
    • (1998) J. Biol. Chem. , vol.273 , pp. 8691-8698
    • Bhandari, V.1
  • 44
    • 33746325839 scopus 로고    scopus 로고
    • Braithwaite, S.P. et al. Regulation of NMDA receptor trafficking and function by striatal enriched tyrosine phosphatase (STEP) Eur. J. Neurosci. (in press)
  • 45
    • 23044445669 scopus 로고    scopus 로고
    • Regulation of NMDA receptor trafficking by β-amyloid
    • Snyder E.M., et al. Regulation of NMDA receptor trafficking by β-amyloid. Nat. Neurosci. 8 (2005) 1051-1058
    • (2005) Nat. Neurosci. , vol.8 , pp. 1051-1058
    • Snyder, E.M.1
  • 46
    • 1642536318 scopus 로고    scopus 로고
    • Dopamine D1-dependent trafficking of striatal N-methyl-d-aspartate glutamate receptors requires Fyn protein tyrosine kinase but not DARPP-32
    • Dunah A.W., et al. Dopamine D1-dependent trafficking of striatal N-methyl-d-aspartate glutamate receptors requires Fyn protein tyrosine kinase but not DARPP-32. Mol. Pharmacol. 65 (2004) 121-129
    • (2004) Mol. Pharmacol. , vol.65 , pp. 121-129
    • Dunah, A.W.1
  • 47
    • 0034899681 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the N-methyl-d-aspartate receptor by exogenous and postsynaptic density-associated Src-family kinases
    • Cheung H.H., and Gurd J.W. Tyrosine phosphorylation of the N-methyl-d-aspartate receptor by exogenous and postsynaptic density-associated Src-family kinases. J. Neurochem. 78 (2001) 524-534
    • (2001) J. Neurochem. , vol.78 , pp. 524-534
    • Cheung, H.H.1    Gurd, J.W.2
  • 48
    • 0347506604 scopus 로고    scopus 로고
    • Differential binding of the AP-2 adaptor complex and PSD-95 to the C-terminus of the NMDA receptor subunit NR2B regulates surface expression
    • Lavezzari G., et al. Differential binding of the AP-2 adaptor complex and PSD-95 to the C-terminus of the NMDA receptor subunit NR2B regulates surface expression. Neuropharmacology 45 (2003) 729-737
    • (2003) Neuropharmacology , vol.45 , pp. 729-737
    • Lavezzari, G.1
  • 49
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh D.M., et al. Naturally secreted oligomers of amyloid β protein potently inhibit hippocampal long-term potentiation in vivo. Nature 416 (2002) 535-539
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1
  • 50
    • 0344672942 scopus 로고    scopus 로고
    • APP processing and synaptic function
    • Kamenetz F., et al. APP processing and synaptic function. Neuron 37 (2003) 925-937
    • (2003) Neuron , vol.37 , pp. 925-937
    • Kamenetz, F.1
  • 51
    • 27144489060 scopus 로고    scopus 로고
    • Fyn kinase induces synaptic and cognitive impairments in a transgenic mouse model of Alzheimer's disease
    • Chin J., et al. Fyn kinase induces synaptic and cognitive impairments in a transgenic mouse model of Alzheimer's disease. J. Neurosci. 25 (2005) 9694-9703
    • (2005) J. Neurosci. , vol.25 , pp. 9694-9703
    • Chin, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.