메뉴 건너뛰기




Volumn 456, Issue 7224, 2008, Pages 904-909

Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; CELL ADHESION MOLECULE; CELL PROTEIN; CYTOSKELETON PROTEIN; GUANOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; MITOCHONDRIAL PROTEIN; MYELIN ASSOCIATED GLYCOPROTEIN; NEUROTRANSMITTER RECEPTOR; PALMITOYL PROTEIN; PROTEIN CDC42; RECEPTOR PROTEIN; SCAFFOLD PROTEIN; SNARE PROTEIN; UNCLASSIFIED DRUG;

EID: 57749183941     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature07605     Document Type: Review
Times cited : (459)

References (32)
  • 1
    • 25844522857 scopus 로고    scopus 로고
    • Modulation of neuronal protein trafficking and function by palmitoylation
    • Huang, K. & El-Husseini, A. Modulation of neuronal protein trafficking and function by palmitoylation. Curr. Opin. Neurobiol. 15, 527-535 (2005).
    • (2005) Curr. Opin. Neurobiol , vol.15 , pp. 527-535
    • Huang, K.1    El-Husseini, A.2
  • 2
    • 34247590130 scopus 로고    scopus 로고
    • Palmitoylation of ligands, receptors, and intracellular signaling molecules
    • Resh, M. D. Palmitoylation of ligands, receptors, and intracellular signaling molecules. Sci. STKE 2006, re14 (2006).
    • (2006) Sci. STKE , vol.2006
    • Resh, M.D.1
  • 3
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: Regulation and function
    • Smotrys, J. E. & Linder, M. E. Palmitoylation of intracellular signaling proteins: regulation and function. Annu. Rev. Biochem. 73, 559-587 (2004).
    • (2004) Annu. Rev. Biochem , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 4
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: Policing protein stability and traffic
    • Linder, M. E. & Deschenes, R. J. Palmitoylation: policing protein stability and traffic. Nature Rev. Mol. Cell Biol. 8, 74-84 (2007).
    • (2007) Nature Rev. Mol. Cell Biol , vol.8 , pp. 74-84
    • Linder, M.E.1    Deschenes, R.J.2
  • 5
    • 18344396972 scopus 로고    scopus 로고
    • Synaptic strength regulated by palmitate cycling on PSD-95
    • El-Husseini, A. E.-D. et al. Synaptic strength regulated by palmitate cycling on PSD-95. Cell 108, 849-863 (2002).
    • (2002) Cell , vol.108 , pp. 849-863
    • El-Husseini, A.E.-D.1
  • 6
    • 33646899047 scopus 로고    scopus 로고
    • Global analysis of protein palmitoylation in yeast
    • Roth, A. F. et al. Global analysis of protein palmitoylation in yeast. Cell 125, 1003-1013 (2006).
    • (2006) Cell , vol.125 , pp. 1003-1013
    • Roth, A.F.1
  • 7
    • 0842266659 scopus 로고    scopus 로고
    • Labeling and quantifying sites of protein palmitoylation
    • Drisdel, R. C. & Green, W. N. Labeling and quantifying sites of protein palmitoylation. Biotechniques 36, 276-285 (2004).
    • (2004) Biotechniques , vol.36 , pp. 276-285
    • Drisdel, R.C.1    Green, W.N.2
  • 8
    • 0033051101 scopus 로고    scopus 로고
    • Direct analysis of protein complexes using mass spectrometry
    • Link, A. J. et al. Direct analysis of protein complexes using mass spectrometry. Nature Biotechnol. 17, 676-682 (1999).
    • (1999) Nature Biotechnol , vol.17 , pp. 676-682
    • Link, A.J.1
  • 9
    • 3242731195 scopus 로고    scopus 로고
    • A model for random sampling and estimation of relative protein abundance in shotgun proteomics
    • Liu, H., Sadygov, R. G. & Yates, J. R. III. A model for random sampling and estimation of relative protein abundance in shotgun proteomics. Anal. Chem. 76, 4193-4201 (2004).
    • (2004) Anal. Chem , vol.76 , pp. 4193-4201
    • Liu, H.1    Sadygov, R.G.2    Yates III, J.R.3
  • 10
    • 34447115260 scopus 로고    scopus 로고
    • Palmitoylated proteins: Purification and identification
    • Wan, J. et al. Palmitoylated proteins: purification and identification. Nature Protoc. 2, 1573-1584 (2007).
    • (2007) Nature Protoc , vol.2 , pp. 1573-1584
    • Wan, J.1
  • 11
    • 23944433700 scopus 로고    scopus 로고
    • Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites
    • Hayashi, T., Rumbaugh, G. & Huganir, R. L. Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites. Neuron 47, 709-723 (2005).
    • (2005) Neuron , vol.47 , pp. 709-723
    • Hayashi, T.1    Rumbaugh, G.2    Huganir, R.L.3
  • 12
    • 33644858848 scopus 로고    scopus 로고
    • Role of numb in dendritic spine development with a Cdc42 GEF intersectin and EphB2
    • Nishimura, T. et al. Role of numb in dendritic spine development with a Cdc42 GEF intersectin and EphB2. Mol. Biol. Cell 17, 1273-1285 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1273-1285
    • Nishimura, T.1
  • 13
    • 18844443706 scopus 로고    scopus 로고
    • Rho family GTPases and dendrite plasticity
    • Negishi, M. & Katoh, H. Rho family GTPases and dendrite plasticity. Neuroscientist 11, 187-191 (2005).
    • (2005) Neuroscientist , vol.11 , pp. 187-191
    • Negishi, M.1    Katoh, H.2
  • 14
    • 19944433966 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphogenesis by insulin receptor substrate 53, a downstream effector of Rac1 and Cdc42 small GTPases
    • Choi, J. et al. Regulation of dendritic spine morphogenesis by insulin receptor substrate 53, a downstream effector of Rac1 and Cdc42 small GTPases. J. Neurosci. 25, 869-879 (2005).
    • (2005) J. Neurosci , vol.25 , pp. 869-879
    • Choi, J.1
  • 15
    • 0037884921 scopus 로고    scopus 로고
    • Small GTPase Cdc42 is required for multiple aspects of dendritic morphogenesis
    • Scott, E. K., Reuter, J. E. & Luo, L. Small GTPase Cdc42 is required for multiple aspects of dendritic morphogenesis. J. Neurosci. 23, 3118-3123 (2003).
    • (2003) J. Neurosci , vol.23 , pp. 3118-3123
    • Scott, E.K.1    Reuter, J.E.2    Luo, L.3
  • 16
    • 12444340440 scopus 로고    scopus 로고
    • p250GAP, a novel brain-enriched GTPase-activating protein for Rho family GTPases, is involved in the N-methyl-d-aspartate receptor signaling
    • Nakazawa, T. et al. p250GAP, a novel brain-enriched GTPase-activating protein for Rho family GTPases, is involved in the N-methyl-d-aspartate receptor signaling. Mol. Biol. Cell 14, 2921-2934 (2003).
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2921-2934
    • Nakazawa, T.1
  • 17
    • 0032143533 scopus 로고    scopus 로고
    • Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases
    • Wilson, A. L. et al. Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases. Biochem. J. 333, 497-504 (1998).
    • (1998) Biochem. J , vol.333 , pp. 497-504
    • Wilson, A.L.1
  • 18
    • 0030588593 scopus 로고    scopus 로고
    • Genomic organization and chromosomal location of murine Cdc42
    • Marks, P. W. & Kwiatkowski, D. J. Genomic organization and chromosomal location of murine Cdc42. Genomics 38, 13-18 (1996).
    • (1996) Genomics , vol.38 , pp. 13-18
    • Marks, P.W.1    Kwiatkowski, D.J.2
  • 19
    • 34547133773 scopus 로고    scopus 로고
    • The p21-activated kinase 3 implicated in mental retardation regulates spine morphogenesis through a Cdc42-dependent pathway
    • Kreis, P. et al. The p21-activated kinase 3 implicated in mental retardation regulates spine morphogenesis through a Cdc42-dependent pathway. J. Biol. Chem. 282, 21497-21506 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 21497-21506
    • Kreis, P.1
  • 20
    • 33845912667 scopus 로고    scopus 로고
    • Sequential implication of the mental retardation proteins ARHGEF6 and PAK3 in spine morphogenesis
    • Node-Langlois, R., Muller, D. & Boda, B. Sequential implication of the mental retardation proteins ARHGEF6 and PAK3 in spine morphogenesis. J. Cell Sci. 119, 4986-4993 (2006).
    • (2006) J. Cell Sci , vol.119 , pp. 4986-4993
    • Node-Langlois, R.1    Muller, D.2    Boda, B.3
  • 21
    • 47049098701 scopus 로고    scopus 로고
    • N-wasp and the arp2/3 complex are critical regulators of actin in the development of dendritic spines and synapses
    • Wegner, A. M. et al. N-wasp and the arp2/3 complex are critical regulators of actin in the development of dendritic spines and synapses. J. Biol. Chem. 283, 15912-15920 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 15912-15920
    • Wegner, A.M.1
  • 22
    • 18844403842 scopus 로고    scopus 로고
    • Molecular mechanisms of dendritic spine development and remodeling
    • Ethell, I. M. & Pasquale, E. B. Molecular mechanisms of dendritic spine development and remodeling. Prog. Neurobiol. 75, 161-205 (2005).
    • (2005) Prog. Neurobiol , vol.75 , pp. 161-205
    • Ethell, I.M.1    Pasquale, E.B.2
  • 23
    • 0037996880 scopus 로고    scopus 로고
    • Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability
    • Hering, H., Lin, C. C. & Sheng, M. Lipid rafts in the maintenance of synapses, dendritic spines, and surface AMPA receptor stability. J. Neurosci. 23, 3262-3271 (2003).
    • (2003) J. Neurosci , vol.23 , pp. 3262-3271
    • Hering, H.1    Lin, C.C.2    Sheng, M.3
  • 24
    • 0032078861 scopus 로고    scopus 로고
    • Rapid actin-based plasticity in dendritic spines
    • Fischer, M. et al. Rapid actin-based plasticity in dendritic spines. Neuron 20, 847-854 (1998).
    • (1998) Neuron , vol.20 , pp. 847-854
    • Fischer, M.1
  • 25
    • 0037374587 scopus 로고    scopus 로고
    • Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system
    • Ehlers, M. D. Activity level controls postsynaptic composition and signaling via the ubiquitin-proteasome system. Nature Neurosci. 6, 231-242 (2003).
    • (2003) Nature Neurosci , vol.6 , pp. 231-242
    • Ehlers, M.D.1
  • 26
    • 0033306744 scopus 로고    scopus 로고
    • Dendrites are more spiny on mature hippocampal neurons when synapses are inactivated
    • Kirov, S. A. & Harris, K. M. Dendrites are more spiny on mature hippocampal neurons when synapses are inactivated. Nature Neurosci. 2, 878-883 (1999).
    • (1999) Nature Neurosci , vol.2 , pp. 878-883
    • Kirov, S.A.1    Harris, K.M.2
  • 27
    • 0033366383 scopus 로고    scopus 로고
    • Miniature synaptic events maintain dendritic spines via AMPA receptor activation
    • McKinney, R. A. et al. Miniature synaptic events maintain dendritic spines via AMPA receptor activation. Nature Neurosci. 2, 44-49 (1999).
    • (1999) Nature Neurosci , vol.2 , pp. 44-49
    • McKinney, R.A.1
  • 28
    • 33646839766 scopus 로고    scopus 로고
    • Preconditioning doses of NMDA promote neuroprotection by enhancing neuronal excitability
    • Soriano, F. X. et al. Preconditioning doses of NMDA promote neuroprotection by enhancing neuronal excitability. J. Neurosci. 26, 4509-4518 (2006).
    • (2006) J. Neurosci , vol.26 , pp. 4509-4518
    • Soriano, F.X.1
  • 29
    • 0032403433 scopus 로고    scopus 로고
    • Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin
    • Halpain, S., Hipolito, A. & Saffer, L. Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin. J. Neurosci. 18, 9835-9844 (1998).
    • (1998) J. Neurosci , vol.18 , pp. 9835-9844
    • Halpain, S.1    Hipolito, A.2    Saffer, L.3
  • 30
    • 0347091260 scopus 로고    scopus 로고
    • BAK alters neuronal excitability and can switch from anti-to pro-death function during postnatal development
    • Fannjiang, Y. et al. BAK alters neuronal excitability and can switch from anti-to pro-death function during postnatal development. Dev. Cell 4, 575-585 (2003).
    • (2003) Dev. Cell , vol.4 , pp. 575-585
    • Fannjiang, Y.1
  • 31
    • 0035804765 scopus 로고    scopus 로고
    • Fragile X mice develop sensory hyperreactivity to auditory stimuli
    • Chen, L. & Toth, M. Fragile X mice develop sensory hyperreactivity to auditory stimuli. Neuroscience 103, 1043-1050 (2001).
    • (2001) Neuroscience , vol.103 , pp. 1043-1050
    • Chen, L.1    Toth, M.2
  • 32
    • 0029160305 scopus 로고
    • Acylation of adenylyl cyclase catalyst is important for enzymic activity
    • Mollner, S., Beck, K. & Pfeuffer, T. Acylation of adenylyl cyclase catalyst is important for enzymic activity. FEBS Lett. 371, 241-244 (1995).
    • (1995) FEBS Lett , vol.371 , pp. 241-244
    • Mollner, S.1    Beck, K.2    Pfeuffer, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.