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Volumn 77, Issue , 2016, Pages 97-141

Local Palmitoylation Cycles and Specialized Membrane Domain Organization

Author keywords

Acylation; Depalmitoylation; DHHC ZDHHC protein; Membrane domain; Microdomain; Nanodomain; Palmitoylation; PSD; PSD 95; Synapse

Indexed keywords

PROTEIN;

EID: 84961789517     PISSN: 10635823     EISSN: None     Source Type: Book Series    
DOI: 10.1016/bs.ctm.2015.10.003     Document Type: Article
Times cited : (56)

References (174)
  • 3
    • 80053186768 scopus 로고    scopus 로고
    • Plasma membrane association of p63 Rho guanine nucleotide exchange factor (p63RhoGEF) is mediated by palmitoylation and is required for basal activity in cells
    • Aittaleb, M., Nishimura, A., Linder, M.E., Tesmer, J.J., Plasma membrane association of p63 Rho guanine nucleotide exchange factor (p63RhoGEF) is mediated by palmitoylation and is required for basal activity in cells. The Journal of Biological Chemistry 286 (2011), 34448–34456.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 34448-34456
    • Aittaleb, M.1    Nishimura, A.2    Linder, M.E.3    Tesmer, J.J.4
  • 4
    • 84863930969 scopus 로고    scopus 로고
    • The Drosophila protein palmitoylome: characterizing palmitoyl-thioesterases and DHHC palmitoyl-transferases
    • Bannan, B.A., Van Etten, J., Kohler, J.A., Tsoi, Y., Hansen, N.M., Sigmon, S., et al. The Drosophila protein palmitoylome: characterizing palmitoyl-thioesterases and DHHC palmitoyl-transferases. Fly (Austin) 2 (2008), 198–214.
    • (2008) Fly (Austin) , vol.2 , pp. 198-214
    • Bannan, B.A.1    Van Etten, J.2    Kohler, J.A.3    Tsoi, Y.4    Hansen, N.M.5    Sigmon, S.6
  • 5
    • 0032883098 scopus 로고    scopus 로고
    • Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae
    • Bartels, D.J., Mitchell, D.A., Dong, X., Deschenes, R.J., Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae. Molecular and Cellular Biology 19 (1999), 6775–6787.
    • (1999) Molecular and Cellular Biology , vol.19 , pp. 6775-6787
    • Bartels, D.J.1    Mitchell, D.A.2    Dong, X.3    Deschenes, R.J.4
  • 6
    • 84868324295 scopus 로고    scopus 로고
    • Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S-acyltransferase protein family
    • Batistic, O., Genomics and localization of the Arabidopsis DHHC-cysteine-rich domain S-acyltransferase protein family. Plant Physiology 160 (2012), 1597–1612.
    • (2012) Plant Physiology , vol.160 , pp. 1597-1612
    • Batistic, O.1
  • 7
    • 38049048081 scopus 로고    scopus 로고
    • Organizing the fluid membrane bilayer: diseases linked to spectrin and ankyrin
    • Bennett, V., Healy, J., Organizing the fluid membrane bilayer: diseases linked to spectrin and ankyrin. Trends in Molecular Medicine 14 (2008), 28–36.
    • (2008) Trends in Molecular Medicine , vol.14 , pp. 28-36
    • Bennett, V.1    Healy, J.2
  • 8
    • 84887196254 scopus 로고    scopus 로고
    • Spectrin- and ankyrin-based membrane domains and the evolution of vertebrates
    • Bennett, V., Lorenzo, D.N., Spectrin- and ankyrin-based membrane domains and the evolution of vertebrates. Current Topics in Membranes 72 (2013), 1–37.
    • (2013) Current Topics in Membranes , vol.72 , pp. 1-37
    • Bennett, V.1    Lorenzo, D.N.2
  • 9
    • 84880474167 scopus 로고    scopus 로고
    • Palmitoylation of amyloid precursor protein regulates amyloidogenic processing in lipid rafts
    • Bhattacharyya, R., Barren, C., Kovacs, D.M., Palmitoylation of amyloid precursor protein regulates amyloidogenic processing in lipid rafts. The Journal of Neuroscience 33 (2013), 11169–11183.
    • (2013) The Journal of Neuroscience , vol.33 , pp. 11169-11183
    • Bhattacharyya, R.1    Barren, C.2    Kovacs, D.M.3
  • 10
    • 0035968261 scopus 로고    scopus 로고
    • Palmitoylation of CCR5 is critical for receptor trafficking and efficient activation of intracellular signaling pathways
    • Blanpain, C., Wittamer, V., Vanderwinden, J.M., Boom, A., Renneboog, B., Lee, B., et al. Palmitoylation of CCR5 is critical for receptor trafficking and efficient activation of intracellular signaling pathways. The Journal of Biological Chemistry 276 (2001), 23795–23804.
    • (2001) The Journal of Biological Chemistry , vol.276 , pp. 23795-23804
    • Blanpain, C.1    Wittamer, V.2    Vanderwinden, J.M.3    Boom, A.4    Renneboog, B.5    Lee, B.6
  • 11
    • 84878758131 scopus 로고    scopus 로고
    • What does S-palmitoylation do to membrane proteins?
    • Blaskovic, S., Blanc, M., van der Goot, F.G., What does S-palmitoylation do to membrane proteins?. FEBS Journal 280 (2013), 2766–2774.
    • (2013) FEBS Journal , vol.280 , pp. 2766-2774
    • Blaskovic, S.1    Blanc, M.2    van der Goot, F.G.3
  • 13
    • 77949716057 scopus 로고    scopus 로고
    • Joubert syndrome Arl13b functions at ciliary membranes and stabilizes protein transport in Caenorhabditis elegans
    • Cevik, S., Hori, Y., Kaplan, O.I., Kida, K., Toivenon, T., Foley-Fisher, C., et al. Joubert syndrome Arl13b functions at ciliary membranes and stabilizes protein transport in Caenorhabditis elegans. The Journal of Cell Biology 188 (2010), 953–969.
    • (2010) The Journal of Cell Biology , vol.188 , pp. 953-969
    • Cevik, S.1    Hori, Y.2    Kaplan, O.I.3    Kida, K.4    Toivenon, T.5    Foley-Fisher, C.6
  • 16
    • 77954475177 scopus 로고    scopus 로고
    • Interplay of palmitoylation and phosphorylation in the trafficking and localization of phosphodiesterase 10A: implications for the treatment of schizophrenia
    • Charych, E.I., Jiang, L.X., Lo, F., Sullivan, K., Brandon, N.J., Interplay of palmitoylation and phosphorylation in the trafficking and localization of phosphodiesterase 10A: implications for the treatment of schizophrenia. The Journal of Neuroscience 30 (2010), 9027–9037.
    • (2010) The Journal of Neuroscience , vol.30 , pp. 9027-9037
    • Charych, E.I.1    Jiang, L.X.2    Lo, F.3    Sullivan, K.4    Brandon, N.J.5
  • 18
    • 34548216374 scopus 로고    scopus 로고
    • Shuttling of G protein subunits between the plasma membrane and intracellular membranes
    • Chisari, M., Saini, D.K., Kalyanaraman, V., Gautam, N., Shuttling of G protein subunits between the plasma membrane and intracellular membranes. The Journal of Biological Chemistry 282 (2007), 24092–24098.
    • (2007) The Journal of Biological Chemistry , vol.282 , pp. 24092-24098
    • Chisari, M.1    Saini, D.K.2    Kalyanaraman, V.3    Gautam, N.4
  • 19
    • 79953193710 scopus 로고    scopus 로고
    • Flotillin-1 is essential for PKC-triggered endocytosis and membrane microdomain localization of DAT
    • Cremona, M.L., Matthies, H.J., Pau, K., Bowton, E., Speed, N., Lute, B.J., et al. Flotillin-1 is essential for PKC-triggered endocytosis and membrane microdomain localization of DAT. Nature Neuroscience 14 (2011), 469–477.
    • (2011) Nature Neuroscience , vol.14 , pp. 469-477
    • Cremona, M.L.1    Matthies, H.J.2    Pau, K.3    Bowton, E.4    Speed, N.5    Lute, B.J.6
  • 22
    • 84905393016 scopus 로고    scopus 로고
    • Palmitoylation of gephyrin controls receptor clustering and plasticity of GABAergic synapses
    • Dejanovic, B., Semtner, M., Ebert, S., Lamkemeyer, T., Neuser, F., Luscher, B., et al. Palmitoylation of gephyrin controls receptor clustering and plasticity of GABAergic synapses. PLoS Biology, 12, 2014, e1001908.
    • (2014) PLoS Biology , vol.12 , pp. e1001908
    • Dejanovic, B.1    Semtner, M.2    Ebert, S.3    Lamkemeyer, T.4    Neuser, F.5    Luscher, B.6
  • 25
    • 0028920139 scopus 로고
    • Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae
    • Dietzen, D.J., Hastings, W.R., Lublin, D.M., Caveolin is palmitoylated on multiple cysteine residues. Palmitoylation is not necessary for localization of caveolin to caveolae. The Journal of Biological Chemistry 270 (1995), 6838–6842.
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 6838-6842
    • Dietzen, D.J.1    Hastings, W.R.2    Lublin, D.M.3
  • 26
    • 80053351683 scopus 로고    scopus 로고
    • Proteomic analysis of palmitoylated platelet proteins
    • Dowal, L., Yang, W., Freeman, M.R., Steen, H., Flaumenhaft, R., Proteomic analysis of palmitoylated platelet proteins. Blood 118 (2011), e62–73.
    • (2011) Blood , vol.118 , pp. e62-73
    • Dowal, L.1    Yang, W.2    Freeman, M.R.3    Steen, H.4    Flaumenhaft, R.5
  • 27
    • 22344431893 scopus 로고    scopus 로고
    • Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family
    • Drenan, R.M., Doupnik, C.A., Boyle, M.P., Muglia, L.J., Huettner, J.E., Linder, M.E., et al. Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family. The Journal of Cell Biology 169 (2005), 623–633.
    • (2005) The Journal of Cell Biology , vol.169 , pp. 623-633
    • Drenan, R.M.1    Doupnik, C.A.2    Boyle, M.P.3    Muglia, L.J.4    Huettner, J.E.5    Linder, M.E.6
  • 28
    • 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 (2004), 276–285.
    • (2004) Biotechniques , vol.36 , pp. 276-285
    • Drisdel, R.C.1    Green, W.N.2
  • 29
    • 0033603315 scopus 로고    scopus 로고
    • Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling
    • Druey, K.M., Ugur, O., Caron, J.M., Chen, C.K., Backlund, P.S., Jones, T.L., Amino-terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling. The Journal of Biological Chemistry 274 (1999), 18836–18842.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 18836-18842
    • Druey, K.M.1    Ugur, O.2    Caron, J.M.3    Chen, C.K.4    Backlund, P.S.5    Jones, T.L.6
  • 30
    • 84907969440 scopus 로고    scopus 로고
    • A systematic analysis of protein palmitoylation in Caenorhabditis elegans
    • Edmonds, M.J., Morgan, A., A systematic analysis of protein palmitoylation in Caenorhabditis elegans. BMC Genomics, 15, 2014, 841.
    • (2014) BMC Genomics , vol.15 , pp. 841
    • Edmonds, M.J.1    Morgan, A.2
  • 31
    • 0036779578 scopus 로고    scopus 로고
    • Protein palmitoylation: a regulator of neuronal development and function
    • El-Husseini Ael, D., Bredt, D.S., Protein palmitoylation: a regulator of neuronal development and function. Nature Reviews Neuroscience 3 (2002), 791–802.
    • (2002) Nature Reviews Neuroscience , vol.3 , pp. 791-802
    • El-Husseini Ael, D.1    Bredt, D.S.2
  • 34
    • 66949128729 scopus 로고    scopus 로고
    • Identification of a palmitoyl acyltransferase required for protein sorting to the flagellar membrane
    • Emmer, B.T., Souther, C., Toriello, K.M., Olson, C.L., Epting, C.L., Engman, D.M., Identification of a palmitoyl acyltransferase required for protein sorting to the flagellar membrane. Journal of Cell Science 122 (2009), 867–874.
    • (2009) Journal of Cell Science , vol.122 , pp. 867-874
    • Emmer, B.T.1    Souther, C.2    Toriello, K.M.3    Olson, C.L.4    Epting, C.L.5    Engman, D.M.6
  • 36
    • 79953132315 scopus 로고    scopus 로고
    • Palmitoylation controls dopamine transporter kinetics, degradation, and protein kinase C-dependent regulation
    • Foster, J.D., Vaughan, R.A., Palmitoylation controls dopamine transporter kinetics, degradation, and protein kinase C-dependent regulation. The Journal of Biological Chemistry 286 (2011), 5175–5186.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 5175-5186
    • Foster, J.D.1    Vaughan, R.A.2
  • 39
    • 84880136469 scopus 로고    scopus 로고
    • Global analysis of apicomplexan protein S-acyl transferases reveals an enzyme essential for invasion
    • Frenal, K., Tay, C.L., Mueller, C., Bushell, E.S., Jia, Y., Graindorge, A., et al. Global analysis of apicomplexan protein S-acyl transferases reveals an enzyme essential for invasion. Traffic 14 (2013), 895–911.
    • (2013) Traffic , vol.14 , pp. 895-911
    • Frenal, K.1    Tay, C.L.2    Mueller, C.3    Bushell, E.S.4    Jia, Y.5    Graindorge, A.6
  • 40
    • 84896772057 scopus 로고    scopus 로고
    • S-palmitoylation represents a novel mechanism regulating the mitochondrial targeting of BAX and initiation of apoptosis
    • Frohlich, M., Dejanovic, B., Kashkar, H., Schwarz, G., Nussberger, S., S-palmitoylation represents a novel mechanism regulating the mitochondrial targeting of BAX and initiation of apoptosis. Cell Death and Disease, 5, 2014, e1057.
    • (2014) Cell Death and Disease , vol.5 , pp. e1057
    • Frohlich, M.1    Dejanovic, B.2    Kashkar, H.3    Schwarz, G.4    Nussberger, S.5
  • 42
    • 77249134163 scopus 로고    scopus 로고
    • Protein palmitoylation in neuronal development and synaptic plasticity
    • Fukata, Y., Fukata, M., Protein palmitoylation in neuronal development and synaptic plasticity. Nature Reviews Neuroscience 11 (2010), 161–175.
    • (2010) Nature Reviews Neuroscience , vol.11 , pp. 161-175
    • Fukata, Y.1    Fukata, M.2
  • 44
    • 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., Systematic screening for palmitoyl transferase activity of the DHHC protein family in mammalian cells. Methods 40 (2006), 177–182.
    • (2006) Methods , vol.40 , pp. 177-182
    • Fukata, Y.1    Iwanaga, T.2    Fukata, M.3
  • 45
    • 84897053323 scopus 로고    scopus 로고
    • Method for cellular imaging of palmitoylated proteins with clickable probes and proximity ligation applied to Hedgehog, tubulin, and Ras
    • Gao, X., Hannoush, R.N., Method for cellular imaging of palmitoylated proteins with clickable probes and proximity ligation applied to Hedgehog, tubulin, and Ras. Journal of the American Chemical Society 136 (2014), 4544–4550.
    • (2014) Journal of the American Chemical Society , vol.136 , pp. 4544-4550
    • Gao, X.1    Hannoush, R.N.2
  • 46
    • 84890978108 scopus 로고    scopus 로고
    • Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine
    • Gao, X., Hannoush, R.N., Single-cell imaging of Wnt palmitoylation by the acyltransferase porcupine. Nature Chemical Biology 10 (2014), 61–68.
    • (2014) Nature Chemical Biology , vol.10 , pp. 61-68
    • Gao, X.1    Hannoush, R.N.2
  • 47
    • 0033198917 scopus 로고    scopus 로고
    • 1 adenosine receptor: enhanced proteolysis of palmitoylation-deficient mutant receptors
    • 1 adenosine receptor: enhanced proteolysis of palmitoylation-deficient mutant receptors. Biochemical Journal 342 (1999), 387–395.
    • (1999) Biochemical Journal , vol.342 , pp. 387-395
    • Gao, Z.1    Ni, Y.2    Szabo, G.3    Linden, J.4
  • 48
    • 84928143324 scopus 로고    scopus 로고
    • Palmitoylation of LIM Kinase-1 ensures spine-specific actin polymerization and morphological plasticity
    • George, J., Soares, C., Montersino, A., Beique, J.C., Thomas, G.M., Palmitoylation of LIM Kinase-1 ensures spine-specific actin polymerization and morphological plasticity. eLife, 4, 2015, e06327.
    • (2015) eLife , vol.4 , pp. e06327
    • George, J.1    Soares, C.2    Montersino, A.3    Beique, J.C.4    Thomas, G.M.5
  • 49
    • 33749185252 scopus 로고    scopus 로고
    • Analysis of ProDH, COMT and ZDHHC8 risk variants does not support individual or interactive effects on schizophrenia susceptibility
    • Glaser, B., Moskvina, V., Kirov, G., Murphy, K.C., Williams, H., Williams, N., et al. Analysis of ProDH, COMT and ZDHHC8 risk variants does not support individual or interactive effects on schizophrenia susceptibility. Schizophrenia Research 87 (2006), 21–27.
    • (2006) Schizophrenia Research , vol.87 , pp. 21-27
    • Glaser, B.1    Moskvina, V.2    Kirov, G.3    Murphy, K.C.4    Williams, H.5    Williams, N.6
  • 50
  • 51
    • 79957617680 scopus 로고    scopus 로고
    • The palmitoyl transferase DHHC2 targets a dynamic membrane cycling pathway: regulation by a C-terminal domain
    • Greaves, J., Carmichael, J.A., Chamberlain, L.H., The palmitoyl transferase DHHC2 targets a dynamic membrane cycling pathway: regulation by a C-terminal domain. Molecular Biology of the Cell 22 (2011), 1887–1895.
    • (2011) Molecular Biology of the Cell , vol.22 , pp. 1887-1895
    • Greaves, J.1    Carmichael, J.A.2    Chamberlain, L.H.3
  • 52
    • 79955649200 scopus 로고    scopus 로고
    • DHHC palmitoyl transferases: substrate interactions and (patho)physiology
    • Greaves, J., Chamberlain, L.H., DHHC palmitoyl transferases: substrate interactions and (patho)physiology. Trends in Biochemical Sciences 36 (2011), 245–253.
    • (2011) Trends in Biochemical Sciences , vol.36 , pp. 245-253
    • Greaves, J.1    Chamberlain, L.H.2
  • 54
    • 67650803380 scopus 로고    scopus 로고
    • Imaging the lipidome: omega-alkynyl fatty acids for detection and cellular visualization of lipid-modified proteins
    • Hannoush, R.N., Arenas-Ramirez, N., Imaging the lipidome: omega-alkynyl fatty acids for detection and cellular visualization of lipid-modified proteins. ACS Chemical Biology 4 (2009), 581–587.
    • (2009) ACS Chemical Biology , vol.4 , pp. 581-587
    • Hannoush, R.N.1    Arenas-Ramirez, N.2
  • 55
    • 77953773167 scopus 로고    scopus 로고
    • The chemical toolbox for monitoring protein fatty acylation and prenylation
    • Hannoush, R.N., Sun, J., The chemical toolbox for monitoring protein fatty acylation and prenylation. Nature Chemical Biology 6 (2010), 498–506.
    • (2010) Nature Chemical Biology , vol.6 , pp. 498-506
    • Hannoush, R.N.1    Sun, J.2
  • 56
    • 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 (2005), 709–723.
    • (2005) Neuron , vol.47 , pp. 709-723
    • Hayashi, T.1    Rumbaugh, G.2    Huganir, R.L.3
  • 57
    • 70350207200 scopus 로고    scopus 로고
    • Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking
    • Hayashi, T., Thomas, G.M., Huganir, R.L., Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking. Neuron 64 (2009), 213–226.
    • (2009) Neuron , vol.64 , pp. 213-226
    • Hayashi, T.1    Thomas, G.M.2    Huganir, R.L.3
  • 58
    • 84904645592 scopus 로고    scopus 로고
    • Ankyrin-G palmitoylation and betaII-spectrin binding to phosphoinositide lipids drive lateral membrane assembly
    • He, M., Abdi, K.M., Bennett, V., Ankyrin-G palmitoylation and betaII-spectrin binding to phosphoinositide lipids drive lateral membrane assembly. The Journal of Cell Biology 206 (2014), 273–288.
    • (2014) The Journal of Cell Biology , vol.206 , pp. 273-288
    • He, M.1    Abdi, K.M.2    Bennett, V.3
  • 59
    • 84871565497 scopus 로고    scopus 로고
    • Cysteine 70 of ankyrin-G is S-palmitoylated and is required for function of ankyrin-G in membrane domain assembly
    • He, M., Jenkins, P., Bennett, V., Cysteine 70 of ankyrin-G is S-palmitoylated and is required for function of ankyrin-G in membrane domain assembly. The Journal of Biological Chemistry 287 (2012), 43995–44005.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 43995-44005
    • He, M.1    Jenkins, P.2    Bennett, V.3
  • 60
    • 44649139158 scopus 로고    scopus 로고
    • Multiple roles for protein palmitoylation in plants
    • Hemsley, P.A., Grierson, C.S., Multiple roles for protein palmitoylation in plants. Trends in Plant Science 13 (2008), 295–302.
    • (2008) Trends in Plant Science , vol.13 , pp. 295-302
    • Hemsley, P.A.1    Grierson, C.S.2
  • 61
    • 30844460508 scopus 로고    scopus 로고
    • The TIP GROWTH DEFECTIVE1 S-acyl transferase regulates plant cell growth in Arabidopsis
    • Hemsley, P.A., Kemp, A.C., Grierson, C.S., The TIP GROWTH DEFECTIVE1 S-acyl transferase regulates plant cell growth in Arabidopsis. Plant Cell 17 (2005), 2554–2563.
    • (2005) Plant Cell , vol.17 , pp. 2554-2563
    • Hemsley, P.A.1    Kemp, A.C.2    Grierson, C.S.3
  • 62
    • 84872144570 scopus 로고    scopus 로고
    • A proteomic approach identifies many novel palmitoylated proteins in Arabidopsis
    • Hemsley, P.A., Weimar, T., Lilley, K.S., Dupree, P., Grierson, C.S., A proteomic approach identifies many novel palmitoylated proteins in Arabidopsis. New Phytologist 197 (2013), 805–814.
    • (2013) New Phytologist , vol.197 , pp. 805-814
    • Hemsley, P.A.1    Weimar, T.2    Lilley, K.S.3    Dupree, P.4    Grierson, C.S.5
  • 63
    • 67649882018 scopus 로고    scopus 로고
    • Analysis of DHHC acyltransferases implies overlapping substrate specificity and a two-step reaction mechanism
    • Hou, H., John Peter, A.T., Meiringer, C., Subramanian, K., Ungermann, C., Analysis of DHHC acyltransferases implies overlapping substrate specificity and a two-step reaction mechanism. Traffic 10 (2009), 1061–1073.
    • (2009) Traffic , vol.10 , pp. 1061-1073
    • Hou, H.1    John Peter, A.T.2    Meiringer, C.3    Subramanian, K.4    Ungermann, C.5
  • 65
    • 68849113445 scopus 로고    scopus 로고
    • Neuronal palmitoyl acyl transferases exhibit distinct substrate specificity
    • Huang, K., Sanders, S., Singaraja, R., Orban, P., Cijsouw, T., Arstikaitis, P., et al. Neuronal palmitoyl acyl transferases exhibit distinct substrate specificity. FASEB Journal 23 (2009), 2605–2615.
    • (2009) FASEB Journal , vol.23 , pp. 2605-2615
    • Huang, K.1    Sanders, S.2    Singaraja, R.3    Orban, P.4    Cijsouw, T.5    Arstikaitis, P.6
  • 66
    • 4544246530 scopus 로고    scopus 로고
    • Deletion of the neuron-specific protein delta-catenin leads to severe cognitive and synaptic dysfunction
    • Israely, I., Costa, R.M., Xie, C.W., Silva, A.J., Kosik, K.S., Liu, X., Deletion of the neuron-specific protein delta-catenin leads to severe cognitive and synaptic dysfunction. Current Biology 14 (2004), 1657–1663.
    • (2004) Current Biology , vol.14 , pp. 1657-1663
    • Israely, I.1    Costa, R.M.2    Xie, C.W.3    Silva, A.J.4    Kosik, K.S.5    Liu, X.6
  • 67
    • 84861212051 scopus 로고    scopus 로고
    • Proteomic analysis of S-acylated proteins in human B cells reveals palmitoylation of the immune regulators CD20 and CD23
    • Ivaldi, C., Martin, B.R., Kieffer-Jaquinod, S., Chapel, A., Levade, T., Garin, J., et al. Proteomic analysis of S-acylated proteins in human B cells reveals palmitoylation of the immune regulators CD20 and CD23. PLoS One, 7, 2012, e37187.
    • (2012) PLoS One , vol.7 , pp. e37187
    • Ivaldi, C.1    Martin, B.R.2    Kieffer-Jaquinod, S.3    Chapel, A.4    Levade, T.5    Garin, J.6
  • 68
    • 84855494963 scopus 로고    scopus 로고
    • An electrostatic switch controls palmitoylation of the large conductance voltage- and calcium-activated potassium (BK) channel
    • Jeffries, O., Tian, L., McClafferty, H., Shipston, M.J., An electrostatic switch controls palmitoylation of the large conductance voltage- and calcium-activated potassium (BK) channel. The Journal of Biological Chemistry 287 (2012), 1468–1477.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 1468-1477
    • Jeffries, O.1    Tian, L.2    McClafferty, H.3    Shipston, M.J.4
  • 69
    • 84857737571 scopus 로고    scopus 로고
    • DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities
    • Jennings, B.C., Linder, M.E., DHHC protein S-acyltransferases use similar ping-pong kinetic mechanisms but display different acyl-CoA specificities. The Journal of Biological Chemistry 287 (2012), 7236–7245.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 7236-7245
    • Jennings, B.C.1    Linder, M.E.2
  • 70
    • 84896847417 scopus 로고    scopus 로고
    • A mechanism regulating G protein-coupled receptor signaling that requires cycles of protein palmitoylation and depalmitoylation
    • Jia, L., Chisari, M., Maktabi, M.H., Sobieski, C., Zhou, H., Konopko, A.M., et al. A mechanism regulating G protein-coupled receptor signaling that requires cycles of protein palmitoylation and depalmitoylation. The Journal of Biological Chemistry 289 (2014), 6249–6257.
    • (2014) The Journal of Biological Chemistry , vol.289 , pp. 6249-6257
    • Jia, L.1    Chisari, M.2    Maktabi, M.H.3    Sobieski, C.4    Zhou, H.5    Konopko, A.M.6
  • 71
    • 84865125774 scopus 로고    scopus 로고
    • Analysis of protein palmitoylation reveals a pervasive role in Plasmodium development and pathogenesis
    • Jones, M.L., Collins, M.O., Goulding, D., Choudhary, J.S., Rayner, J.C., Analysis of protein palmitoylation reveals a pervasive role in Plasmodium development and pathogenesis. Cell Host and Microbe 12 (2012), 246–258.
    • (2012) Cell Host and Microbe , vol.12 , pp. 246-258
    • Jones, M.L.1    Collins, M.O.2    Goulding, D.3    Choudhary, J.S.4    Rayner, J.C.5
  • 72
    • 0029147830 scopus 로고
    • Conformations of peptides corresponding to fatty acylation sites in proteins. A circular dichroism study
    • Joseph, M., Nagaraj, R., Conformations of peptides corresponding to fatty acylation sites in proteins. A circular dichroism study. The Journal of Biological Chemistry 270 (1995), 19439–19445.
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 19439-19445
    • Joseph, M.1    Nagaraj, R.2
  • 73
    • 57749183941 scopus 로고    scopus 로고
    • Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation
    • Kang, R., Wan, J., Arstikaitis, P., Takahashi, H., Huang, K., Bailey, A.O., et al. Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation. Nature 456 (2008), 904–909.
    • (2008) Nature , vol.456 , pp. 904-909
    • Kang, R.1    Wan, J.2    Arstikaitis, P.3    Takahashi, H.4    Huang, K.5    Bailey, A.O.6
  • 75
    • 84961290390 scopus 로고    scopus 로고
    • Advances in Phos-tag-based methodologies for separation and detection of the phosphoproteome
    • Kinoshita, E., Kinoshita-Kikuta, E., Koike, T., Advances in Phos-tag-based methodologies for separation and detection of the phosphoproteome. Biochimica et Biophysica Acta 1854 (2015), 601–608.
    • (2015) Biochimica et Biophysica Acta , vol.1854 , pp. 601-608
    • Kinoshita, E.1    Kinoshita-Kikuta, E.2    Koike, T.3
  • 77
    • 40449113771 scopus 로고    scopus 로고
    • Identification of palmitoylated mitochondrial proteins using a bio-orthogonal azido-palmitate analogue
    • Kostiuk, M.A., Corvi, M.M., Keller, B.O., Plummer, G., Prescher, J.A., Hangauer, M.J., et al. Identification of palmitoylated mitochondrial proteins using a bio-orthogonal azido-palmitate analogue. FASEB Journal 22 (2008), 721–732.
    • (2008) FASEB Journal , vol.22 , pp. 721-732
    • Kostiuk, M.A.1    Corvi, M.M.2    Keller, B.O.3    Plummer, G.4    Prescher, J.A.5    Hangauer, M.J.6
  • 78
    • 84859434125 scopus 로고    scopus 로고
    • Palmitoylated calnexin is a key component of the ribosome-translocon complex
    • Lakkaraju, A.K., Abrami, L., Lemmin, T., Blaskovic, S., Kunz, B., Kihara, A., et al. Palmitoylated calnexin is a key component of the ribosome-translocon complex. EMBO Journal 31 (2012), 1823–1835.
    • (2012) EMBO Journal , vol.31 , pp. 1823-1835
    • Lakkaraju, A.K.1    Abrami, L.2    Lemmin, T.3    Blaskovic, S.4    Kunz, B.5    Kihara, A.6
  • 81
    • 77951225186 scopus 로고    scopus 로고
    • DHHC5 interacts with PDZ domain 3 of post-synaptic density-95 (PSD-95) protein and plays a role in learning and memory
    • Li, Y., Hu, J., Hofer, K., Wong, A.M., Cooper, J.D., Birnbaum, S.G., et al. DHHC5 interacts with PDZ domain 3 of post-synaptic density-95 (PSD-95) protein and plays a role in learning and memory. The Journal of Biological Chemistry 285 (2010), 13022–13031.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 13022-13031
    • Li, Y.1    Hu, J.2    Hofer, K.3    Wong, A.M.4    Cooper, J.D.5    Birnbaum, S.G.6
  • 82
    • 84855253929 scopus 로고    scopus 로고
    • DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells
    • Li, Y., Martin, B.R., Cravatt, B.F., Hofmann, S.L., DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells. The Journal of Biological Chemistry 287 (2012), 523–530.
    • (2012) The Journal of Biological Chemistry , vol.287 , pp. 523-530
    • Li, Y.1    Martin, B.R.2    Cravatt, B.F.3    Hofmann, S.L.4
  • 83
    • 67649800746 scopus 로고    scopus 로고
    • Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation
    • Lin, D.T., Makino, Y., Sharma, K., Hayashi, T., Neve, R., Takamiya, K., et al. Regulation of AMPA receptor extrasynaptic insertion by 4.1N, phosphorylation and palmitoylation. Nature Neuroscience 12 (2009), 879–887.
    • (2009) Nature Neuroscience , vol.12 , pp. 879-887
    • Lin, D.T.1    Makino, Y.2    Sharma, K.3    Hayashi, T.4    Neve, R.5    Takamiya, K.6
  • 87
    • 84857190393 scopus 로고    scopus 로고
    • Palmitoylated TMX and calnexin target to the mitochondria-associated membrane
    • Lynes, E.M., Bui, M., Yap, M.C., Benson, M.D., Schneider, B., Ellgaard, L., et al. Palmitoylated TMX and calnexin target to the mitochondria-associated membrane. EMBO Journal 31 (2012), 457–470.
    • (2012) EMBO Journal , vol.31 , pp. 457-470
    • Lynes, E.M.1    Bui, M.2    Yap, M.C.3    Benson, M.D.4    Schneider, B.5    Ellgaard, L.6
  • 88
    • 84878459382 scopus 로고    scopus 로고
    • Nanoscale scaffolding domains within the postsynaptic density concentrate synaptic AMPA receptors
    • MacGillavry, H.D., Song, Y., Raghavachari, S., Blanpied, T.A., Nanoscale scaffolding domains within the postsynaptic density concentrate synaptic AMPA receptors. Neuron 78 (2013), 615–622.
    • (2013) Neuron , vol.78 , pp. 615-622
    • MacGillavry, H.D.1    Song, Y.2    Raghavachari, S.3    Blanpied, T.A.4
  • 89
    • 23644444150 scopus 로고    scopus 로고
    • Loss of ZDHHC15 expression in a woman with a balanced translocation t(X;15)(q13.3;cen) and severe mental retardation
    • Mansouri, M.R., Marklund, L., Gustavsson, P., Davey, E., Carlsson, B., Larsson, C., et al. Loss of ZDHHC15 expression in a woman with a balanced translocation t(X;15)(q13.3;cen) and severe mental retardation. European Journal of Human Genetics 13 (2005), 970–977.
    • (2005) European Journal of Human Genetics , vol.13 , pp. 970-977
    • Mansouri, M.R.1    Marklund, L.2    Gustavsson, P.3    Davey, E.4    Carlsson, B.5    Larsson, C.6
  • 90
    • 80052981392 scopus 로고    scopus 로고
    • Molecular determinants of ciliary membrane localization of Trypanosoma cruzi flagellar calcium-binding protein
    • Maric, D., McGwire, B.S., Buchanan, K.T., Olson, C.L., Emmer, B.T., Epting, C.L., et al. Molecular determinants of ciliary membrane localization of Trypanosoma cruzi flagellar calcium-binding protein. The Journal of Biological Chemistry 286 (2011), 33109–33117.
    • (2011) The Journal of Biological Chemistry , vol.286 , pp. 33109-33117
    • Maric, D.1    McGwire, B.S.2    Buchanan, K.T.3    Olson, C.L.4    Emmer, B.T.5    Epting, C.L.6
  • 91
    • 84861100269 scopus 로고    scopus 로고
    • Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases
    • Marin, E.P., Derakhshan, B., Lam, T.T., Davalos, A., Sessa, W.C., Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases. Circulation Research 110 (2012), 1336–1344.
    • (2012) Circulation Research , vol.110 , pp. 1336-1344
    • Marin, E.P.1    Derakhshan, B.2    Lam, T.T.3    Davalos, A.4    Sessa, W.C.5
  • 92
    • 59349119386 scopus 로고    scopus 로고
    • Large-scale profiling of protein palmitoylation in mammalian cells
    • Martin, B.R., Cravatt, B.F., Large-scale profiling of protein palmitoylation in mammalian cells. Nature Methods 6 (2009), 135–138.
    • (2009) Nature Methods , vol.6 , pp. 135-138
    • Martin, B.R.1    Cravatt, B.F.2
  • 96
    • 80054036585 scopus 로고    scopus 로고
    • Proteomic profiling of S-acylated macrophage proteins identifies a role for palmitoylation in mitochondrial targeting of phospholipid scramblase 3
    • M110 006007
    • Merrick, B.A., Dhungana, S., Williams, J.G., Aloor, J.J., Peddada, S., Tomer, K.B., et al. Proteomic profiling of S-acylated macrophage proteins identifies a role for palmitoylation in mitochondrial targeting of phospholipid scramblase 3. Molecular and Cellular Proteomics, 10, 2011 M110 006007.
    • (2011) Molecular and Cellular Proteomics , vol.10
    • Merrick, B.A.1    Dhungana, S.2    Williams, J.G.3    Aloor, J.J.4    Peddada, S.5    Tomer, K.B.6
  • 97
    • 73649134679 scopus 로고    scopus 로고
    • Palmitoylation regulates epidermal homeostasis and hair follicle differentiation
    • Mill, P., Lee, A.W., Fukata, Y., Tsutsumi, R., Fukata, M., Keighren, M., et al. Palmitoylation regulates epidermal homeostasis and hair follicle differentiation. PLoS Genetics, 5, 2009, e1000748.
    • (2009) PLoS Genetics , vol.5 , pp. e1000748
    • Mill, P.1    Lee, A.W.2    Fukata, Y.3    Tsutsumi, R.4    Fukata, M.5    Keighren, M.6
  • 99
    • 84903538724 scopus 로고    scopus 로고
    • Mutations in the X-linked intellectual disability gene, zDHHC9, alter autopalmitoylation activity by distinct mechanisms
    • Mitchell, D.A., Hamel, L.D., Reddy, K.D., Farh, L., Rettew, L.M., Sanchez, P.R., et al. Mutations in the X-linked intellectual disability gene, zDHHC9, alter autopalmitoylation activity by distinct mechanisms. The Journal of Biological Chemistry 289 (2014), 18582–18592.
    • (2014) The Journal of Biological Chemistry , vol.289 , pp. 18582-18592
    • Mitchell, D.A.1    Hamel, L.D.2    Reddy, K.D.3    Farh, L.4    Rettew, L.M.5    Sanchez, P.R.6
  • 100
    • 78649662343 scopus 로고    scopus 로고
    • Mutational analysis of Saccharomyces cerevisiae Erf2 reveals a two-step reaction mechanism for protein palmitoylation by DHHC enzymes
    • Mitchell, D.A., Mitchell, G., Ling, Y., Budde, C., Deschenes, R.J., Mutational analysis of Saccharomyces cerevisiae Erf2 reveals a two-step reaction mechanism for protein palmitoylation by DHHC enzymes. The Journal of Biological Chemistry 285 (2010), 38104–38114.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 38104-38114
    • Mitchell, D.A.1    Mitchell, G.2    Ling, Y.3    Budde, C.4    Deschenes, R.J.5
  • 101
    • 0037073697 scopus 로고    scopus 로고
    • Flotillin-1/reggie-2 traffics to surface raft domains via a novel golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation
    • Morrow, I.C., Rea, S., Martin, S., Prior, I.A., Prohaska, R., Hancock, J.F., et al. Flotillin-1/reggie-2 traffics to surface raft domains via a novel golgi-independent pathway. Identification of a novel membrane targeting domain and a role for palmitoylation. The Journal of Biological Chemistry 277 (2002), 48834–48841.
    • (2002) The Journal of Biological Chemistry , vol.277 , pp. 48834-48841
    • Morrow, I.C.1    Rea, S.2    Martin, S.3    Prior, I.A.4    Prohaska, R.5    Hancock, J.F.6
  • 102
    • 54949150182 scopus 로고    scopus 로고
    • Palmitoylation-dependent neurodevelopmental deficits in a mouse model of 22q11 microdeletion
    • Mukai, J., Dhilla, A., Drew, L.J., Stark, K.L., Cao, L., MacDermott, A.B., et al. Palmitoylation-dependent neurodevelopmental deficits in a mouse model of 22q11 microdeletion. Nature Neuroscience 11 (2008), 1302–1310.
    • (2008) Nature Neuroscience , vol.11 , pp. 1302-1310
    • Mukai, J.1    Dhilla, A.2    Drew, L.J.3    Stark, K.L.4    Cao, L.5    MacDermott, A.B.6
  • 103
    • 3042804077 scopus 로고    scopus 로고
    • Evidence that the gene encoding ZDHHC8 contributes to the risk of schizophrenia
    • Mukai, J., Liu, H., Burt, R.A., Swor, D.E., Lai, W.S., Karayiorgou, M., et al. Evidence that the gene encoding ZDHHC8 contributes to the risk of schizophrenia. Nature Genetics 36 (2004), 725–731.
    • (2004) Nature Genetics , vol.36 , pp. 725-731
    • Mukai, J.1    Liu, H.2    Burt, R.A.3    Swor, D.E.4    Lai, W.S.5    Karayiorgou, M.6
  • 104
    • 84929046357 scopus 로고    scopus 로고
    • Molecular substrates of altered axonal growth and brain connectivity in a mouse model of schizophrenia
    • Mukai, J., Tamura, M., Fenelon, K., Rosen, A.M., Spellman, T.J., Kang, R., et al. Molecular substrates of altered axonal growth and brain connectivity in a mouse model of schizophrenia. Neuron 86 (2015), 680–695.
    • (2015) Neuron , vol.86 , pp. 680-695
    • Mukai, J.1    Tamura, M.2    Fenelon, K.3    Rosen, A.M.4    Spellman, T.J.5    Kang, R.6
  • 105
    • 84881139928 scopus 로고    scopus 로고
    • Super-resolution imaging reveals that AMPA receptors inside synapses are dynamically organized in nanodomains regulated by PSD95
    • Nair, D., Hosy, E., Petersen, J.D., Constals, A., Giannone, G., Choquet, D., et al. Super-resolution imaging reveals that AMPA receptors inside synapses are dynamically organized in nanodomains regulated by PSD95. The Journal of Neuroscience 33 (2013), 13204–13224.
    • (2013) The Journal of Neuroscience , vol.33 , pp. 13204-13224
    • Nair, D.1    Hosy, E.2    Petersen, J.D.3    Constals, A.4    Giannone, G.5    Choquet, D.6
  • 107
    • 0035173062 scopus 로고    scopus 로고
    • Palmitoylation of the Rous sarcoma virus transmembrane glycoprotein is required for protein stability and virus infectivity
    • Ochsenbauer-Jambor, C., Miller, D.C., Roberts, C.R., Rhee, S.S., Hunter, E., Palmitoylation of the Rous sarcoma virus transmembrane glycoprotein is required for protein stability and virus infectivity. Journal of Virology 75 (2001), 11544–11554.
    • (2001) Journal of Virology , vol.75 , pp. 11544-11554
    • Ochsenbauer-Jambor, C.1    Miller, D.C.2    Roberts, C.R.3    Rhee, S.S.4    Hunter, E.5
  • 108
    • 84870478193 scopus 로고    scopus 로고
    • Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system
    • Ohno, Y., Kashio, A., Ogata, R., Ishitomi, A., Yamazaki, Y., Kihara, A., Analysis of substrate specificity of human DHHC protein acyltransferases using a yeast expression system. Molecular Biology of the Cell 23 (2012), 4543–4551.
    • (2012) Molecular Biology of the Cell , vol.23 , pp. 4543-4551
    • Ohno, Y.1    Kashio, A.2    Ogata, R.3    Ishitomi, A.4    Yamazaki, Y.5    Kihara, A.6
  • 109
    • 33646830442 scopus 로고    scopus 로고
    • Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins
    • Ohno, Y., Kihara, A., Sano, T., Igarashi, Y., Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins. Biochimica et Biophysica Acta 1761 (2006), 474–483.
    • (2006) Biochimica et Biophysica Acta , vol.1761 , pp. 474-483
    • Ohno, Y.1    Kihara, A.2    Sano, T.3    Igarashi, Y.4
  • 110
    • 38049072215 scopus 로고    scopus 로고
    • Huntingtin-interacting protein 14, a palmitoyl transferase required for exocytosis and targeting of CSP to synaptic vesicles
    • Ohyama, T., Verstreken, P., Ly, C.V., Rosenmund, T., Rajan, A., Tien, A.C., et al. Huntingtin-interacting protein 14, a palmitoyl transferase required for exocytosis and targeting of CSP to synaptic vesicles. The Journal of Cell Biology 179 (2007), 1481–1496.
    • (2007) The Journal of Cell Biology , vol.179 , pp. 1481-1496
    • Ohyama, T.1    Verstreken, P.2    Ly, C.V.3    Rosenmund, T.4    Rajan, A.5    Tien, A.C.6
  • 111
    • 84880078204 scopus 로고    scopus 로고
    • In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10 (zDHHC1/3/11)-mediated neurochondrin palmitoylation in its targeting to Rab5-positive endosomes
    • Oku, S., Takahashi, N., Fukata, Y., Fukata, M., In silico screening for palmitoyl substrates reveals a role for DHHC1/3/10 (zDHHC1/3/11)-mediated neurochondrin palmitoylation in its targeting to Rab5-positive endosomes. The Journal of Biological Chemistry 288 (2013), 19816–19829.
    • (2013) The Journal of Biological Chemistry , vol.288 , pp. 19816-19829
    • Oku, S.1    Takahashi, N.2    Fukata, Y.3    Fukata, M.4
  • 112
    • 0033855298 scopus 로고    scopus 로고
    • Isolation of a novel gene on 8p21.3-22 whose expression is reduced significantly in human colorectal cancers with liver metastasis
    • Oyama, T., Miyoshi, Y., Koyama, K., Nakagawa, H., Yamori, T., Ito, T., et al. Isolation of a novel gene on 8p21.3-22 whose expression is reduced significantly in human colorectal cancers with liver metastasis. Genes, Chromosomes and Cancer 29 (2000), 9–15.
    • (2000) Genes, Chromosomes and Cancer , vol.29 , pp. 9-15
    • Oyama, T.1    Miyoshi, Y.2    Koyama, K.3    Nakagawa, H.4    Yamori, T.5    Ito, T.6
  • 113
    • 84901412371 scopus 로고    scopus 로고
    • Membrane-localized estrogen receptor alpha is required for normal organ development and function
    • Pedram, A., Razandi, M., Lewis, M., Hammes, S., Levin, E.R., Membrane-localized estrogen receptor alpha is required for normal organ development and function. Developmental Cell 29 (2014), 482–490.
    • (2014) Developmental Cell , vol.29 , pp. 482-490
    • Pedram, A.1    Razandi, M.2    Lewis, M.3    Hammes, S.4    Levin, E.R.5
  • 116
    • 34247636034 scopus 로고    scopus 로고
    • Mutations in ZDHHC9, which encodes a palmitoyltransferase of NRAS and HRAS, cause X-linked mental retardation associated with a Marfanoid habitus
    • Raymond, F.L., Tarpey, P.S., Edkins, S., Tofts, C., O'Meara, S., Teague, J., et al. Mutations in ZDHHC9, which encodes a palmitoyltransferase of NRAS and HRAS, cause X-linked mental retardation associated with a Marfanoid habitus. American Journal of Human Genetics 80 (2007), 982–987.
    • (2007) American Journal of Human Genetics , vol.80 , pp. 982-987
    • Raymond, F.L.1    Tarpey, P.S.2    Edkins, S.3    Tofts, C.4    O'Meara, S.5    Teague, J.6
  • 117
    • 0031978614 scopus 로고    scopus 로고
    • Palmitoylation of neurofascin at a site in the membrane-spanning domain highly conserved among the L1 family of cell adhesion molecules
    • Ren, Q., Bennett, V., Palmitoylation of neurofascin at a site in the membrane-spanning domain highly conserved among the L1 family of cell adhesion molecules. Journal of Neurochemistry 70 (1998), 1839–1849.
    • (1998) Journal of Neurochemistry , vol.70 , pp. 1839-1849
    • Ren, Q.1    Bennett, V.2
  • 118
    • 84877799575 scopus 로고    scopus 로고
    • Proteomic analysis of protein palmitoylation in adipocytes
    • Ren, W., Jhala, U.S., Du, K., Proteomic analysis of protein palmitoylation in adipocytes. Adipocyte 2 (2013), 17–28.
    • (2013) Adipocyte , vol.2 , pp. 17-28
    • Ren, W.1    Jhala, U.S.2    Du, K.3
  • 120
    • 77951913833 scopus 로고    scopus 로고
    • The palmitoylation machinery is a spatially organizing system for peripheral membrane proteins
    • Rocks, O., Gerauer, M., Vartak, N., Koch, S., Huang, Z.P., Pechlivanis, M., et al. The palmitoylation machinery is a spatially organizing system for peripheral membrane proteins. Cell 141 (2010), 458–471.
    • (2010) Cell , vol.141 , pp. 458-471
    • Rocks, O.1    Gerauer, M.2    Vartak, N.3    Koch, S.4    Huang, Z.P.5    Pechlivanis, M.6
  • 121
    • 33745745892 scopus 로고    scopus 로고
    • Spatio-temporal segregation of Ras signals: one ship, three anchors, many harbors
    • Rocks, O., Peyker, A., Bastiaens, P.I., Spatio-temporal segregation of Ras signals: one ship, three anchors, many harbors. Current Opinion in Cell Biology 18 (2006), 351–357.
    • (2006) Current Opinion in Cell Biology , vol.18 , pp. 351-357
    • Rocks, O.1    Peyker, A.2    Bastiaens, P.I.3
  • 122
    • 20144375061 scopus 로고    scopus 로고
    • An acylation cycle regulates localization and activity of palmitoylated Ras isoforms
    • Rocks, O., Peyker, A., Kahms, M., Verveer, P.J., Koerner, C., Lumbierres, M., et al. An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. Science 307 (2005), 1746–1752.
    • (2005) Science , vol.307 , pp. 1746-1752
    • Rocks, O.1    Peyker, A.2    Kahms, M.3    Verveer, P.J.4    Koerner, C.5    Lumbierres, M.6
  • 124
    • 0037078323 scopus 로고    scopus 로고
    • The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase
    • Roth, A.F., Feng, Y., Chen, L., Davis, N.G., The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase. The Journal of Cell Biology 159 (2002), 23–28.
    • (2002) The Journal of Cell Biology , vol.159 , pp. 23-28
    • Roth, A.F.1    Feng, Y.2    Chen, L.3    Davis, N.G.4
  • 125
    • 33646899047 scopus 로고    scopus 로고
    • Global analysis of protein palmitoylation in yeast
    • Roth, A.F., Wan, J., Bailey, A.O., Sun, B., Kuchar, J.A., Green, W.N., et al. Global analysis of protein palmitoylation in yeast. Cell 125 (2006), 1003–1013.
    • (2006) Cell , vol.125 , pp. 1003-1013
    • Roth, A.F.1    Wan, J.2    Bailey, A.O.3    Sun, B.4    Kuchar, J.A.5    Green, W.N.6
  • 126
    • 20044376098 scopus 로고    scopus 로고
    • No association was found between a functional SNP in ZDHHC8 and schizophrenia in a Japanese case-control population
    • Saito, S., Ikeda, M., Iwata, N., Suzuki, T., Kitajima, T., Yamanouchi, Y., et al. No association was found between a functional SNP in ZDHHC8 and schizophrenia in a Japanese case-control population. Neuroscience Letters 374 (2005), 21–24.
    • (2005) Neuroscience Letters , vol.374 , pp. 21-24
    • Saito, S.1    Ikeda, M.2    Iwata, N.3    Suzuki, T.4    Kitajima, T.5    Yamanouchi, Y.6
  • 127
    • 77954160193 scopus 로고    scopus 로고
    • Mice with alopecia, osteoporosis, and systemic amyloidosis due to mutation in Zdhhc13, a gene coding for palmitoyl acyltransferase
    • Saleem, A.N., Chen, Y.H., Baek, H.J., Hsiao, Y.W., Huang, H.W., Kao, H.J., et al. Mice with alopecia, osteoporosis, and systemic amyloidosis due to mutation in Zdhhc13, a gene coding for palmitoyl acyltransferase. PLoS Genetics, 6, 2010, e1000985.
    • (2010) PLoS Genetics , vol.6 , pp. e1000985
    • Saleem, A.N.1    Chen, Y.H.2    Baek, H.J.3    Hsiao, Y.W.4    Huang, H.W.5    Kao, H.J.6
  • 128
    • 84930320332 scopus 로고    scopus 로고
    • A single protein s-acyl transferase acts through diverse substrates to determine cryptococcal morphology, stress tolerance, and pathogenic outcome
    • Santiago-Tirado, F.H., Peng, T., Yang, M., Hang, H.C., Doering, T.L., A single protein s-acyl transferase acts through diverse substrates to determine cryptococcal morphology, stress tolerance, and pathogenic outcome. PLoS Pathogens, 11, 2015, e1004908.
    • (2015) PLoS Pathogens , vol.11 , pp. e1004908
    • Santiago-Tirado, F.H.1    Peng, T.2    Yang, M.3    Hang, H.C.4    Doering, T.L.5
  • 130
    • 0018643375 scopus 로고
    • Fatty acid binding to vesicular stomatitis virus glycoprotein: a new type of post-translational modification of the viral glycoprotein
    • Schmidt, M.F., Schlesinger, M.J., Fatty acid binding to vesicular stomatitis virus glycoprotein: a new type of post-translational modification of the viral glycoprotein. Cell 17 (1979), 813–819.
    • (1979) Cell , vol.17 , pp. 813-819
    • Schmidt, M.F.1    Schlesinger, M.J.2
  • 131
    • 84862897870 scopus 로고    scopus 로고
    • Palmitoylation by DHHC3 is critical for the function, expression, and stability of integrin alpha6beta4
    • Sharma, C., Rabinovitz, I., Hemler, M.E., Palmitoylation by DHHC3 is critical for the function, expression, and stability of integrin alpha6beta4. Cellular and Molecular Life Sciences 69 (2012), 2233–2244.
    • (2012) Cellular and Molecular Life Sciences , vol.69 , pp. 2233-2244
    • Sharma, C.1    Rabinovitz, I.2    Hemler, M.E.3
  • 132
    • 51049123096 scopus 로고    scopus 로고
    • DHHC2 affects palmitoylation, stability, and functions of tetraspanins CD9 and CD151
    • Sharma, C., Yang, X.H., Hemler, M.E., DHHC2 affects palmitoylation, stability, and functions of tetraspanins CD9 and CD151. Molecular Biology of the Cell 19 (2008), 3415–3425.
    • (2008) Molecular Biology of the Cell , vol.19 , pp. 3415-3425
    • Sharma, C.1    Yang, X.H.2    Hemler, M.E.3
  • 133
    • 34548436564 scopus 로고    scopus 로고
    • The postsynaptic architecture of excitatory synapses: a more quantitative view
    • Sheng, M., Hoogenraad, C.C., The postsynaptic architecture of excitatory synapses: a more quantitative view. Annual Review of Biochemistry 76 (2007), 823–847.
    • (2007) Annual Review of Biochemistry , vol.76 , pp. 823-847
    • Sheng, M.1    Hoogenraad, C.C.2
  • 134
    • 84901813852 scopus 로고    scopus 로고
    • Ion channel regulation by protein S-acylation
    • Shipston, M.J., Ion channel regulation by protein S-acylation. Journal of General Physiology 143 (2014), 659–678.
    • (2014) Journal of General Physiology , vol.143 , pp. 659-678
    • Shipston, M.J.1
  • 136
    • 84908223216 scopus 로고    scopus 로고
    • Psychiatric risk factor ANK3/ankyrin-G nanodomains regulate the structure and function of glutamatergic synapses
    • Smith, K.R., Kopeikina, K.J., Fawcett-Patel, J.M., Leaderbrand, K., Gao, R., Schurmann, B., et al. Psychiatric risk factor ANK3/ankyrin-G nanodomains regulate the structure and function of glutamatergic synapses. Neuron 84 (2014), 399–415.
    • (2014) Neuron , vol.84 , pp. 399-415
    • Smith, K.R.1    Kopeikina, K.J.2    Fawcett-Patel, J.M.3    Leaderbrand, K.4    Gao, R.5    Schurmann, B.6
  • 138
    • 84898637549 scopus 로고    scopus 로고
    • Palmitoyl acyltransferase, Zdhhc13, facilitates bone mass acquisition by regulating postnatal epiphyseal development and endochondral ossification: a mouse model
    • Song, I.W., Li, W.R., Chen, L.Y., Shen, L.F., Liu, K.M., Yen, J.J., et al. Palmitoyl acyltransferase, Zdhhc13, facilitates bone mass acquisition by regulating postnatal epiphyseal development and endochondral ossification: a mouse model. PLoS One, 9, 2014, e92194.
    • (2014) PLoS One , vol.9 , pp. e92194
    • Song, I.W.1    Li, W.R.2    Chen, L.Y.3    Shen, L.F.4    Liu, K.M.5    Yen, J.J.6
  • 140
    • 0023394457 scopus 로고
    • Ankyrin-bound fatty acid turns over rapidly at the erythrocyte plasma membrane
    • Staufenbiel, M., Ankyrin-bound fatty acid turns over rapidly at the erythrocyte plasma membrane. Molecular and Cellular Biology 7 (1987), 2981–2984.
    • (1987) Molecular and Cellular Biology , vol.7 , pp. 2981-2984
    • Staufenbiel, M.1
  • 141
    • 84873127663 scopus 로고    scopus 로고
    • Chemical proteomics: a powerful tool for exploring protein lipidation
    • Storck, E.M., Serwa, R.A., Tate, E.W., Chemical proteomics: a powerful tool for exploring protein lipidation. Biochemical Society Transactions 41 (2013), 56–61.
    • (2013) Biochemical Society Transactions , vol.41 , pp. 56-61
    • Storck, E.M.1    Serwa, R.A.2    Tate, E.W.3
  • 142
    • 36348948083 scopus 로고    scopus 로고
    • Drosophila huntingtin-interacting protein 14 is a presynaptic protein required for photoreceptor synaptic transmission and expression of the palmitoylated proteins synaptosome-associated protein 25 and cysteine string protein
    • Stowers, R.S., Isacoff, E.Y., Drosophila huntingtin-interacting protein 14 is a presynaptic protein required for photoreceptor synaptic transmission and expression of the palmitoylated proteins synaptosome-associated protein 25 and cysteine string protein. The Journal of Neuroscience 27 (2007), 12874–12883.
    • (2007) The Journal of Neuroscience , vol.27 , pp. 12874-12883
    • Stowers, R.S.1    Isacoff, E.Y.2
  • 148
    • 84863012668 scopus 로고    scopus 로고
    • Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking
    • Thomas, G.M., Hayashi, T., Chiu, S.L., Chen, C.M., Huganir, R.L., Palmitoylation by DHHC5/8 targets GRIP1 to dendritic endosomes to regulate AMPA-R trafficking. Neuron 73 (2012), 482–496.
    • (2012) Neuron , vol.73 , pp. 482-496
    • Thomas, G.M.1    Hayashi, T.2    Chiu, S.L.3    Chen, C.M.4    Huganir, R.L.5
  • 149
    • 84884547415 scopus 로고    scopus 로고
    • DHHC8-dependent PICK1 palmitoylation is required for induction of cerebellar long-term synaptic depression
    • Thomas, G.M., Hayashi, T., Huganir, R.L., Linden, D.J., DHHC8-dependent PICK1 palmitoylation is required for induction of cerebellar long-term synaptic depression. The Journal of Neuroscience 33 (2013), 15401–15407.
    • (2013) The Journal of Neuroscience , vol.33 , pp. 15401-15407
    • Thomas, G.M.1    Hayashi, T.2    Huganir, R.L.3    Linden, D.J.4
  • 150
    • 84873167786 scopus 로고    scopus 로고
    • Palmitoylation-dependent regulation of glutamate receptors and their PDZ domain-containing partners
    • Thomas, G.M., Huganir, R.L., Palmitoylation-dependent regulation of glutamate receptors and their PDZ domain-containing partners. Biochemical Society Transactions 41 (2013), 72–78.
    • (2013) Biochemical Society Transactions , vol.41 , pp. 72-78
    • Thomas, G.M.1    Huganir, R.L.2
  • 151
    • 77954900572 scopus 로고    scopus 로고
    • Multiple palmitoyltransferases are required for palmitoylation-dependent regulation of large conductance calcium- and voltage-activated potassium channels
    • Tian, L., McClafferty, H., Jeffries, O., Shipston, M.J., Multiple palmitoyltransferases are required for palmitoylation-dependent regulation of large conductance calcium- and voltage-activated potassium channels. The Journal of Biological Chemistry 285 (2010), 23954–23962.
    • (2010) The Journal of Biological Chemistry , vol.285 , pp. 23954-23962
    • Tian, L.1    McClafferty, H.2    Jeffries, O.3    Shipston, M.J.4
  • 152
    • 4043143032 scopus 로고    scopus 로고
    • G-protein-coupled receptor phosphorylation and palmitoylation
    • Tobin, A.B., Wheatley, M., G-protein-coupled receptor phosphorylation and palmitoylation. Methods in Molecular Biology 259 (2004), 275–281.
    • (2004) Methods in Molecular Biology , vol.259 , pp. 275-281
    • Tobin, A.B.1    Wheatley, M.2
  • 155
    • 0033621480 scopus 로고    scopus 로고
    • Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10
    • Tu, Y., Popov, S., Slaughter, C., Ross, E.M., Palmitoylation of a conserved cysteine in the regulator of G protein signaling (RGS) domain modulates the GTPase-activating activity of RGS4 and RGS10. The Journal of Biological Chemistry 274 (1999), 38260–38267.
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 38260-38267
    • Tu, Y.1    Popov, S.2    Slaughter, C.3    Ross, E.M.4
  • 156
    • 23044444831 scopus 로고    scopus 로고
    • Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation
    • Valdez-Taubas, J., Pelham, H., Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation. EMBO Journal 24 (2005), 2524–2532.
    • (2005) EMBO Journal , vol.24 , pp. 2524-2532
    • Valdez-Taubas, J.1    Pelham, H.2
  • 157
    • 17844408453 scopus 로고    scopus 로고
    • Palmitoylation of claudins is required for efficient tight-junction localization
    • Van Itallie, C.M., Gambling, T.M., Carson, J.L., Anderson, J.M., Palmitoylation of claudins is required for efficient tight-junction localization. Journal of Cell Science 118 (2005), 1427–1436.
    • (2005) Journal of Cell Science , vol.118 , pp. 1427-1436
    • Van Itallie, C.M.1    Gambling, T.M.2    Carson, J.L.3    Anderson, J.M.4
  • 158
    • 84865844356 scopus 로고    scopus 로고
    • Palmitoylation of virus proteins
    • Veit, M., Palmitoylation of virus proteins. Biology of the Cell 104 (2012), 493–515.
    • (2012) Biology of the Cell , vol.104 , pp. 493-515
    • Veit, M.1
  • 159
    • 0035876373 scopus 로고    scopus 로고
    • Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion
    • Veit, M., Laage, R., Dietrich, L., Wang, L., Ungermann, C., Vac8p release from the SNARE complex and its palmitoylation are coupled and essential for vacuole fusion. EMBO Journal 20 (2001), 3145–3155.
    • (2001) EMBO Journal , vol.20 , pp. 3145-3155
    • Veit, M.1    Laage, R.2    Dietrich, L.3    Wang, L.4    Ungermann, C.5
  • 160
    • 84888288922 scopus 로고    scopus 로고
    • Tracking brain palmitoylation change: predominance of glial change in a mouse model of Huntington's disease
    • Wan, J., Savas, J.N., Roth, A.F., Sanders, S.S., Singaraja, R.R., Hayden, M.R., et al. Tracking brain palmitoylation change: predominance of glial change in a mouse model of Huntington's disease. Chemistry and Biology 20 (2013), 1421–1434.
    • (2013) Chemistry and Biology , vol.20 , pp. 1421-1434
    • Wan, J.1    Savas, J.N.2    Roth, A.F.3    Sanders, S.S.4    Singaraja, R.R.5    Hayden, M.R.6
  • 162
    • 0028173706 scopus 로고
    • Activation and depalmitoylation of Gs alpha
    • Wedegaertner, P.B., Bourne, H.R., Activation and depalmitoylation of Gs alpha. Cell 77 (1994), 1063–1070.
    • (1994) Cell , vol.77 , pp. 1063-1070
    • Wedegaertner, P.B.1    Bourne, H.R.2
  • 163
  • 165
    • 84920997601 scopus 로고    scopus 로고
    • The palmitoyl acyltransferase DHHC2 regulates recycling endosome exocytosis and synaptic potentiation through palmitoylation of AKAP79/150
    • Woolfrey, K.M., Sanderson, J.L., Dell'Acqua, M.L., The palmitoyl acyltransferase DHHC2 regulates recycling endosome exocytosis and synaptic potentiation through palmitoylation of AKAP79/150. The Journal of Neuroscience 35 (2015), 442–456.
    • (2015) The Journal of Neuroscience , vol.35 , pp. 442-456
    • Woolfrey, K.M.1    Sanderson, J.L.2    Dell'Acqua, M.L.3
  • 166
    • 84874026361 scopus 로고    scopus 로고
    • Reduced expression of ZDHHC2 is associated with lymph node metastasis and poor prognosis in gastric adenocarcinoma
    • Yan, S.M., Tang, J.J., Huang, C.Y., Xi, S.Y., Huang, M.Y., Liang, J.Z., et al. Reduced expression of ZDHHC2 is associated with lymph node metastasis and poor prognosis in gastric adenocarcinoma. PLoS One, 8, 2013, e56366.
    • (2013) PLoS One , vol.8 , pp. e56366
    • Yan, S.M.1    Tang, J.J.2    Huang, C.Y.3    Xi, S.Y.4    Huang, M.Y.5    Liang, J.Z.6
  • 167
    • 76649102423 scopus 로고    scopus 로고
    • Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes
    • Yang, W., Di Vizio, D., Kirchner, M., Steen, H., Freeman, M.R., Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes. Molecular and Cellular Proteomics 9 (2010), 54–70.
    • (2010) Molecular and Cellular Proteomics , vol.9 , pp. 54-70
    • Yang, W.1    Di Vizio, D.2    Kirchner, M.3    Steen, H.4    Freeman, M.R.5
  • 169
  • 170
    • 84885397632 scopus 로고    scopus 로고
    • Putative DHHC-cysteine-rich domain S-acyltransferase in plants
    • Yuan, X., Zhang, S., Sun, M., Liu, S., Qi, B., Li, X., Putative DHHC-cysteine-rich domain S-acyltransferase in plants. PLoS One, 8, 2013, e75985.
    • (2013) PLoS One , vol.8 , pp. e75985
    • Yuan, X.1    Zhang, S.2    Sun, M.3    Liu, S.4    Qi, B.5    Li, X.6
  • 171
    • 47849089020 scopus 로고    scopus 로고
    • Identification of CKAP4/p63 as a major substrate of the palmitoyl acyltransferase DHHC2, a putative tumor suppressor, using a novel proteomics method
    • Zhang, J., Planey, S.L., Ceballos, C., Stevens, S.M. Jr., Keay, S.K., Zacharias, D.A., Identification of CKAP4/p63 as a major substrate of the palmitoyl acyltransferase DHHC2, a putative tumor suppressor, using a novel proteomics method. Molecular and Cellular Proteomics 7 (2008), 1378–1388.
    • (2008) Molecular and Cellular Proteomics , vol.7 , pp. 1378-1388
    • Zhang, J.1    Planey, S.L.2    Ceballos, C.3    Stevens, S.M.4    Keay, S.K.5    Zacharias, D.A.6
  • 172
    • 84880959257 scopus 로고    scopus 로고
    • Quantitative control of protein S-palmitoylation regulates meiotic entry in fission yeast
    • Zhang, M.M., Wu, P.Y., Kelly, F.D., Nurse, P., Hang, H.C., Quantitative control of protein S-palmitoylation regulates meiotic entry in fission yeast. PLoS Biology, 11, 2013, e1001597.
    • (2013) PLoS Biology , vol.11 , pp. e1001597
    • Zhang, M.M.1    Wu, P.Y.2    Kelly, F.D.3    Nurse, P.4    Hang, H.C.5
  • 174
    • 0037162696 scopus 로고    scopus 로고
    • Ras and Rap control AMPA receptor trafficking during synaptic plasticity
    • Zhu, J.J., Qin, Y., Zhao, M., Van Aelst, L., Malinow, R., Ras and Rap control AMPA receptor trafficking during synaptic plasticity. Cell 110 (2002), 443–455.
    • (2002) Cell , vol.110 , pp. 443-455
    • Zhu, J.J.1    Qin, Y.2    Zhao, M.3    Van Aelst, L.4    Malinow, R.5


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