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Volumn 36, Issue 24, 2016, Pages 6431-6444

Identification of PSD-95 depalmitoylating enzymes

Author keywords

ABHD protein; ABHD17; AMPA receptor; Palmitoylation; PSD 95; Synapse

Indexed keywords

AMPA RECEPTOR; POSTSYNAPTIC DENSITY PROTEIN 95; SCAFFOLD PROTEIN; ABHD2 PROTEIN, MOUSE; ACYLGLYCEROL LIPASE; DLGH4 PROTEIN, MOUSE; GUANYLATE KINASE; HYDROLASE; MEMBRANE PROTEIN; PALMITIC ACID DERIVATIVE; SERINE; SERINE HYDROXAMATE; SMALL INTERFERING RNA; TRITIUM;

EID: 84974814561     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.0419-16.2016     Document Type: Article
Times cited : (175)

References (41)
  • 2
    • 37149013708 scopus 로고    scopus 로고
    • A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol
    • Blankman JL, Simon GM, Cravatt BF (2007) A comprehensive profile of brain enzymes that hydrolyze the endocannabinoid 2-arachidonoylglycerol. Chem Biol 14:1347–1356.
    • (2007) Chem Biol , vol.14 , pp. 1347-1356
    • Blankman, J.L.1    Simon, G.M.2    Cravatt, B.F.3
  • 3
    • 84883244717 scopus 로고    scopus 로고
    • The PEG-switch assay: A fast semiquantitative method to determine protein reversible cysteine oxidation
    • Burgoyne JR, Oviosu O, Eaton P (2013) The PEG-switch assay: a fast semiquantitative method to determine protein reversible cysteine oxidation. J Pharmacol Toxicol Methods 68:297–301.
    • (2013) J Pharmacol Toxicol Methods , vol.68 , pp. 297-301
    • Burgoyne, J.R.1    Oviosu, O.2    Eaton, P.3
  • 4
    • 0027518208 scopus 로고
    • Purification and properties of a palmitoylprotein thioesterase that cleaves palmitate from H-Ras
    • Camp LA, Hofmann SL (1993) Purification and properties of a palmitoylprotein thioesterase that cleaves palmitate from H-Ras. J Biol Chem 268: 22566–22574.
    • (1993) J Biol Chem , vol.268 , pp. 22566-22574
    • Camp, L.A.1    Hofmann, S.L.2
  • 5
    • 84926624340 scopus 로고    scopus 로고
    • The physiology of protein S-acylation
    • Chamberlain LH, Shipston MJ (2015) The physiology of protein S-acylation. Physiol Rev 95:341–376.
    • (2015) Physiol Rev , vol.95 , pp. 341-376
    • Chamberlain, L.H.1    Shipston, M.J.2
  • 7
    • 84887002896 scopus 로고    scopus 로고
    • The dynamic synapse
    • Choquet D, Triller A (2013) The dynamic synapse. Neuron 80:691–703.
    • (2013) Neuron , vol.80 , pp. 691-703
    • Choquet, D.1    Triller, A.2
  • 8
    • 0033103971 scopus 로고    scopus 로고
    • Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs
    • Craven SE, El-Husseini AE, Bredt DS (1999) Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs. Neuron 22:497–509.
    • (1999) Neuron , vol.22 , pp. 497-509
    • Craven, S.E.1    El-Husseini, A.E.2    Bredt, D.S.3
  • 9
    • 0842266659 scopus 로고    scopus 로고
    • Labeling and quantifying sites of protein palmitoylation
    • Drisdel RC, Green WN (2004) Labeling and quantifying sites of protein palmitoylation. Biotechniques 36:276–285.
    • (2004) Biotechniques , vol.36 , pp. 276-285
    • Drisdel, R.C.1    Green, W.N.2
  • 10
    • 0032546946 scopus 로고    scopus 로고
    • A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein alpha subunits and p21(RAS)
    • Duncan JA, Gilman AG (1998) A cytoplasmic acyl-protein thioesterase that removes palmitate from G protein alpha subunits and p21(RAS). J Biol Chem 273:15830–15837.
    • (1998) J Biol Chem , vol.273 , pp. 15830-15837
    • Duncan, J.A.1    Gilman, A.G.2
  • 12
    • 0034627757 scopus 로고    scopus 로고
    • Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering
    • El-Husseini AE, Craven SE, Chetkovich DM, Firestein BL, Schnell E, Aoki C, Bredt DS (2000b) Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering. J Cell Biol 148:159–172.
    • (2000) J Cell Biol , vol.148 , pp. 159-172
    • El-Husseini, A.E.1    Craven, S.E.2    Chetkovich, D.M.3    Firestein, B.L.4    Schnell, E.5    Aoki, C.6    Bredt, D.S.7
  • 14
    • 34547115016 scopus 로고    scopus 로고
    • Synaptic trafficking of glutamate receptors by MAGUK scaffolding proteins
    • Elias GM, Nicoll RA (2007) Synaptic trafficking of glutamate receptors by MAGUK scaffolding proteins. Trends Cell Biol 17:343–352.
    • (2007) Trends Cell Biol , vol.17 , pp. 343-352
    • Elias, G.M.1    Nicoll, R.A.2
  • 15
    • 77249134163 scopus 로고    scopus 로고
    • Protein palmitoylation in neuronal development and synaptic plasticity
    • Fukata Y, Fukata M (2010) Protein palmitoylation in neuronal development and synaptic plasticity. Nat Rev Neurosci 11:161–175.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 161-175
    • Fukata, Y.1    Fukata, M.2
  • 17
    • 33748958810 scopus 로고    scopus 로고
    • Systematic screening for palmitoyl transferase activity of the DHHC protein family in mammalian cells
    • Fukata Y, Iwanaga T, Fukata M (2006) Systematic screening for palmitoyl transferase activity of the DHHC protein family in mammalian cells. Methods 40:177–182.
    • (2006) Methods , vol.40 , pp. 177-182
    • Fukata, Y.1    Iwanaga, T.2    Fukata, M.3
  • 19
    • 23944433700 scopus 로고    scopus 로고
    • Differential regulation of AMPAreceptor subunit trafficking by palmitoylation of two distinct sites
    • Hayashi T, Rumbaugh G, Huganir RL (2005) Differential regulation of AMPAreceptor subunit trafficking by palmitoylation of two distinct sites. Neuron 47:709–723.
    • (2005) Neuron , vol.47 , pp. 709-723
    • Hayashi, T.1    Rumbaugh, G.2    Huganir, R.L.3
  • 21
    • 84887009409 scopus 로고    scopus 로고
    • AMPARs and synaptic plasticity: The last 25 years
    • Huganir RL, Nicoll RA (2013) AMPARs and synaptic plasticity: the last 25 years. Neuron 80:704–717.
    • (2013) Neuron , vol.80 , pp. 704-717
    • Huganir, R.L.1    Nicoll, R.A.2
  • 24
    • 77951913551 scopus 로고    scopus 로고
    • Syntaxin-4 defines a domain for activity-dependent exocytosis in dendritic spines
    • Kennedy MJ, Davison IG, Robinson CG, Ehlers MD (2010) Syntaxin-4 defines a domain for activity-dependent exocytosis in dendritic spines. Cell 141:524–535.
    • (2010) Cell , vol.141 , pp. 524-535
    • Kennedy, M.J.1    Davison, I.G.2    Robinson, C.G.3    Ehlers, M.D.4
  • 25
    • 5044224260 scopus 로고    scopus 로고
    • PDZ domain proteins of synapses
    • Kim E, Sheng M (2004) PDZ domain proteins of synapses. Nat Rev Neurosci 5:771–781.
    • (2004) Nat Rev Neurosci , vol.5 , pp. 771-781
    • Kim, E.1    Sheng, M.2
  • 26
    • 0027529190 scopus 로고
    • Comparison of the acyl chain specificities of human myristoyl-CoA synthetase and human myristoyl-CoA:Protein N-myristoyltransferase
    • Kishore NS, Wood DC, Mehta PP, Wade AC, Lu T, Gokel GW, Gordon JI (1993) Comparison of the acyl chain specificities of human myristoyl-CoA synthetase and human myristoyl-CoA:protein N-myristoyltransferase. J Biol Chem 268:4889–4902.
    • (1993) J Biol Chem , vol.268 , pp. 4889-4902
    • Kishore, N.S.1    Wood, D.C.2    Mehta, P.P.3    Wade, A.C.4    Lu, T.5    Gokel, G.W.6    Gordon, J.I.7
  • 27
    • 84956877118 scopus 로고    scopus 로고
    • ABHD17 proteins are novel protein depalmitoylases that regulate N-Ras palmitate turnover and subcellular localization
    • Lin DT, Conibear E (2015) ABHD17 proteins are novel protein depalmitoylases that regulate N-Ras palmitate turnover and subcellular localization. eLife 4:e11306.
    • (2015) Elife , vol.4
    • Lin, D.T.1    Conibear, E.2
  • 28
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: Policing protein stability and traffic
    • Linder ME, Deschenes RJ (2007) Palmitoylation: policing protein stability and traffic. Nat Rev Mol Cell Biol 8:74–84.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 74-84
    • Linder, M.E.1    Deschenes, R.J.2
  • 29
    • 84873700102 scopus 로고    scopus 로고
    • Mammalian alpha beta hydrolase domain (ABHD) proteins: Lipid metabolizing enzymes at the interface of cell signaling and energy metabolism
    • Lord CC, Thomas G, Brown JM (2013) Mammalian alpha beta hydrolase domain (ABHD) proteins: lipid metabolizing enzymes at the interface of cell signaling and energy metabolism. Biochim Biophys Acta 1831: 792–802.
    • (2013) Biochim Biophys Acta , vol.1831 , pp. 792-802
    • Lord, C.C.1    Thomas, G.2    Brown, J.M.3
  • 30
    • 0035662634 scopus 로고    scopus 로고
    • Development of a sensitive assay to detect reversibly oxidized protein cysteine sulfhydryl groups
    • Makmura L, Hamann M, Areopagita A, Furuta S, Muñoz A, Momand J (2001) Development of a sensitive assay to detect reversibly oxidized protein cysteine sulfhydryl groups. Antioxid Redox Signal 3:1105–1118.
    • (2001) Antioxid Redox Signal , vol.3 , pp. 1105-1118
    • Makmura, L.1    Hamann, M.2    Areopagita, A.3    Furuta, S.4    Momand, A.J.5
  • 32
    • 78650516076 scopus 로고    scopus 로고
    • Post-translational myristoylation: Fat matters in cellular life and death
    • Martin DD, Beauchamp E, Berthiaume LG (2011) Post-translational myristoylation: Fat matters in cellular life and death. Biochimie 93:18–31.
    • (2011) Biochimie , vol.93 , pp. 18-31
    • Martin, D.D.1    Beauchamp, E.2    Berthiaume, L.G.3
  • 33
    • 78649662343 scopus 로고    scopus 로고
    • Mutational analysis of Saccharomyces cerevisiae Erf2 reveals a two-step reaction mechanism for protein palmitoylation by DHHC enzymes
    • Mitchell DA, Mitchell G, Ling Y, Budde C, Deschenes RJ (2010) Mutational analysis of Saccharomyces cerevisiae Erf2 reveals a two-step reaction mechanism for protein palmitoylation by DHHC enzymes. J Biol Chem 285: 38104–38114.
    • (2010) J Biol Chem , vol.285 , pp. 38104-38114
    • Mitchell, D.A.1    Mitchell, G.2    Ling, Y.3    Budde, C.4    Deschenes, R.J.5
  • 34
    • 84859910414 scopus 로고    scopus 로고
    • A novel and conserved protein AHO-3 is required for thermotactic plasticity associated with feeding states in Caenorhabditis elegans
    • Nishio N, Mohri-Shiomi A, Nishida Y, Hiramatsu N, Kodama-Namba E, Kimura KD, Kuhara A, Mori I (2012) A novel and conserved protein AHO-3 is required for thermotactic plasticity associated with feeding states in Caenorhabditis elegans. Genes Cells 17:365–386.
    • (2012) Genes Cells , vol.17 , pp. 365-386
    • Nishio, N.1    Mohri-Shiomi, A.2    Nishida, Y.3    Hiramatsu, N.4    Kodama-Namba, E.5    Kimura, K.D.6    Kuhara, A.7    Mori, I.8
  • 37
    • 77955865876 scopus 로고    scopus 로고
    • Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags
    • Rexach JE, Rogers CJ, Yu SH, Tao J, Sun YE, Hsieh-Wilson LC (2010) Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags. Nat Chem Biol 6:645–651.
    • (2010) Nat Chem Biol , vol.6 , pp. 645-651
    • Rexach, J.E.1    Rogers, C.J.2    Yu, S.H.3    Tao, J.4    Sun, Y.E.5    Hsieh-Wilson, L.C.6
  • 40
    • 0032730857 scopus 로고    scopus 로고
    • Depalmitoylation of endothelial nitric-oxide synthase by acyl-protein thioesterase 1 is potentiated by Ca2-calmodulin
    • Yeh DC, Duncan JA, Yamashita S, Michel T (1999) Depalmitoylation of endothelial nitric-oxide synthase by acyl-protein thioesterase 1 is potentiated by Ca2-calmodulin. J Biol Chem 274:33148–33154.
    • (1999) J Biol Chem , vol.274 , pp. 33148-33154
    • Yeh, D.C.1    Duncan, J.A.2    Yamashita, S.3    Michel, T.4
  • 41
    • 84962128761 scopus 로고    scopus 로고
    • Mechanistic basis of MAGUK-organized complexes in synaptic development and signalling
    • Zhu J, Shang Y, Zhang M (2016) Mechanistic basis of MAGUK-organized complexes in synaptic development and signalling. Nat Rev Neurosci 17:209–223.
    • (2016) Nat Rev Neurosci , vol.17 , pp. 209-223
    • Zhu, J.1    Shang, Y.2    Zhang, M.3


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