메뉴 건너뛰기




Volumn 122, Issue 6, 2009, Pages 867-874

Identification of a palmitoyl acyltransferase required for protein sorting to the flagellar membrane

Author keywords

Acylation; Flagellum; Membrane microdomains; Palmitoylation; Trypanosoma

Indexed keywords

ACYLTRANSFERASE; ASPARTYLHISTIDYLHISTIDYLCYSTEINE CYSTEINE RICH DOMAIN PROTEIN; CALCIUM BINDING PROTEIN; CALFLAGIN PROTEIN; CELL ENZYME; PALMITOYL ACYLTRANSFERASE; PROTEIN; TBPAT7 PROTEIN; UNCLASSIFIED DRUG; BIOTIN; FLAGELLAR CALCIUM BINDING PROTEIN, TRYPANOSOMA CRUZI; FLAGELLAR CALCIUM-BINDING PROTEIN, TRYPANOSOMA CRUZI; MYRISTIC ACID; PROTOZOAL PROTEIN;

EID: 66949128729     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.041764     Document Type: Article
Times cited : (65)

References (44)
  • 1
    • 41649095182 scopus 로고    scopus 로고
    • Intraflagellar transport and functional analysis of genes required for flagellum formation in trypanosomes
    • Absalon, S., Blisnick, T., Kohl, L., Toutirais, G., Dore, G., Julkowska, D., Tavenet, A. and Bastin, P. (2008). Intraflagellar transport and functional analysis of genes required for flagellum formation in trypanosomes. Mol. Biol. Cell 19, 929-944.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 929-944
    • Absalon, S.1    Blisnick, T.2    Kohl, L.3    Toutirais, G.4    Dore, G.5    Julkowska, D.6    Tavenet, A.7    Bastin, P.8
  • 2
    • 0027275067 scopus 로고
    • Molecular cloning and cellular localization of a BiP homologue in Trypanosoma brucei: Divergent ER retention signals in a lower eukaryote
    • Bangs, J. D., Uyetake, L., Brickman, M. J., Balber, A. E. and Boothroyd, J. C. (1993). Molecular cloning and cellular localization of a BiP homologue in Trypanosoma brucei: divergent ER retention signals in a lower eukaryote. J. Cell Sci. 105, 1101-1113.
    • (1993) J. Cell Sci , vol.105 , pp. 1101-1113
    • Bangs, J.D.1    Uyetake, L.2    Brickman, M.J.3    Balber, A.E.4    Boothroyd, J.C.5
  • 3
    • 0014595902 scopus 로고
    • Interactions of lipids with a membrane structural protein from myelin
    • Braun, P. E. and Radin, N. S. (1969). Interactions of lipids with a membrane structural protein from myelin. Biochemistry 8, 4310-4318.
    • (1969) Biochemistry , vol.8 , pp. 4310-4318
    • Braun, P.E.1    Radin, N.S.2
  • 4
    • 0033103971 scopus 로고    scopus 로고
    • Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs
    • Craven, S. E., El-Husseini, A. E. and Bredt, D. S. (1999). Synaptic targeting of the postsynaptic density protein PSD-95 mediated by lipid and protein motifs. Neuron 22, 497-509.
    • (1999) Neuron , vol.22 , pp. 497-509
    • Craven, S.E.1    El-Husseini, A.E.2    Bredt, D.S.3
  • 5
    • 33750444557 scopus 로고    scopus 로고
    • Trypanosome IFT mutants provide insight into the motor location for mobility of the flagella connector and flagellar membrane formation
    • Davidge, J. A., Chambers, E., Dickinson, H. A., Towers, K., Ginger, M. L., McKean, P. G. and Gull, K. (2006). Trypanosome IFT mutants provide insight into the motor location for mobility of the flagella connector and flagellar membrane formation. J. Cell Sci. 119, 3935-3943.
    • (2006) J. Cell Sci , vol.119 , pp. 3935-3943
    • Davidge, J.A.1    Chambers, E.2    Dickinson, H.A.3    Towers, K.4    Ginger, M.L.5    McKean, P.G.6    Gull, K.7
  • 6
    • 0035976907 scopus 로고    scopus 로고
    • Polarized targeting of peripheral membrane proteins in neurons
    • El-Husseini Ael, D., Craven, S. E., Brock, S. C. and Bredt, D. S. (2001). Polarized targeting of peripheral membrane proteins in neurons. J. Biol. Chem. 276, 44984-44992.
    • (2001) J. Biol. Chem , vol.276 , pp. 44984-44992
    • El-Husseini Ael, D.1    Craven, S.E.2    Brock, S.C.3    Bredt, D.S.4
  • 7
    • 0035955697 scopus 로고    scopus 로고
    • The biology and enzymology of protein N-myristoylation
    • Farazi, T. A., Waksman, G. and Gordon, J. I. (2001). The biology and enzymology of protein N-myristoylation. J. Biol. Chem. 276, 39501-39504.
    • (2001) J. Biol. Chem , vol.276 , pp. 39501-39504
    • Farazi, T.A.1    Waksman, G.2    Gordon, J.I.3
  • 8
    • 40949155069 scopus 로고    scopus 로고
    • Sphingolipid synthesis is necessary for kinetoplast segregation and cytokinesis in Trypanosoma brucei
    • Fridberg, A., Olson, C. L., Nakayasu, E. S., Tyler, K. M., Almeida, I. C. and Engman, D. M. (2008). Sphingolipid synthesis is necessary for kinetoplast segregation and cytokinesis in Trypanosoma brucei. J. Cell Sci. 121, 522-535.
    • (2008) J. Cell Sci , vol.121 , pp. 522-535
    • Fridberg, A.1    Olson, C.L.2    Nakayasu, E.S.3    Tyler, K.M.4    Almeida, I.C.5    Engman, D.M.6
  • 9
    • 0034010126 scopus 로고    scopus 로고
    • A novel phosphatidylinositol-phospholipase C of Trypanosoma cruzi that is lipid modified and activated during trypomastigote to amastigote differentiation
    • Furuya, T., Kashuba, C., Docampo, R. and Moreno, S. N. (2000). A novel phosphatidylinositol-phospholipase C of Trypanosoma cruzi that is lipid modified and activated during trypomastigote to amastigote differentiation. J. Biol. Chem. 275, 6428-6438.
    • (2000) J. Biol. Chem , vol.275 , pp. 6428-6438
    • Furuya, T.1    Kashuba, C.2    Docampo, R.3    Moreno, S.N.4
  • 10
    • 0033560770 scopus 로고    scopus 로고
    • Flagellar protein localization mediated by a calcium-myristoyl/palmitoyl switch mechanism
    • Godsel, L. M. and Engman, D. M. (1999). Flagellar protein localization mediated by a calcium-myristoyl/palmitoyl switch mechanism. EMBO J. 18, 2057-2065.
    • (1999) EMBO J , vol.18 , pp. 2057-2065
    • Godsel, L.M.1    Engman, D.M.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
    • 0034895593 scopus 로고    scopus 로고
    • CAP5.5, a life-cycle-regulated, cytoskeleton-associated protein is a member of a novel family of calpain-related proteins in Trypanosoma brucei
    • Hertz-Fowler, C., Ersfeld, K. and Gull, K. (2001). CAP5.5, a life-cycle-regulated, cytoskeleton-associated protein is a member of a novel family of calpain-related proteins in Trypanosoma brucei. Mol. Biochem. Parasitol. 116, 25-34.
    • (2001) Mol. Biochem. Parasitol , vol.116 , pp. 25-34
    • Hertz-Fowler, C.1    Ersfeld, K.2    Gull, K.3
  • 14
    • 0004966285 scopus 로고
    • Lipids of ciliary and flagellar membranes
    • ed. R. A. Bloodgood, pp, New York: Plenum Press
    • Kaneshiro, E. S. (1990). Lipids of ciliary and flagellar membranes. In Ciliary and Flagellar Membranes (ed. R. A. Bloodgood), pp. 241-265. New York: Plenum Press.
    • (1990) Ciliary and Flagellar Membranes , pp. 241-265
    • Kaneshiro, E.S.1
  • 15
    • 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
  • 16
    • 24644487690 scopus 로고    scopus 로고
    • The flagellum of trypanosomes
    • Kohl, L. and Bastin, P. (2005). The flagellum of trypanosomes. Int. Rev. Cytol. 244, 227-285.
    • (2005) Int. Rev. Cytol , vol.244 , pp. 227-285
    • Kohl, L.1    Bastin, P.2
  • 18
    • 0029585763 scopus 로고
    • The Chlamydomonas kinesin-like protein FLA10 is involved in motility associated with the flagellar membrane
    • Kozminski, K. G., Beech, P. L. and Rosenbaum, J. L. (1995). The Chlamydomonas kinesin-like protein FLA10 is involved in motility associated with the flagellar membrane. J. Cell Biol. 131, 1517-1527.
    • (1995) J. Cell Biol , vol.131 , pp. 1517-1527
    • Kozminski, K.G.1    Beech, P.L.2    Rosenbaum, J.L.3
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0027262263 scopus 로고
    • Rapid isolation of DNA from trypanosomatid protozoa using a simple 'mini-prep' procedure
    • Medina-Acosta, E. and Cross, G. A. (1993). Rapid isolation of DNA from trypanosomatid protozoa using a simple 'mini-prep' procedure. Mol. Biochem. Parasitol. 59, 327-329.
    • (1993) Mol. Biochem. Parasitol , vol.59 , pp. 327-329
    • Medina-Acosta, E.1    Cross, G.A.2
  • 22
    • 33846227881 scopus 로고    scopus 로고
    • Kinetoplastid PPEF phosphatases: Dual acylated proteins expressed in the endomembrane system of Leishmania
    • Mills, E., Price, H. P., Johner, A., Emerson, J. E. and Smith, D. F. (2007). Kinetoplastid PPEF phosphatases: dual acylated proteins expressed in the endomembrane system of Leishmania. Mol. Biochem. Parasitol. 152, 22-34.
    • (2007) Mol. Biochem. Parasitol , vol.152 , pp. 22-34
    • Mills, E.1    Price, H.P.2    Johner, A.3    Emerson, J.E.4    Smith, D.F.5
  • 23
    • 33744826797 scopus 로고    scopus 로고
    • Protein palmitoylation by a family of DHHC protein S-acyltransferases
    • Mitchell, D. A., Vasudevan, A., Linder, M. E. and Deschenes, R. J. (2006). Protein palmitoylation 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
  • 24
    • 0032580320 scopus 로고    scopus 로고
    • Two-sided confidence intervals for the single proportion: Comparison of seven methods
    • Newcombe, R. G. (1998). Two-sided confidence intervals for the single proportion: comparison of seven methods. Stat. Med. 17, 857-872.
    • (1998) Stat. Med , vol.17 , pp. 857-872
    • Newcombe, R.G.1
  • 25
    • 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. and Igarashi, Y. (2006). Intracellular localization and tissue-specific distribution of human and yeast DHHC cysteine-rich domain-containing proteins. Biochim. Biophys. Acta 1761, 474-483.
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 474-483
    • Ohno, Y.1    Kihara, A.2    Sano, T.3    Igarashi, Y.4
  • 26
    • 18144423507 scopus 로고    scopus 로고
    • A lipid-modified phosphoinositide-specific phospholipase C (TcPI-PLC) is involved in differentiation of trypomastigotes to amastigotes of Trypanosoma cruzi
    • Okura, M., Fang, J., Salto, M. L., Singer, R. S., Docampo, R. and Moreno, S. N. (2005). A lipid-modified phosphoinositide-specific phospholipase C (TcPI-PLC) is involved in differentiation of trypomastigotes to amastigotes of Trypanosoma cruzi. J. Biol. Chem. 280, 16235-16243.
    • (2005) J. Biol. Chem , vol.280 , pp. 16235-16243
    • Okura, M.1    Fang, J.2    Salto, M.L.3    Singer, R.S.4    Docampo, R.5    Moreno, S.N.6
  • 28
    • 24944555725 scopus 로고    scopus 로고
    • Intraflagellar transport is required for the vectorial movement of TRPV channels in the ciliary membrane
    • Qin, H., Burnette, D. T., Bae, Y. K., Forscher, P., Barr, M. M. and Rosenbaum, J. L. (2005). Intraflagellar transport is required for the vectorial movement of TRPV channels in the ciliary membrane. Curr. Biol. 15, 1695-1699.
    • (2005) Curr. Biol , vol.15 , pp. 1695-1699
    • Qin, H.1    Burnette, D.T.2    Bae, Y.K.3    Forscher, P.4    Barr, M.M.5    Rosenbaum, J.L.6
  • 29
    • 0037466382 scopus 로고    scopus 로고
    • RNAit: An automated web-based tool for the selection of RNAi targets in Trypanosoma brucei
    • Redmond, S., Vadivelu, J. and Field, M. C. (2003). RNAit: an automated web-based tool for the selection of RNAi targets in Trypanosoma brucei. Mol. Biochem. Parasitol. 128, 115-118.
    • (2003) Mol. Biochem. Parasitol , vol.128 , pp. 115-118
    • Redmond, S.1    Vadivelu, J.2    Field, M.C.3
  • 31
    • 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
  • 34
    • 0022857138 scopus 로고
    • Freeze-fracture studies on the surface membranes of pleomorphic bloodstream and in vitro transformed procyclic Trypanosoma brucei
    • Tetley, L. (1986). Freeze-fracture studies on the surface membranes of pleomorphic bloodstream and in vitro transformed procyclic Trypanosoma brucei. Acta Trop. 43, 307-317.
    • (1986) Acta Trop , vol.43 , pp. 307-317
    • Tetley, L.1
  • 35
  • 37
    • 34447115260 scopus 로고    scopus 로고
    • Palmitoylated proteins: Purification and identification
    • Wan, J., Roth, A. F., Bailey, A. O. and Davis, N. G. (2007). Palmitoylated proteins: purification and identification. Nat. Protoc. 2, 1573-1584.
    • (2007) Nat. Protoc , vol.2 , pp. 1573-1584
    • Wan, J.1    Roth, A.F.2    Bailey, A.O.3    Davis, N.G.4
  • 38
    • 0034704084 scopus 로고    scopus 로고
    • Inhibition of Trypanosoma brucei gene expression by RNA interference using an integratable vector with opposing T7 promoters
    • Wang, Z., Morris, J. C., Drew, M. E. and Englund, P. T. (2000). Inhibition of Trypanosoma brucei gene expression by RNA interference using an integratable vector with opposing T7 promoters. J. Biol. Chem. 275, 40174-40179.
    • (2000) J. Biol. Chem , vol.275 , pp. 40174-40179
    • Wang, Z.1    Morris, J.C.2    Drew, M.E.3    Englund, P.T.4
  • 39
    • 0021355340 scopus 로고
    • A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids
    • Wessel, D. and Flugge, U. I. (1984). A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal. Biochem. 138, 141-143.
    • (1984) Anal. Biochem , vol.138 , pp. 141-143
    • Wessel, D.1    Flugge, U.I.2
  • 40
    • 0033525524 scopus 로고    scopus 로고
    • A tightly regulated inducible expression system for conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei
    • Wirtz, E., Leal, S., Ochatt, C. and Cross, G. A. (1999). A tightly regulated inducible expression system for conditional gene knock-outs and dominant-negative genetics in Trypanosoma brucei. Mol. Biochem. Parasitol. 99, 89-101.
    • (1999) Mol. Biochem. Parasitol , vol.99 , pp. 89-101
    • Wirtz, E.1    Leal, S.2    Ochatt, C.3    Cross, G.A.4
  • 41
    • 0024369960 scopus 로고
    • Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies
    • Woods, A., Sherwin, T., Sasse, R., MacRae, T. H., Baines, A. J. and Gull, K. (1989). Definition of individual components within the cytoskeleton of Trypanosoma brucei by a library of monoclonal antibodies. J. Cell Sci. 93, 491-500.
    • (1989) J. Cell Sci , vol.93 , pp. 491-500
    • Woods, A.1    Sherwin, T.2    Sasse, R.3    MacRae, T.H.4    Baines, A.J.5    Gull, K.6
  • 42
    • 0027102657 scopus 로고
    • A high molecular mass phosphoprotein defined by a novel monoclonal antibody is closely associated with the intermicrotubule cross bridges in the Trypanosoma brucei cytoskeleton
    • Woods, A., Baines, A. J. and Gull, K. (1992). A high molecular mass phosphoprotein defined by a novel monoclonal antibody is closely associated with the intermicrotubule cross bridges in the Trypanosoma brucei cytoskeleton. J. Cell Sci. 103, 665-675.
    • (1992) J. Cell Sci , vol.103 , pp. 665-675
    • Woods, A.1    Baines, A.J.2    Gull, K.3
  • 43
    • 0026793533 scopus 로고
    • The predominant calcimedins from Trypanosoma brucei comprise a family of flagellar EF-hand calcium-binding proteins
    • Wu, Y., Haghighat, N. G. and Ruben, L. (1992). The predominant calcimedins from Trypanosoma brucei comprise a family of flagellar EF-hand calcium-binding proteins. Biochem. J. 287, 187-193.
    • (1992) Biochem. J , vol.287 , pp. 187-193
    • Wu, Y.1    Haghighat, N.G.2    Ruben, L.3
  • 44
    • 0028593503 scopus 로고
    • The gene family of EF-hand calcium-binding proteins from the flagellum of Trypanosoma brucei
    • Wu, Y., Deford, J., Benjamin, R., Lee, M. G. and Ruben, L. (1994). The gene family of EF-hand calcium-binding proteins from the flagellum of Trypanosoma brucei. Biochem. J. 304, 833-841.
    • (1994) Biochem. J , vol.304 , pp. 833-841
    • Wu, Y.1    Deford, J.2    Benjamin, R.3    Lee, M.G.4    Ruben, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.