메뉴 건너뛰기




Volumn 44, Issue 6, 2004, Pages 987-996

Identification of PSD-95 palmitoylating enzymes

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA AMINO 3 HYDROXY 5 METHYL 4 ISOXAZOLEPROPIONIC ACID; AMPA RECEPTOR; POSTSYNAPTIC DENSITY PROTEIN 95; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; TRANSFERASE;

EID: 10444253304     PISSN: 08966273     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neuron.2004.12.005     Document Type: Article
Times cited : (439)

References (38)
  • 1
    • 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. Mol. Cell. Biol. 19:1999;6775-6787
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6775-6787
    • Bartels, D.J.1    Mitchell, D.A.2    Dong, X.3    Deschenes, R.J.4
  • 2
    • 0029022642 scopus 로고
    • Chemical analysis of acylation sites and species
    • Bizzozero O.A. Chemical analysis of acylation sites and species. Methods Enzymol. 250:1995;361-379
    • (1995) Methods Enzymol. , vol.250 , pp. 361-379
    • Bizzozero, O.A.1
  • 3
    • 0029103106 scopus 로고
    • Dynamic regulation of G-protein coupled receptor palmitoylation: Potential role in receptor function
    • Bouvier M., Loisel T.P., Hebert T. Dynamic regulation of G-protein coupled receptor palmitoylation. potential role in receptor function Biochem. Soc. Trans. 23:1995;577-581
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 577-581
    • Bouvier, M.1    Loisel, T.P.2    Hebert, T.3
  • 4
    • 0028351930 scopus 로고
    • Lipid modifications of G proteins
    • Casey P.J. Lipid modifications of G proteins. Curr. Opin. Cell Biol. 6:1994;219-225
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 219-225
    • Casey, P.J.1
  • 5
    • 0027340389 scopus 로고
    • Increased palmitoylation of the Gs protein alpha subunit after activation by the beta-adrenergic receptor or cholera toxin
    • Degtyarev M.Y., Spiegel A.M., Jones T.L. Increased palmitoylation of the Gs protein alpha subunit after activation by the beta-adrenergic receptor or cholera toxin. J. Biol. Chem. 268:1993;23769-23772
    • (1993) J. Biol. Chem. , vol.268 , pp. 23769-23772
    • Degtyarev, M.Y.1    Spiegel, A.M.2    Jones, T.L.3
  • 6
    • 0032497835 scopus 로고    scopus 로고
    • Signalling functions of protein palmitoylation
    • Dunphy J.T., Linder M.E. Signalling functions of protein palmitoylation. Biochim. Biophys. Acta. 1436:1998;245-261
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 245-261
    • Dunphy, J.T.1    Linder, M.E.2
  • 7
    • 0034627757 scopus 로고    scopus 로고
    • Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering
    • a
    • El-Husseini A.E., Craven S.E., Chetkovich D.M., Firestein B.L., Schnell E., Aoki C., Bredt D.S. Dual palmitoylation of PSD-95 mediates its vesiculotubular sorting, postsynaptic targeting, and ion channel clustering. J. Cell Biol. 148:2000;159-171. a
    • (2000) J. Cell Biol. , vol.148 , pp. 159-171
    • 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
  • 9
    • 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 Nat. Rev. Neurosci. 3:2002;791-802
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 791-802
    • El-Husseini Ael, D.1    Bredt, D.S.2
  • 11
    • 0033621812 scopus 로고    scopus 로고
    • Interaction with Gbetagamma is required for membrane targeting and palmitoylation of Galpha(s) and Galpha(q)
    • Evanko D.S., Thiyagarajan M.M., Wedegaertner P.B. Interaction with Gbetagamma is required for membrane targeting and palmitoylation of Galpha(s) and Galpha(q). J. Biol. Chem. 275:2000;1327-1336
    • (2000) J. Biol. Chem. , vol.275 , pp. 1327-1336
    • Evanko, D.S.1    Thiyagarajan, M.M.2    Wedegaertner, P.B.3
  • 12
    • 0031952838 scopus 로고    scopus 로고
    • SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway
    • Gonzalo S., Linder M.E. SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway. Mol. Biol. Cell. 9:1998;585-597
    • (1998) Mol. Biol. Cell , vol.9 , pp. 585-597
    • Gonzalo, S.1    Linder, M.E.2
  • 13
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock J.F., Magee A.I., Childs J.E., Marshall C.J. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell. 57:1989;1167-1177
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 14
    • 0026471991 scopus 로고
    • The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS
    • Hess D.T., Slater T.M., Wilson M.C., Skene J.H. The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS. J. Neurosci. 12:1992;4634-4641
    • (1992) J. Neurosci. , vol.12 , pp. 4634-4641
    • Hess, D.T.1    Slater, T.M.2    Wilson, M.C.3    Skene, J.H.4
  • 16
    • 0030800671 scopus 로고    scopus 로고
    • Characterization of the palmitoylation domain of SNAP-25
    • Lane S.R., Liu Y. Characterization of the palmitoylation domain of SNAP-25. J. Neurochem. 69:1997;1864-1869
    • (1997) J. Neurochem. , vol.69 , pp. 1864-1869
    • Lane, S.R.1    Liu, Y.2
  • 17
    • 1242306884 scopus 로고    scopus 로고
    • Model organisms lead the way to protein palmitoyltransferases
    • Linder M.E., Deschenes R.J. Model organisms lead the way to protein palmitoyltransferases. J. Cell Sci. 117:2004;521-526
    • (2004) J. Cell Sci. , vol.117 , pp. 521-526
    • Linder, M.E.1    Deschenes, R.J.2
  • 19
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • Lobo S., Greentree W.K., Linder M.E., Deschenes R.J. Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J. Biol. Chem. 277:2002;41268-41273
    • (2002) J. Biol. Chem. , vol.277 , pp. 41268-41273
    • Lobo, S.1    Greentree, W.K.2    Linder, M.E.3    Deschenes, R.J.4
  • 20
    • 0029039937 scopus 로고
    • The dynamic role of palmitoylation in signal transduction
    • Milligan G., Parenti M., Magee A.I. The dynamic role of palmitoylation in signal transduction. Trends Biochem. Sci. 20:1995;181-187
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 181-187
    • Milligan, G.1    Parenti, M.2    Magee, A.I.3
  • 21
    • 0030936823 scopus 로고    scopus 로고
    • Reversible palmitoylation of signaling proteins
    • Mumby S.M. Reversible palmitoylation of signaling proteins. Curr. Opin. Cell Biol. 9:1997;148-154
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 148-154
    • Mumby, S.M.1
  • 23
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh M.D. Fatty acylation of proteins. new insights into membrane targeting of myristoylated and palmitoylated proteins Biochim. Biophys. Acta. 1451:1999;1-16
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 24
    • 0029014901 scopus 로고
    • Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae
    • Robbins S.M., Quintrell N.A., Bishop J.M. Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae. Mol. Cell. Biol. 15:1995;3507-3515
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3507-3515
    • Robbins, S.M.1    Quintrell, N.A.2    Bishop, J.M.3
  • 25
    • 0029240330 scopus 로고
    • Protein modification. Palmitoylation in G-protein signaling pathways
    • Ross E.M. Protein modification. Palmitoylation in G-protein signaling pathways. Curr. Biol. 5:1995;107-109
    • (1995) Curr. Biol. , vol.5 , pp. 107-109
    • Ross, E.M.1
  • 26
    • 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. J. Cell Biol. 159:2002;23-28
    • (2002) J. Cell Biol. , vol.159 , pp. 23-28
    • Roth, A.F.1    Feng, Y.2    Chen, L.3    Davis, N.G.4
  • 27
    • 0028175989 scopus 로고
    • Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae
    • Shenoy-Scaria A.M., Dietzen D.J., Kwong J., Link D.C., Lublin D.M. Cysteine3 of Src family protein tyrosine kinase determines palmitoylation and localization in caveolae. J. Cell Biol. 126:1994;353-363
    • (1994) J. Cell Biol. , vol.126 , pp. 353-363
    • Shenoy-Scaria, A.M.1    Dietzen, D.J.2    Kwong, J.3    Link, D.C.4    Lublin, D.M.5
  • 29
    • 0024576943 scopus 로고
    • Posttranslational membrane attachment and dynamic fatty acylation of a neuronal growth cone protein, GAP-43
    • Skene J.H., Virag I. Posttranslational membrane attachment and dynamic fatty acylation of a neuronal growth cone protein, GAP-43. J. Cell Biol. 108:1989;613-624
    • (1989) J. Cell Biol. , vol.108 , pp. 613-624
    • Skene, J.H.1    Virag, I.2
  • 30
    • 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. 73:2004;559-587
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 31
    • 0038045645 scopus 로고    scopus 로고
    • Postsynaptic density-95 mimics and occludes hippocampal long-term potentiation and enhances long-term depression
    • Stein V., House D.R., Bredt D.S., Nicoll R.A. Postsynaptic density-95 mimics and occludes hippocampal long-term potentiation and enhances long-term depression. J. Neurosci. 23:2003;5503-5506
    • (2003) J. Neurosci. , vol.23 , pp. 5503-5506
    • Stein, V.1    House, D.R.2    Bredt, D.S.3    Nicoll, R.A.4
  • 32
    • 0025117420 scopus 로고
    • A simple enzymatic method for the preparation of radiolabeled erucoyl-CoA and other long-chain fatty acyl-CoAs and their characterization by mass spectrometry
    • Taylor D.C., Weber N., Hogge L.R., Underhill E.W. A simple enzymatic method for the preparation of radiolabeled erucoyl-CoA and other long-chain fatty acyl-CoAs and their characterization by mass spectrometry. Anal. Biochem. 184:1990;311-316
    • (1990) Anal. Biochem. , vol.184 , pp. 311-316
    • Taylor, D.C.1    Weber, N.2    Hogge, L.R.3    Underhill, E.W.4
  • 33
    • 0031932282 scopus 로고    scopus 로고
    • N-terminal palmitoylation of PSD-95 regulates association with cell membranes and interaction with K+ channel, Kv1.4
    • Topinka J.R., Bredt D.S. N-terminal palmitoylation of PSD-95 regulates association with cell membranes and interaction with K+ channel, Kv1.4. Neuron. 20:1998;125-134
    • (1998) Neuron , vol.20 , pp. 125-134
    • Topinka, J.R.1    Bredt, D.S.2
  • 34
    • 0036389570 scopus 로고    scopus 로고
    • Isolation and characterization of Golgi apparatus-specific GODZ with the DHHC zinc finger domain
    • Uemura T., Mori H., Mishina M. Isolation and characterization of Golgi apparatus-specific GODZ with the DHHC zinc finger domain. Biochem. Biophys. Res. Commun. 296:2002;492-496
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 492-496
    • Uemura, T.1    Mori, H.2    Mishina, M.3
  • 35
    • 0033542139 scopus 로고    scopus 로고
    • SNAP-23 and SNAP-25 are palmitoylated in vivo
    • Vogel K., Roche P.A. SNAP-23 and SNAP-25 are palmitoylated in vivo. Biochem. Biophys. Res. Commun. 258:1999;407-410
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 407-410
    • Vogel, K.1    Roche, P.A.2
  • 36
    • 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
  • 37
    • 0027490954 scopus 로고
    • Palmitoylation is required for signaling functions and membrane attachment of Gq alpha and Gs alpha
    • Wedegaertner P.B., Chu D.H., Wilson P.T., Levis M.J., Bourne H.R. Palmitoylation is required for signaling functions and membrane attachment of Gq alpha and Gs alpha. J. Biol. Chem. 268:1993;25001-25008
    • (1993) J. Biol. Chem. , vol.268 , pp. 25001-25008
    • Wedegaertner, P.B.1    Chu, D.H.2    Wilson, P.T.3    Levis, M.J.4    Bourne, H.R.5
  • 38
    • 0346668323 scopus 로고    scopus 로고
    • Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins
    • Zhao L., Lobo S., Dong X., Ault A.D., Deschenes R.J. Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins. J. Biol. Chem. 277:2002;49352-49359
    • (2002) J. Biol. Chem. , vol.277 , pp. 49352-49359
    • Zhao, L.1    Lobo, S.2    Dong, X.3    Ault, A.D.4    Deschenes, R.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.