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Volumn 20, Issue 6, 2009, Pages 1833-1844

The hydrophobic cysteine-rich domain of SNAP25 couples with downstream residues to mediate membrane interactions and recognition by DHHC palmitoyl transferases

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CYSTEINE; LEUCINE; PALMITOYLTRANSFERASE; SMALL INTERFERING RNA; SNARE PROTEIN; SYNAPTOSOMAL ASSOCIATED PROTEIN 25; SYNTAXIN 1A; TRANSFERASE; UNCLASSIFIED DRUG; ACYLTRANSFERASE;

EID: 65649108966     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E08-08-0880     Document Type: Article
Times cited : (67)

References (44)
  • 1
    • 44449107477 scopus 로고    scopus 로고
    • Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum
    • Abrami, L., Kunz, B. A., Iacovache, I., and van der Goot, F. G. (2008). Palmitoylation and ubiquitination regulate exit of the Wnt signaling protein LRP6 from the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 105, 5384-5389.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 5384-5389
    • Abrami, L.1    Kunz, B.A.2    Iacovache, I.3    van der Goot, F.G.4
  • 2
    • 31944441121 scopus 로고    scopus 로고
    • SNAP25, but Not Syntaxin 1A, Recycles via an ARF6-regulated Pathway in Neuroendocrine Cells
    • Aikawa, Y., Xia, X., and Martin, T.F.J. (2006). SNAP25, but Not Syntaxin 1A, Recycles via an ARF6-regulated Pathway in Neuroendocrine Cells. Mol. Biol. Cell 17, 711-722.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 711-722
    • Aikawa, Y.1    Xia, X.2    Martin, T.F.J.3
  • 4
  • 5
    • 33748958810 scopus 로고    scopus 로고
    • Systematic screening forpalmitoyl transferase activity of the DHHC protein family in mammalian cells
    • Fukata, Y., Iwanaga, T., and Fukata, M. (2006). Systematic screening forpalmitoyl 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
  • 6
    • 0033794696 scopus 로고    scopus 로고
    • Membrane localisation and biological activity of SNAP-25 cysteine mutants in insulin-secreting cells
    • Gonelle-Gispert, C., Molinete, M., Halban, P., and Sadoul, K. (2000). Membrane localisation and biological activity of SNAP-25 cysteine mutants in insulin-secreting cells. J. Cell Sci. 113, 3197-3205.
    • (2000) J. Cell Sci , vol.113 , pp. 3197-3205
    • Gonelle-Gispert, C.1    Molinete, M.2    Halban, P.3    Sadoul, K.4
  • 7
    • 0033597815 scopus 로고    scopus 로고
    • SNAP-25 is targeted to the plasma membrane through a novel membrane-binding domain
    • Gonzalo, S., Greentree, W. K., and Linder, M. E. (1999). SNAP-25 is targeted to the plasma membrane through a novel membrane-binding domain. J. Biol. Chem. 274, 21313-21318.
    • (1999) J. Biol. Chem , vol.274 , pp. 21313-21318
    • Gonzalo, S.1    Greentree, W.K.2    Linder, M.E.3
  • 8
    • 0031952838 scopus 로고    scopus 로고
    • SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway
    • Gonzalo, S., and Linder, M. E. (1998). SNAP-25 palmitoylation and plasma membrane targeting require a functional secretory pathway. Mol. Biol. Cell 9, 585-597.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 585-597
    • Gonzalo, S.1    Linder, M.E.2
  • 10
    • 33750516084 scopus 로고    scopus 로고
    • Dual role of the cysteine-string Domain in membrane binding and palmitoylation-dependent sorting of the molecular chaperone cysteine-string protein
    • Greaves, J., and Chamberlain, L. H. (2006). Dual role of the cysteine-string Domain in membrane binding and palmitoylation-dependent sorting of the molecular chaperone cysteine-string protein. Mol. Biol. Cell 17, 4748-4759.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4748-4759
    • Greaves, J.1    Chamberlain, L.H.2
  • 11
    • 33846620628 scopus 로고    scopus 로고
    • Palmitoylation-dependent protein sorting
    • Greaves, J., and Chamberlain, L. H. (2007). Palmitoylation-dependent protein sorting. J. Cell Biol. 176, 249-254.
    • (2007) J. Cell Biol , vol.176 , pp. 249-254
    • Greaves, J.1    Chamberlain, L.H.2
  • 12
    • 54049132555 scopus 로고    scopus 로고
    • Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein
    • Greaves, J., Salaun, C., Fukata, Y., Fukata, M., and Chamberlain, L. H. (2008). Palmitoylation and membrane interactions of the neuroprotective chaperone cysteine-string protein. J. Biol. Chem. 283, 25014-25026.
    • (2008) J. Biol. Chem , vol.283 , pp. 25014-25026
    • Greaves, J.1    Salaun, C.2    Fukata, Y.3    Fukata, M.4    Chamberlain, L.H.5
  • 13
    • 23944433700 scopus 로고    scopus 로고
    • Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites
    • Hayashi, T., Rumbaugh, G., and Huganir, R. L. (2005). Differential regulation of AMPA receptor 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
  • 16
    • 9644302439 scopus 로고    scopus 로고
    • Presynaptic trafficking of synaptotagmin I is regulated by protein palmitoylation
    • Kang, R., Swayze, R., Lise, M. F., Gerrow, K., Mullard, A., Honer, W. G., and El-Husseini, A. (2004). Presynaptic trafficking of synaptotagmin I is regulated by protein palmitoylation. J. Biol. Chem. 279, 50524-50536.
    • (2004) J. Biol. Chem , vol.279 , pp. 50524-50536
    • Kang, R.1    Swayze, R.2    Lise, M.F.3    Gerrow, K.4    Mullard, A.5    Honer, W.G.6    El-Husseini, A.7
  • 18
    • 33745623380 scopus 로고    scopus 로고
    • Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3
    • Lam, K.K.Y., Davey, M., Sun, B., Roth, A. F., Davis, N. G., and Conibear, E. (2006). Palmitoylation by the DHHC protein Pfa4 regulates the ER exit of Chs3. J. Cell Biol. 174, 19-25.
    • (2006) J. Cell Biol , vol.174 , pp. 19-25
    • Lam, K.K.Y.1    Davey, M.2    Sun, B.3    Roth, A.F.4    Davis, N.G.5    Conibear, E.6
  • 19
    • 0030800671 scopus 로고    scopus 로고
    • Characterisation of the palmitoylation domain of SNAP-25
    • Lane, S., and Liu, S. (1997). Characterisation of the palmitoylation domain of SNAP-25. J. Neurochem. 69, 1864-1869.
    • (1997) J. Neurochem , vol.69 , pp. 1864-1869
    • Lane, S.1    Liu, S.2
  • 20
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: Policing protein stability and traffic
    • Linder, M. E., and Deschenes, R. J. (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
  • 21
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • Lobo, S., Greentree, W. K., Linder, M. E., and Deschenes, R. J. (2002). Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae. J. Biol. Chem. 277, 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
  • 22
    • 0037072816 scopus 로고    scopus 로고
    • SNAP-25 traffics to the plasma membrane by a syntaxin-independent mechanism
    • Loranger, S., and Linder, M. E. (2002). SNAP-25 traffics to the plasma membrane by a syntaxin-independent mechanism. J. Biol. Chem. 277, 34303-34309.
    • (2002) J. Biol. Chem , vol.277 , pp. 34303-34309
    • Loranger, S.1    Linder, M.E.2
  • 24
    • 38349018454 scopus 로고    scopus 로고
    • Munc18-1 prevents the formation of ectopic SNARE complexes in living cells
    • Medine, C. N., Rickman, C., Chamberlain, L. H., and Duncan, R. R. (2007). Munc18-1 prevents the formation of ectopic SNARE complexes in living cells. J. Cell Sci. 120, 4407-4415.
    • (2007) J. Cell Sci , vol.120 , pp. 4407-4415
    • Medine, C.N.1    Rickman, C.2    Chamberlain, L.H.3    Duncan, R.R.4
  • 25
    • 33744826797 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. Protein palmi- toylation by a family of DHHC protein S-acyltransferases
    • Mitchell, D. A., Vasudevan, A., Linder, M. E., and Deschenes, R. J. (2006). Thematic review series: lipid posttranslational modifications. Protein palmi- toylation by a family of DHHC protein S-acyltransferases. J. Lipid Res. 47, 1118-1127.
    • (2006) J. Lipid Res , vol.47 , pp. 1118-1127
    • Mitchell, D.A.1    Vasudevan, A.2    Linder, M.E.3    Deschenes, R.J.4
  • 26
    • 34848907786 scopus 로고    scopus 로고
    • Protein lipidation
    • Nadolski, M. J., and Linder, M. E. (2007). Protein lipidation. FEBS. 274, 5202-5210.
    • (2007) FEBS , vol.274 , pp. 5202-5210
    • Nadolski, M.J.1    Linder, M.E.2
  • 27
    • 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.,Haueter, C., Schulze, K. L., and Bellen, H. J. (2007). Huntingtin-interacting protein 14, a palmitoyl transferase required for exocytosis and targeting of CSP to synaptic vesicles. J. Cell Biol. 179, 1481-1496.
    • (2007) J. Cell Biol , 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    Haueter, C.7    Schulze, K.L.8    Bellen, H.J.9
  • 28
    • 15044343147 scopus 로고    scopus 로고
    • Transmembrane topology of the protein palmitoyl transferase Akr1
    • Politis, E. G., Roth, A. F., and Davis, N. G. (2005). Transmembrane topology of the protein palmitoyl transferase Akr1. J. Biol. Chem. 280, 10156-10163.
    • (2005) J. Biol. Chem , vol.280 , pp. 10156-10163
    • Politis, E.G.1    Roth, A.F.2    Davis, N.G.3
  • 29
    • 0028218727 scopus 로고
    • Differential detergent fractionation of isolated hepatocytes: Biochemical, immunochemical and two- dimensional gel electrophoresis characterization of cytoskeletal and noncy- toskeletal compartments
    • Ramsby, M. L., Makowski, G. S., Khairalla, E. A. (1994). Differential detergent fractionation of isolated hepatocytes: biochemical, immunochemical and two- dimensional gel electrophoresis characterization of cytoskeletal and noncy- toskeletal compartments. Electrophoresis 15, 265-277.
    • (1994) Electrophoresis , vol.15 , pp. 265-277
    • Ramsby, M.L.1    Makowski, G.S.2    Khairalla, E.A.3
  • 30
    • 33750266831 scopus 로고    scopus 로고
    • Trafficking and signaling by fatty-acylated and prenylated proteins
    • Resh, M. D. (2006). Trafficking and signaling by fatty-acylated and prenylated proteins. Nat. Chem. Biol. 2, 584-590.
    • (2006) Nat. Chem. Biol , vol.2 , pp. 584-590
    • Resh, M.D.1
  • 32
    • 0037078323 scopus 로고    scopus 로고
    • The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase
    • Roth, A. F., Feng, Y., Chen, L., and Davis, N. G. (2002). The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase. J. Cell Biol. 159,23-28.
    • (2002) J. Cell Biol , vol.159 , pp. 23-28
    • Roth, A.F.1    Feng, Y.2    Chen, L.3    Davis, N.G.4
  • 35
    • 12544252686 scopus 로고    scopus 로고
    • The SNARE proteins SNAP-25 and SNAP-23 display different affinities for lipid rafts in PC12 cells. Regulation by distinct cysteine-rich domains
    • Salaun, C., Gould, G. W., and Chamberlain, L. H. (2005). The SNARE proteins SNAP-25 and SNAP-23 display different affinities for lipid rafts in PC12 cells. Regulation by distinct cysteine-rich domains. J. Biol. Chem. 280, 1236-1240.
    • (2005) J. Biol. Chem , vol.280 , pp. 1236-1240
    • Salaun, C.1    Gould, G.W.2    Chamberlain, L.H.3
  • 36
    • 0028968896 scopus 로고
    • Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes
    • Shahinian, S., and Silvius, J. (1995). Doubly-lipid-modified protein sequence motifs exhibit long-lived anchorage to lipid bilayer membranes. Biochemistry 34, 3813-3822.
    • (1995) Biochemistry , vol.34 , pp. 3813-3822
    • Shahinian, S.1    Silvius, J.2
  • 37
    • 25444491476 scopus 로고    scopus 로고
    • The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p
    • Smotrys, J. E., Schoenfish, M. J., Stutz, M. A., and Linder, M. E. (2005). The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p. J. Cell Biol. 170, 1091-1099.
    • (2005) J. Cell Biol , vol.170 , pp. 1091-1099
    • Smotrys, J.E.1    Schoenfish, M.J.2    Stutz, M.A.3    Linder, M.E.4
  • 38
    • 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., and Isacoff, E. Y. (2007). 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. J. Neurosci. 27, 12874-12883.
    • (2007) J. Neurosci , vol.27 , pp. 12874-12883
    • Stowers, R.S.1    Isacoff, E.Y.2
  • 39
    • 24744466287 scopus 로고    scopus 로고
    • DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras
    • Swarthout, J. T., Lobo, S., Farh, L., Croke, M. R., Greentree, W. K., Deschenes, R. J., and Linder, M. E. (2005). DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras. J. Biol. Chem. 280, 31141-31148.
    • (2005) J. Biol. Chem , vol.280 , pp. 31141-31148
    • Swarthout, J.T.1    Lobo, S.2    Farh, L.3    Croke, M.R.4    Greentree, W.K.5    Deschenes, R.J.6    Linder, M.E.7
  • 40
    • 0034723194 scopus 로고    scopus 로고
    • Targeting of SNAP-25 to membranes is mediated by its association with the target SNARE syntaxin
    • Vogel, K., Cabaniols, J.-P., and Roche, P. A. (2000). Targeting of SNAP-25 to membranes is mediated by its association with the target SNARE syntaxin. J. Biol. Chem. 275, 2959-2965.
    • (2000) J. Biol. Chem , vol.275 , pp. 2959-2965
    • Vogel, K.1    Cabaniols, J.-P.2    Roche, P.A.3
  • 41
    • 0035425203 scopus 로고    scopus 로고
    • Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting
    • Washbourne, P., Cansino, V., Mathews, J., Graham, M. E., Burgoyne, R., and Wilson, M. (2001). Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting. Biochem. J. 357, 625-634.
    • (2001) Biochem. J , vol.357 , pp. 625-634
    • Washbourne, P.1    Cansino, V.2    Mathews, J.3    Graham, M.E.4    Burgoyne, R.5    Wilson, M.6
  • 42
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host [Guest Pentapeptides]
    • Wimley, W. C., Creamer, T. P., and White, S. H. (1996). Solvation energies of amino acid side chains and backbone in a family of host [Guest Pentapeptides] Biochemistry 35, 5109-5124.
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 43
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • Wimley, W. C., and White, S. H. (1996). Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat. Struct. Mol. Biol. 3, 842-848.
    • (1996) Nat. Struct. Mol. Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 44
    • 0345737131 scopus 로고    scopus 로고
    • An immunohistochemical method that distinguishes free from complexed SNAP-25
    • Xiao, J., Zongping, X., Anuradha, P., Qiong, Z., and Yuechueng, L. (2004). An immunohistochemical method that distinguishes free from complexed SNAP-25. J. Neurosci. Research 75, 143-151.
    • (2004) J. Neurosci. Research , vol.75 , pp. 143-151
    • Xiao, J.1    Zongping, X.2    Anuradha, P.3    Qiong, Z.4    Yuechueng, L.5


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