메뉴 건너뛰기




Volumn 47, Issue 6, 2006, Pages 1118-1127

Protein palmitoylation by a family of DHHC protein S-acyltransferases

Author keywords

Cysteine rich domain; Fatty acylation; Palmitoyl CoenzymeA

Indexed keywords

ACYLTRANSFERASE; ASPARTYLHISTIDYLHISTIDYLCYSTEINE; CASEIN KINASE; LONG CHAIN FATTY ACID; PALMITIC ACID; RAS PROTEIN; S PALMITOYLTRANSFERASE; UNCLASSIFIED DRUG;

EID: 33744826797     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.R600007-JLR200     Document Type: Review
Times cited : (363)

References (74)
  • 1
    • 1242306884 scopus 로고    scopus 로고
    • Model organisms lead the way to protein palmitoyltransferases
    • Linder, M. E., and R. J. Deschenes. 2004. Model organisms lead the way to protein palmitoyltransferases. J. Cell Sci. 117: 521-526.
    • (2004) J. Cell Sci. , vol.117 , pp. 521-526
    • Linder, M.E.1    Deschenes, R.J.2
  • 2
    • 0038321812 scopus 로고    scopus 로고
    • New insights into the mechanisms of protein palmitoylation
    • Linder, M. E., and R. J. Deschenes. 2003. New insights into the mechanisms of protein palmitoylation. Biochemistry. 42: 4311-4320.
    • (2003) Biochemistry , vol.42 , pp. 4311-4320
    • Linder, M.E.1    Deschenes, R.J.2
  • 3
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: Regulation and function
    • Smotrys, J. E., and M. E. Linder. 2004. Palmitoylation of intracellular signaling proteins: regulation and function. Annu. Rev. Biochem. 73: 559-587.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 559-587
    • Smotrys, J.E.1    Linder, M.E.2
  • 4
    • 2942742564 scopus 로고    scopus 로고
    • Novel lipid modifications of secreted protein signals
    • Mann, R. K., and P. A. Beachy. 2004. Novel lipid modifications of secreted protein signals. Annu. Rev. Biochem. 73: 891-923.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 891-923
    • Mann, R.K.1    Beachy, P.A.2
  • 5
    • 0028033931 scopus 로고
    • Cysteine-containing peptide sequences exhibit facile uncatalyzed transacylation and acyl-CoA-dependent acylation at the lipid bilayer interface
    • Quesnel, S., and J. R. Silvius. 1994. Cysteine-containing peptide sequences exhibit facile uncatalyzed transacylation and acyl-CoA-dependent acylation at the lipid bilayer interface. Biochemistry. 33: 13340-13348.
    • (1994) Biochemistry , vol.33 , pp. 13340-13348
    • Quesnel, S.1    Silvius, J.R.2
  • 6
    • 0028980377 scopus 로고
    • Myelin P0 glycoprotein and a synthetic peptide containing the palmitoylation site are both autoacylated
    • Bharadwaj, M., and O. A. Bizzozero. 1995. Myelin P0 glycoprotein and a synthetic peptide containing the palmitoylation site are both autoacylated. J. Neurochem. 65: 1805-1815.
    • (1995) J. Neurochem. , vol.65 , pp. 1805-1815
    • Bharadwaj, M.1    Bizzozero, O.A.2
  • 7
    • 0029814190 scopus 로고    scopus 로고
    • Autoacylation of G protein alpha subunits
    • Duncan, J. A., and A. G. Gilman. 1996. Autoacylation of G protein alpha subunits. J. Biol. Chem. 271: 23594-23600.
    • (1996) J. Biol. Chem. , vol.271 , pp. 23594-23600
    • Duncan, J.A.1    Gilman, A.G.2
  • 8
    • 77956657444 scopus 로고    scopus 로고
    • Reversible modification of proteins with thioester-linked fatty acids
    • F. Tamanoi and D. S. Sigman, editors. Academic Press, San Diego, CA
    • Linder, M. E. 2001. Reversible modification of proteins with thioester-linked fatty acids. In The Enzymes: Protein Lipidation. F. Tamanoi and D. S. Sigman, editors. Academic Press, San Diego, CA. 215-240
    • (2001) The Enzymes: Protein Lipidation , pp. 215-240
    • Linder, M.E.1
  • 10
    • 0035903208 scopus 로고    scopus 로고
    • Heterogeneous fatty acylation of Src family kinases with polyunsaturated fatty acids regulates raft localization and signal transduction
    • Liang, X., A. Nazarian, H. Erdjument-Bromage, W. Bornmann, P. Tempst, and M. D. Resh. 2001. Heterogeneous fatty acylation of Src family kinases with polyunsaturated fatty acids regulates raft localization and signal transduction. J. Biol. Chem. 276: 30987-30994.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30987-30994
    • Liang, X.1    Nazarian, A.2    Erdjument-Bromage, H.3    Bornmann, W.4    Tempst, P.5    Resh, M.D.6
  • 11
    • 0037031868 scopus 로고    scopus 로고
    • Mass spectrometric analysis of GAP-43/neuromodulin reveals the presence of a variety of fatty acylated species
    • Liang, X., Y. Lu, T. A. Neubert, and M. D. Resh. 2002. Mass spectrometric analysis of GAP-43/neuromodulin reveals the presence of a variety of fatty acylated species. J. Biol. Chem. 277: 33032-33040.
    • (2002) J. Biol. Chem. , vol.277 , pp. 33032-33040
    • Liang, X.1    Lu, Y.2    Neubert, T.A.3    Resh, M.D.4
  • 12
    • 0037174987 scopus 로고    scopus 로고
    • Identification of a Ras palmitoyltransferase in Saccharomyces cerevisiae
    • Lobo, S., W. K. Greentree, M. E. Linder, and R. J. Deschenes. 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
  • 13
    • 0037078323 scopus 로고    scopus 로고
    • The yeast DHHC cysteine-rich domain protein Akr1p is a palmitoyl transferase
    • Roth, A. F., Y. Feng, L. Chen, and N. G. Davis. 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
  • 14
    • 0035860538 scopus 로고    scopus 로고
    • Skinny Hedgehog, an acyltransferase required for palmitoylation and activity of the Hedgehog signal
    • Chamoun, Z., R. K. Mann, D. Nellen, D. P. von Kessler, M. Bellotto, P. A. Beachy, and K. Basler. 2001. Skinny Hedgehog, an acyltransferase required for palmitoylation and activity of the Hedgehog signal. Science. 293: 2080-2084.
    • (2001) Science , vol.293 , pp. 2080-2084
    • Chamoun, Z.1    Mann, R.K.2    Nellen, D.3    Von Kessler, D.P.4    Bellotto, M.5    Beachy, P.A.6    Basler, K.7
  • 15
    • 31744439979 scopus 로고    scopus 로고
    • Palmitoylation of the EGFR ligand spitz by rasp increases spitz activity by restricting its diffusion
    • Miura, G. I., J. Buglino, D. Alvarado, M. A. Lemmon, M. D. Resh, and J. E. Treisman. 2006. Palmitoylation of the EGFR ligand spitz by rasp increases spitz activity by restricting its diffusion. Dev. Cell. 10: 167-176.
    • (2006) Dev. Cell , vol.10 , pp. 167-176
    • Miura, G.I.1    Buglino, J.2    Alvarado, D.3    Lemmon, M.A.4    Resh, M.D.5    Treisman, J.E.6
  • 16
    • 4043154959 scopus 로고    scopus 로고
    • Drosophila wnt-1 undergoes a hydrophobic modification and is targeted to lipid rafts, a process that requires porcupine
    • Zhai, L., D. Chaturvedi, and S. Cumberledge. 2004. Drosophila wnt-1 undergoes a hydrophobic modification and is targeted to lipid rafts, a process that requires porcupine. J. Biol. Chem. 279: 33220-33227.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33220-33227
    • Zhai, L.1    Chaturvedi, D.2    Cumberledge, S.3
  • 17
    • 0034161499 scopus 로고    scopus 로고
    • A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling
    • Hofmann, K. 2000. A superfamily of membrane-bound O-acyltransferases with implications for wnt signaling. Trends Biochem. Sci. 25: 111-112.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 111-112
    • Hofmann, K.1
  • 18
    • 0036389570 scopus 로고    scopus 로고
    • Isolation and characterization of Golgi apparatus-specific GODZ with the DHHC zinc finger domain
    • Uemura, T., H. Mori, and M. Mishina. 2002. Isolation and characterization of Golgi apparatus-specific GODZ with the DHHC zinc finger domain. Biochem. Biophys. Res. Commun. 296: 492-496.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 492-496
    • Uemura, T.1    Mori, H.2    Mishina, M.3
  • 19
    • 24744466287 scopus 로고    scopus 로고
    • DHHC9 and GCP16 constitute a human protein fatty acyltransferase with specificity for H- and N-Ras
    • Swarthout, J. T., S. Lobo, L. Farh, M. R. Croke, W. K. Greentree, R. J. Deschenes, and M. E. Linder. 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
  • 20
    • 3142727963 scopus 로고    scopus 로고
    • NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide synthase (nNOS) to the synaptic membrane through a PDZ-dependent interaction and regulates nNOS activity
    • Saitoh, F., Q. B. Tian, A. Okano, H. Sakagami, H. Kondo, and T. Suzuki. 2004. NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide synthase (nNOS) to the synaptic membrane through a PDZ-dependent interaction and regulates nNOS activity. J. Biol. Chem. 279: 29461-29468.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29461-29468
    • Saitoh, F.1    Tian, Q.B.2    Okano, A.3    Sakagami, H.4    Kondo, H.5    Suzuki, T.6
  • 21
    • 0032883098 scopus 로고    scopus 로고
    • Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae
    • Bartels, D. J., D. A. Mitchell, X. Dong, and R. J. Deschenes. 1999. Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae. Mol. Cell. Biol. 19: 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
  • 22
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: Different signals from different locations
    • Hancock, J. F. 2003. Ras proteins: different signals from different locations. Nat. Rev. Mol. Cell Biol. 4: 373-384.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 24
    • 0025183869 scopus 로고
    • Evidence for an S-farnesylcysteine methyl ester at the carboxyl terminus of the Saccharomyces cerevisiae RAS2 protein
    • Stimmel, J. B., R. J. Deschenes, C. Volker, J. Stock, and S. Clarke. 1990. Evidence for an S-farnesylcysteine methyl ester at the carboxyl terminus of the Saccharomyces cerevisiae RAS2 protein. Biochemistry. 29: 9651-9659.
    • (1990) Biochemistry , vol.29 , pp. 9651-9659
    • Stimmel, J.B.1    Deschenes, R.J.2    Volker, C.3    Stock, J.4    Clarke, S.5
  • 25
    • 0030909336 scopus 로고    scopus 로고
    • Modulation of Ras and a-factor function by carboxyl-terminal proteolysis
    • Boyartchuk, V. L., M. N. Ashby, and J. Rine. 1997. Modulation of Ras and a-factor function by carboxyl-terminal proteolysis. Science. 275: 1796-1800.
    • (1997) Science , vol.275 , pp. 1796-1800
    • Boyartchuk, V.L.1    Ashby, M.N.2    Rine, J.3
  • 26
    • 0025051169 scopus 로고
    • Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae
    • Hrycyna, C. A., and S. Clarke. 1990. Farnesyl cysteine C-terminal methyltransferase activity is dependent upon the STE14 gene product in Saccharomyces cerevisiae. Mol. Cell. Biol. 10: 5071-5076.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5071-5076
    • Hrycyna, C.A.1    Clarke, S.2
  • 27
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock, J. F., A. I. Magee, J. E. Childs, and C. J. Marshall. 1989. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell. 57: 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
  • 28
    • 0027956349 scopus 로고
    • A polybasic domain allows nonprenylated Ras proteins to function in Saccharomyces cerevisiae
    • Mitchell, D. A., L. Farh, T. K. Marshall, and R. J. Deschenes. 1994. A polybasic domain allows nonprenylated Ras proteins to function in Saccharomyces cerevisiae. J. Biol. Chem. 269: 21540-21546.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21540-21546
    • Mitchell, D.A.1    Farh, L.2    Marshall, T.K.3    Deschenes, R.J.4
  • 29
    • 0028872726 scopus 로고
    • Mutations in the SHR5 gene of Saccharomyces cerevisiae suppress Ras function and block membrane attachment and palmitoylation of Ras proteins
    • Jung, V., L. Chen, S. L. Hofmann, M. Wigler, and S. Powers. 1995. Mutations in the SHR5 gene of Saccharomyces cerevisiae suppress Ras function and block membrane attachment and palmitoylation of Ras proteins. Mol. Cell. Biol. 15: 1333-1342.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1333-1342
    • Jung, V.1    Chen, L.2    Hofmann, S.L.3    Wigler, M.4    Powers, S.5
  • 30
    • 0032530150 scopus 로고    scopus 로고
    • Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage
    • Schmidt, W. K., A. Tam, K. Fujimura-Kamada, and S. Michaelis. 1998. Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage. Proc. Natl. Acad. Sci. USA. 95: 11175-11180.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11175-11180
    • Schmidt, W.K.1    Tam, A.2    Fujimura-Kamada, K.3    Michaelis, S.4
  • 31
    • 0031858844 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae prenylcysteine carboxyl methyltransferase Ste14p is in the endoplasmic reticulum membrane
    • Romano, J. D., W. K. Schmidt, and S. Michaelis. 1998. The Saccharomyces cerevisiae prenylcysteine carboxyl methyltransferase Ste14p is in the endoplasmic reticulum membrane. Mol. Biol. Cell. 9: 2231-2247.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2231-2247
    • Romano, J.D.1    Schmidt, W.K.2    Michaelis, S.3
  • 32
    • 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., S. Lobo, X. Dong, A. D. Ault, and R. J. Deschenes. 2002. Erf4p and Erf2p form an endoplasmic reticulum-associated complex involved in the plasma membrane localization of yeast Ras proteins. J. Biol. Chem. 277: 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
  • 33
    • 25444491476 scopus 로고    scopus 로고
    • The vacuolar DHHC-CRD protein Pfa3p is a protein acyltransferase for Vac8p
    • Smotrys, J. E., M. J. Schoenfish, M. A. Stutz, and M. E. Linder. 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
  • 34
    • 0030855771 scopus 로고    scopus 로고
    • The ankyrin repeat-containing protein Akr1p is required for the endocytosis of yeast pheromone receptors
    • Givan, S. A., and G. F. Sprague, Jr. 1997. The ankyrin repeat-containing protein Akr1p is required for the endocytosis of yeast pheromone receptors. Mol. Biol. Cell. 8: 1317-1327.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1317-1327
    • Givan, S.A.1    Sprague Jr., G.F.2
  • 35
    • 0029655984 scopus 로고    scopus 로고
    • Interactions between the ankyrin repeat-containing protein Akr1p and the pheromone response pathway in Saccharomyces cerevisiae
    • Kao, L. R., J. Peterson, R. Ji, L. Bender, and A. Bender. 1996. Interactions between the ankyrin repeat-containing protein Akr1p and the pheromone response pathway in Saccharomyces cerevisiae. Mol. Cell. Biol. 16: 168-178.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 168-178
    • Kao, L.R.1    Peterson, J.2    Ji, R.3    Bender, L.4    Bender, A.5
  • 36
    • 0029954765 scopus 로고    scopus 로고
    • AKR1 encodes a candidate effector of the G beta gamma complex in the Saccharomyces cerevisiae pheromone response pathway and contributes to control of both cell shape and signal transduction
    • Pryciak, P. M., and L. H. Hartwell. 1996. AKR1 encodes a candidate effector of the G beta gamma complex in the Saccharomyces cerevisiae pheromone response pathway and contributes to control of both cell shape and signal transduction. Mol. Cell. Biol. 16: 2614-2626.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2614-2626
    • Pryciak, P.M.1    Hartwell, L.H.2
  • 37
    • 0033934481 scopus 로고    scopus 로고
    • Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane
    • Feng, Y., and N. G. Davis. 2000. Akr1p and the type I casein kinases act prior to the ubiquitination step of yeast endocytosis: Akr1p is required for kinase localization to the plasma membrane. Mol. Cell. Biol. 20: 5350-5359.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5350-5359
    • Feng, Y.1    Davis, N.G.2
  • 38
    • 1542344019 scopus 로고    scopus 로고
    • The yeast casein kinase Yck3p is palmitoylated, then sorted to the vacuolar membrane with AP-3-dependent recognition of a YXXPhi adaptin sorting signal
    • Sun, B., L. Chen, W. Cao, A. F. Roth, and N. G. Davis. 2004. The yeast casein kinase Yck3p is palmitoylated, then sorted to the vacuolar membrane with AP-3-dependent recognition of a YXXPhi adaptin sorting signal. Mol. Biol. Cell. 15: 1397-1406.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1397-1406
    • Sun, B.1    Chen, L.2    Cao, W.3    Roth, A.F.4    Davis, N.G.5
  • 39
    • 0032911043 scopus 로고    scopus 로고
    • The Yck2 yeast casein kinase 1 isoform shows cell cycle-specific localization to sites of polarized growth and is required for proper septin organization
    • Robinson, L. C., C. Bradley, J. D. Bryan, A. Jerome, Y. Kweon, and H. R. Panek. 1999. The Yck2 yeast casein kinase 1 isoform shows cell cycle-specific localization to sites of polarized growth and is required for proper septin organization. Mol. Biol. Cell. 10: 1077-1092.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1077-1092
    • Robinson, L.C.1    Bradley, C.2    Bryan, J.D.3    Jerome, A.4    Kweon, Y.5    Panek, H.R.6
  • 40
    • 0037115490 scopus 로고    scopus 로고
    • Plasma membrane localization of the Yck2p yeast casein kinase 1 isoform requires the C-terminal extension and secretory pathway function
    • Babu, P., J. D. Bryan, H. R. Panek, S. L. Jordan, B. M. Forbrich, S. C. Kelley, R. T. Colvin, and L. C. Robinson. 2002. Plasma membrane localization of the Yck2p yeast casein kinase 1 isoform requires the C-terminal extension and secretory pathway function. J. Cell Sci. 115: 4957-4968.
    • (2002) J. Cell Sci. , vol.115 , pp. 4957-4968
    • Babu, P.1    Bryan, J.D.2    Panek, H.R.3    Jordan, S.L.4    Forbrich, B.M.5    Kelley, S.C.6    Colvin, R.T.7    Robinson, L.C.8
  • 41
    • 15044343147 scopus 로고    scopus 로고
    • Transmembrane topology of the protein palmitoyl transferase Akr1
    • Politis, E. G., A. F. Roth, and N. G. Davis. 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
  • 42
    • 27144458423 scopus 로고    scopus 로고
    • Long-chain base kinase Lcb4 Is anchored to the membrane through its palmitoylation by Akr1
    • Kihara, A., F. Kurotsu, T. Sano, S. Iwaki, and Y. Igarashi. 2005. Long-chain base kinase Lcb4 Is anchored to the membrane through its palmitoylation by Akr1. Mol. Cell. Biol. 25: 9189-9197.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 9189-9197
    • Kihara, A.1    Kurotsu, F.2    Sano, T.3    Iwaki, S.4    Igarashi, Y.5
  • 44
    • 0032498794 scopus 로고    scopus 로고
    • Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole
    • Wang, Y. X., N. L. Catlett, and L. S. Weisman. 1998. Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. J. Cell Biol. 140: 1063-1074.
    • (1998) J. Cell Biol. , vol.140 , pp. 1063-1074
    • Wang, Y.X.1    Catlett, N.L.2    Weisman, L.S.3
  • 45
    • 0031669618 scopus 로고    scopus 로고
    • YEB3/VAC8 encodes a myristylated armadillo protein of the Saccharomyces cerevisiae vacuolar membrane that functions in vacuole fusion and inheritance
    • Pan, X., and D. S. Goldfarb. 1998. YEB3/VAC8 encodes a myristylated armadillo protein of the Saccharomyces cerevisiae vacuolar membrane that functions in vacuole fusion and inheritance. J. Cell Sci. 111: 2137-2147.
    • (1998) J. Cell Sci. , vol.111 , pp. 2137-2147
    • Pan, X.1    Goldfarb, D.S.2
  • 46
    • 10044268365 scopus 로고    scopus 로고
    • On the mechanism of protein palmitoylation
    • Dietrich, L. E., and C. Ungermann. 2004. On the mechanism of protein palmitoylation. EMBO Rep. 5: 1053-1057.
    • (2004) EMBO Rep. , vol.5 , pp. 1053-1057
    • Dietrich, L.E.1    Ungermann, C.2
  • 47
    • 0842285407 scopus 로고    scopus 로고
    • The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion
    • Dietrich, L. E., R. Gurezka, M. Veit, and C. Ungermann. 2004. The SNARE Ykt6 mediates protein palmitoylation during an early stage of homotypic vacuole fusion. EMBO J. 23: 45-53.
    • (2004) EMBO J. , vol.23 , pp. 45-53
    • Dietrich, L.E.1    Gurezka, R.2    Veit, M.3    Ungermann, C.4
  • 48
    • 23044444831 scopus 로고    scopus 로고
    • Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation
    • Valdez-Taubas, J., and H. Pelham. 2005. Swf1-dependent palmitoylation of the SNARE Tlg1 prevents its ubiquitination and degradation. EMBO J. 24: 2524-2532.
    • (2005) EMBO J. , vol.24 , pp. 2524-2532
    • Valdez-Taubas, J.1    Pelham, H.2
  • 49
    • 0032837425 scopus 로고    scopus 로고
    • A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae
    • Coe, J. G., A. C. Lim, J. Xu, and W. Hong. 1999. A role for Tlg1p in the transport of proteins within the Golgi apparatus of Saccharomyces cerevisiae. Mol. Biol. Cell. 10: 2407-2423.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2407-2423
    • Coe, J.G.1    Lim, A.C.2    Xu, J.3    Hong, W.4
  • 50
    • 0033614462 scopus 로고    scopus 로고
    • The Drosophila STAMgene homolog is in a tight gene cluster, and its expression correlates to that of the adjacent gene ial
    • Mesilaty-Gross, S., A. Reich, B. Motro, and R. Wides. 1999. The Drosophila STAMgene homolog is in a tight gene cluster, and its expression correlates to that of the adjacent gene ial. Gene. 231: 173-186.
    • (1999) Gene , vol.231 , pp. 173-186
    • Mesilaty-Gross, S.1    Reich, A.2    Motro, B.3    Wides, R.4
  • 51
    • 0033012819 scopus 로고    scopus 로고
    • The DHHC domain: A new highly conserved cysteine-rich motif
    • Putilina, T., P. Wong, and S. Gentleman. 1999. The DHHC domain: a new highly conserved cysteine-rich motif. Mol. Cell. Biochem. 195: 219-226.
    • (1999) Mol. Cell. Biochem. , vol.195 , pp. 219-226
    • Putilina, T.1    Wong, P.2    Gentleman, S.3
  • 52
    • 0039445009 scopus 로고    scopus 로고
    • Variations of the C2H2 zinc finger motif in the yeast genome and classification of yeast zinc finger proteins
    • Bohm, S., D. Frishman, and H. W. Mewes. 1997. Variations of the C2H2 zinc finger motif in the yeast genome and classification of yeast zinc finger proteins. Nucleic Acids Res. 25: 2464-2469.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2464-2469
    • Bohm, S.1    Frishman, D.2    Mewes, H.W.3
  • 54
    • 0347064341 scopus 로고    scopus 로고
    • Identification and characterization of GCP16, a novel acylated Golgi protein that interacts with GCP170
    • Ohta, E., Y. Misumi, M. Sohda, T. Fujiwara, A. Yano, and Y. Ikehara. 2003. Identification and characterization of GCP16, a novel acylated Golgi protein that interacts with GCP170. J. Biol. Chem. 278: 51957-51967.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51957-51967
    • Ohta, E.1    Misumi, Y.2    Sohda, M.3    Fujiwara, T.4    Yano, A.5    Ikehara, Y.6
  • 55
    • 25844522857 scopus 로고    scopus 로고
    • Modulation of neuronal protein trafficking and function by palmitoylation
    • Huang, K., and A. El-Husseini. 2005. Modulation of neuronal protein trafficking and function by palmitoylation. Curr. Opin. Neurobiol. 15: 527-535.
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 527-535
    • Huang, K.1    El-Husseini, A.2
  • 59
    • 10444233515 scopus 로고    scopus 로고
    • Greasing transmission: Palmitoylation at the synapse
    • Washbourne, P. 2004. Greasing transmission: palmitoylation at the synapse. Neuron. 44: 901-902.
    • (2004) Neuron , vol.44 , pp. 901-902
    • Washbourne, P.1
  • 61
    • 11244337380 scopus 로고    scopus 로고
    • Huntingtin interacting protein 14 is an oncogenic human protein: Palmitoyl acyltransferase
    • Ducker, C. E., E. M. Stettler, K. J. French, J. J. Upson, and C. D. Smith. 2004. Huntingtin interacting protein 14 is an oncogenic human protein: palmitoyl acyltransferase. Oncogene. 23: 9230-9237.
    • (2004) Oncogene , vol.23 , pp. 9230-9237
    • Ducker, C.E.1    Stettler, E.M.2    French, K.J.3    Upson, J.J.4    Smith, C.D.5
  • 63
    • 23944433700 scopus 로고    scopus 로고
    • Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites
    • Hayashi, T., G. Rumbaugh, and R. L. Huganir. 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
  • 64
    • 0029616578 scopus 로고
    • Mutagenesis of palmitoylation sites in endothelial nitric oxide synthase identifies a novel motif for dual acylation and subcellular targeting
    • Robinson, L. J., and T. Michel. 1995. Mutagenesis of palmitoylation sites in endothelial nitric oxide synthase identifies a novel motif for dual acylation and subcellular targeting. Proc. Natl. Acad. Sci. USA. 92: 11776-11780.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11776-11780
    • Robinson, L.J.1    Michel, T.2
  • 65
    • 30844460508 scopus 로고    scopus 로고
    • The TIP GROWTH DEFECTIVE1 S-acyl transferase regulates plant cell growth in Arabidopsis
    • Hemsley, P. A., A. C. Kemp, and C. S. Grierson. 2005. The TIP GROWTH DEFECTIVE1 S-acyl transferase regulates plant cell growth in Arabidopsis. Plant Cell. 17: 2554-2563.
    • (2005) Plant Cell , vol.17 , pp. 2554-2563
    • Hemsley, P.A.1    Kemp, A.C.2    Grierson, C.S.3
  • 67
    • 0027050783 scopus 로고
    • Biochemistry of protein prenylation
    • Casey, P. J. 1992. Biochemistry of protein prenylation. J. Lipid Res. 33: 1731-1740.
    • (1992) J. Lipid Res. , vol.33 , pp. 1731-1740
    • Casey, P.J.1
  • 68
    • 15044352445 scopus 로고    scopus 로고
    • Fatty acylation and prenylation of proteins: What's hot in fat
    • Magee, T., and M. C. Seabra. 2005. Fatty acylation and prenylation of proteins: what's hot in fat. Curr. Opin. Cell Biol. 17: 190-196.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 190-196
    • Magee, T.1    Seabra, M.C.2
  • 69
    • 30844467746 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. Farnesyl transferase inhibitors
    • Basso, A. D., P. Kirschmeier, and W. R. Bishop. 2006. Thematic review series: lipid posttranslational modifications. Farnesyl transferase inhibitors. J. Lipid Res. 47: 15-31.
    • (2006) J. Lipid Res. , vol.47 , pp. 15-31
    • Basso, A.D.1    Kirschmeier, P.2    Bishop, W.R.3
  • 70
    • 33644748133 scopus 로고    scopus 로고
    • Structural biology of protein farnesyltransferase and geranylgeranyltransferase type-I
    • Lane, K. T., and L. S. Beese. 2006. Structural biology of protein farnesyltransferase and geranylgeranyltransferase type-I. J. Lipid Res. 47: 681-699.
    • (2006) J. Lipid Res. , vol.47 , pp. 681-699
    • Lane, K.T.1    Beese, L.S.2
  • 71
    • 0031664339 scopus 로고    scopus 로고
    • Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor
    • Boyartchuk, V. L., and J. Rine. 1998. Roles of prenyl protein proteases in maturation of Saccharomyces cerevisiae a-factor. Genetics. 150: 95-101.
    • (1998) Genetics , vol.150 , pp. 95-101
    • Boyartchuk, V.L.1    Rine, J.2
  • 72
    • 0025764049 scopus 로고
    • The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins
    • Hrycyna, C. A., S. K. Sapperstein, S. Clarke, and S. M. Michaelis. 1991. The Saccharomyces cerevisiae STE14 gene encodes a methyltransferase that mediates C-terminal methylation of a-factor and RAS proteins. EMBO J. 10: 1699-1709.
    • (1991) EMBO J. , vol.10 , pp. 1699-1709
    • Hrycyna, C.A.1    Sapperstein, S.K.2    Clarke, S.3    Michaelis, S.M.4
  • 73
    • 30844434561 scopus 로고    scopus 로고
    • Prelamin A, Zmpste24, misshapen cell nuclei, and progeria - New evidence suggesting that protein farnesylation could be important for disease pathogenesis
    • Young, S. G., L. G. Fong, and S. Michaelis. 2005. Prelamin A, Zmpste24, misshapen cell nuclei, and progeria - new evidence suggesting that protein farnesylation could be important for disease pathogenesis. J. Lipid Res. 46: 2531-2558.
    • (2005) J. Lipid Res. , vol.46 , pp. 2531-2558
    • Young, S.G.1    Fong, L.G.2    Michaelis, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.