메뉴 건너뛰기




Volumn 175, Issue 2, 2011, Pages 162-168

Evidence for prenylation-dependent targeting of a Ykt6 SNARE in Plasmodium falciparum

Author keywords

Plasmodium falciparum; Prenylation; Protein trafficking; SNARE; Ykt6

Indexed keywords

PROTEIN FARNESYLTRANSFERASE; PROTEIN YKT6; SNARE PROTEIN; UNCLASSIFIED DRUG;

EID: 78650306655     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2010.11.007     Document Type: Article
Times cited : (18)

References (54)
  • 1
    • 20444407298 scopus 로고    scopus 로고
    • SNAREs and traffic
    • W. Hong SNAREs and traffic Biochim Biophys Acta 1744 2005 120 144
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 120-144
    • Hong, W.1
  • 2
    • 33747622293 scopus 로고    scopus 로고
    • SNAREs - Engines for membrane fusion
    • R. Jahn, and R.H. Scheller SNAREs - engines for membrane fusion Nat Rev Mol Cell Biol 7 2006 631 643
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 631-643
    • Jahn, R.1    Scheller, R.H.2
  • 3
    • 0035279058 scopus 로고    scopus 로고
    • SNAREs and the specificity of membrane fusion
    • H.R. Pelham SNAREs and the specificity of membrane fusion Trends Cell Biol 11 2001 99 101
    • (2001) Trends Cell Biol , vol.11 , pp. 99-101
    • Pelham, H.R.1
  • 5
    • 0036786921 scopus 로고    scopus 로고
    • Tail-anchored protein insertion into yeast ER requires a novel posttranslational mechanism which is independent of the SEC machinery
    • G.J. Steel, J. Brownsword, and C.J. Stirling Tail-anchored protein insertion into yeast ER requires a novel posttranslational mechanism which is independent of the SEC machinery Biochemistry 41 2002 11914 11920
    • (2002) Biochemistry , vol.41 , pp. 11914-11920
    • Steel, G.J.1    Brownsword, J.2    Stirling, C.J.3
  • 6
    • 33947218544 scopus 로고    scopus 로고
    • Identification of a targeting factor for posttranslational membrane protein insertion into the ER
    • S. Stefanovic, and R.S. Hegde Identification of a targeting factor for posttranslational membrane protein insertion into the ER Cell 128 2007 1147 1159
    • (2007) Cell , vol.128 , pp. 1147-1159
    • Stefanovic, S.1    Hegde, R.S.2
  • 7
    • 34250183921 scopus 로고    scopus 로고
    • Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones
    • B.M. Abell, C. Rabu, P. Leznicki, J.C. Young, and S. High Post-translational integration of tail-anchored proteins is facilitated by defined molecular chaperones J Cell Sci 120 2007 1743 1751
    • (2007) J Cell Sci , vol.120 , pp. 1743-1751
    • Abell, B.M.1    Rabu, C.2    Leznicki, P.3    Young, J.C.4    High, S.5
  • 8
    • 34547937485 scopus 로고    scopus 로고
    • How tails guide tail-anchored proteins to their destinations
    • N. Borgese, S. Brambillasca, and S. Colombo How tails guide tail-anchored proteins to their destinations Curr Opin Cell Biol 19 2007 368 375
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 368-375
    • Borgese, N.1    Brambillasca, S.2    Colombo, S.3
  • 9
    • 0035102443 scopus 로고    scopus 로고
    • Targeting of C-terminal (tail)-anchored proteins: Understanding how cytoplasmic activities are anchored to intracellular membranes
    • B. Wattenberg, and T. Lithgow Targeting of C-terminal (tail)-anchored proteins: understanding how cytoplasmic activities are anchored to intracellular membranes Traffic 2 2001 66 71
    • (2001) Traffic , vol.2 , pp. 66-71
    • Wattenberg, B.1    Lithgow, T.2
  • 10
    • 0027997974 scopus 로고
    • Localization of Sed5, a putative vesicle targeting molecule, to the cis-Golgi network involves both its transmembrane and cytoplasmic domains
    • D.K. Banfield, M.J. Lewis, C. Rabouille, G. Warren, and H.R. Pelham Localization of Sed5, a putative vesicle targeting molecule, to the cis-Golgi network involves both its transmembrane and cytoplasmic domains J Cell Biol 127 1994 357 371
    • (1994) J Cell Biol , vol.127 , pp. 357-371
    • Banfield, D.K.1    Lewis, M.J.2    Rabouille, C.3    Warren, G.4    Pelham, H.R.5
  • 11
    • 1842636943 scopus 로고    scopus 로고
    • Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation
    • M. Fukasawa, O. Varlamov, W.S. Eng, T.H. Sollner, and J.E. Rothman Localization and activity of the SNARE Ykt6 determined by its regulatory domain and palmitoylation Proc Natl Acad Sci USA 101 2004 4815 4820
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4815-4820
    • Fukasawa, M.1    Varlamov, O.2    Eng, W.S.3    Sollner, T.H.4    Rothman, J.E.5
  • 12
    • 0030814115 scopus 로고    scopus 로고
    • Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi transport
    • J.A. McNew, M. Sogaard, and N.M. Lampen Ykt6p, a prenylated SNARE essential for endoplasmic reticulum-Golgi transport J Biol Chem 272 1997 17776 17783
    • (1997) J Biol Chem , vol.272 , pp. 17776-17783
    • McNew, J.A.1    Sogaard, M.2    Lampen, N.M.3
  • 13
    • 49749148054 scopus 로고    scopus 로고
    • Depalmitoylation of Ykt6 prevents its entry into the multivesicular body pathway
    • C.T. Meiringer, K. Auffarth, H. Hou, and C. Ungermann Depalmitoylation of Ykt6 prevents its entry into the multivesicular body pathway Traffic 9 2008 1510 1521
    • (2008) Traffic , vol.9 , pp. 1510-1521
    • Meiringer, C.T.1    Auffarth, K.2    Hou, H.3    Ungermann, C.4
  • 15
    • 33646777423 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. CAAX modification and membrane targeting of Ras
    • L.P. Wright, and M.R. Philips Thematic review series: lipid posttranslational modifications. CAAX modification and membrane targeting of Ras J Lipid Res 47 2006 883 891
    • (2006) J Lipid Res , vol.47 , pp. 883-891
    • Wright, L.P.1    Philips, M.R.2
  • 16
    • 15044352445 scopus 로고    scopus 로고
    • Fatty acylation and prenylation of proteins: What's hot in fat
    • T. Magee, and M.C. Seabra Fatty acylation and prenylation of proteins: what's hot in fat Curr Opin Cell Biol 17 2005 190 196
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 190-196
    • Magee, T.1    Seabra, M.C.2
  • 17
    • 33750266831 scopus 로고    scopus 로고
    • Trafficking and signaling by fatty-acylated and prenylated proteins
    • M.D. Resh Trafficking and signaling by fatty-acylated and prenylated proteins Nat Chem Biol 2 2006 584 590
    • (2006) Nat Chem Biol , vol.2 , pp. 584-590
    • Resh, M.D.1
  • 18
    • 16344396081 scopus 로고    scopus 로고
    • Postprenylation CAAX processing is required for proper localization of Ras but not Rho GTPases
    • D. Michaelson, W. Ali, and V.K. Chiu Postprenylation CAAX processing is required for proper localization of Ras but not Rho GTPases Mol Biol Cell 16 2005 1606 1616
    • (2005) Mol Biol Cell , vol.16 , pp. 1606-1616
    • Michaelson, D.1    Ali, W.2    Chiu, V.K.3
  • 19
    • 0344721502 scopus 로고    scopus 로고
    • Lipid modifications of proteins - Slipping in and out of membranes
    • S. Yalovsky, M. Rodr Guez-Concepcion, and W. Gruissem Lipid modifications of proteins - slipping in and out of membranes Trends Plant Sci 4 1999 439 445
    • (1999) Trends Plant Sci , vol.4 , pp. 439-445
    • Yalovsky, S.1    Rodr Guez-Concepcion, M.2    Gruissem, W.3
  • 20
    • 34347218222 scopus 로고    scopus 로고
    • Protein isoprenylation in biology and disease: General overview and perspectives from studies with genetically engineered animals
    • D. Perez-Sala Protein isoprenylation in biology and disease: general overview and perspectives from studies with genetically engineered animals Front Biosci 12 2007 4456 4472
    • (2007) Front Biosci , vol.12 , pp. 4456-4472
    • Perez-Sala, D.1
  • 21
    • 0033538559 scopus 로고    scopus 로고
    • Endomembrane trafficking of ras: The CAAX motif targets proteins to the ER and Golgi
    • E. Choy, V.K. Chiu, and J. Silletti Endomembrane trafficking of ras: the CAAX motif targets proteins to the ER and Golgi Cell 98 1999 69 80
    • (1999) Cell , vol.98 , pp. 69-80
    • Choy, E.1    Chiu, V.K.2    Silletti, J.3
  • 22
    • 0026353346 scopus 로고
    • Sequence dependence of protein isoprenylation
    • S.L. Moores, M.D. Schaber, and S.D. Mosser Sequence dependence of protein isoprenylation J Biol Chem 266 1991 14603 14610
    • (1991) J Biol Chem , vol.266 , pp. 14603-14610
    • Moores, S.L.1    Schaber, M.D.2    Mosser, S.D.3
  • 23
    • 0034525357 scopus 로고    scopus 로고
    • The Arabidopsis genome. An abundance of soluble N-ethylmaleimide- sensitive factor adaptor protein receptors
    • A.A. Sanderfoot, F.F. Assaad, and N.V. Raikhel The Arabidopsis genome. An abundance of soluble N-ethylmaleimide-sensitive factor adaptor protein receptors Plant Physiol 124 2000 1558 1569
    • (2000) Plant Physiol , vol.124 , pp. 1558-1569
    • Sanderfoot, A.A.1    Assaad, F.F.2    Raikhel, N.V.3
  • 25
    • 7444236944 scopus 로고    scopus 로고
    • Protein trafficking in Plasmodium falciparum-infected red blood cells
    • B.M. Cooke, K. Lingelbach, L.H. Bannister, and L. Tilley Protein trafficking in Plasmodium falciparum-infected red blood cells Trends Parasitol 20 2004 581 589
    • (2004) Trends Parasitol , vol.20 , pp. 581-589
    • Cooke, B.M.1    Lingelbach, K.2    Bannister, L.H.3    Tilley, L.4
  • 26
    • 17144386621 scopus 로고    scopus 로고
    • Protein transport and trafficking in Plasmodium falciparum-infected erythrocytes
    • DOI 10.1017/S0031182004006729
    • J.M. Przyborski, and M. Lanzer Protein transport and trafficking in Plasmodium falciparum-infected erythrocytes Parasitology 130 2005 373 388 (Pubitemid 40516287)
    • (2005) Parasitology , vol.130 , Issue.4 , pp. 373-388
    • Przyborski, J.M.1    Lanzer, M.2
  • 27
    • 0034818888 scopus 로고    scopus 로고
    • Vesicle-mediated trafficking of parasite proteins to the host cell cytosol and erythrocyte surface membrane in Plasmodium falciparum infected erythrocytes
    • T.F. Taraschi, D. Trelka, S. Martinez, T. Schneider, and M.E. O'Donnell Vesicle-mediated trafficking of parasite proteins to the host cell cytosol and erythrocyte surface membrane in Plasmodium falciparum infected erythrocytes Int J Parasitol 31 2001 1381 1391
    • (2001) Int J Parasitol , vol.31 , pp. 1381-1391
    • Taraschi, T.F.1    Trelka, D.2    Martinez, S.3    Schneider, T.4    O'Donnell, M.E.5
  • 28
    • 38149074832 scopus 로고    scopus 로고
    • Protein transport across the parasitophorous vacuole of Plasmodium falciparum: Into the great wide open
    • S. Charpian, and J.M. Przyborski Protein transport across the parasitophorous vacuole of Plasmodium falciparum: into the great wide open Traffic 9 2008 157 165
    • (2008) Traffic , vol.9 , pp. 157-165
    • Charpian, S.1    Przyborski, J.M.2
  • 29
    • 0036319221 scopus 로고    scopus 로고
    • Protein and lipid trafficking induced in erythrocytes infected by malaria parasites
    • K. Haldar, N. Mohandas, and B.U. Samuel Protein and lipid trafficking induced in erythrocytes infected by malaria parasites Cell Microbiol 4 2002 383 395
    • (2002) Cell Microbiol , vol.4 , pp. 383-395
    • Haldar, K.1    Mohandas, N.2    Samuel, B.U.3
  • 30
    • 38649133377 scopus 로고    scopus 로고
    • Characterization of a PRL protein tyrosine phosphatase from Plasmodium falciparum
    • P.R. Pendyala, L. Ayong, and J. Eatrides Characterization of a PRL protein tyrosine phosphatase from Plasmodium falciparum Mol Biochem Parasitol 158 2008 1 10
    • (2008) Mol Biochem Parasitol , vol.158 , pp. 1-10
    • Pendyala, P.R.1    Ayong, L.2    Eatrides, J.3
  • 32
    • 0032407858 scopus 로고    scopus 로고
    • Cycloguanil and its parent compound proguanil demonstrate distinct activities against Plasmodium falciparum malaria parasites transformed with human dihydrofolate reductase
    • D.A. Fidock, T. Nomura, and T.E. Wellems Cycloguanil and its parent compound proguanil demonstrate distinct activities against Plasmodium falciparum malaria parasites transformed with human dihydrofolate reductase Mol Pharmacol 54 1998 1140 1147
    • (1998) Mol Pharmacol , vol.54 , pp. 1140-1147
    • Fidock, D.A.1    Nomura, T.2    Wellems, T.E.3
  • 33
    • 44249122262 scopus 로고    scopus 로고
    • Plasmodium falciparum Sec24 marks transitional ER that exports a model cargo via a diacidic motif
    • M.C. Lee, P.A. Moura, E.A. Miller, and D.A. Fidock Plasmodium falciparum Sec24 marks transitional ER that exports a model cargo via a diacidic motif Mol Microbiol 2008
    • (2008) Mol Microbiol
    • Lee, M.C.1    Moura, P.A.2    Miller, E.A.3    Fidock, D.A.4
  • 35
    • 0344052673 scopus 로고    scopus 로고
    • Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion
    • C. Ungermann, G.F. von Mollard, O.N. Jensen, N. Margolis, T.H. Stevens, and W. Wickner Three v-SNAREs and two t-SNAREs, present in a pentameric cis-SNARE complex on isolated vacuoles, are essential for homotypic fusion J Cell Biol 145 1999 1435 1442
    • (1999) J Cell Biol , vol.145 , pp. 1435-1442
    • Ungermann, C.1    Von Mollard, G.F.2    Jensen, O.N.3    Margolis, N.4    Stevens, T.H.5    Wickner, W.6
  • 36
    • 0037572294 scopus 로고    scopus 로고
    • Ykt6p is a multifunctional yeast R-SNARE that is required for multiple membrane transport pathways to the vacuole
    • Y. Kweon, A. Rothe, E. Conibear, and T.H. Stevens Ykt6p is a multifunctional yeast R-SNARE that is required for multiple membrane transport pathways to the vacuole Mol Biol Cell 14 2003 1868 1881
    • (2003) Mol Biol Cell , vol.14 , pp. 1868-1881
    • Kweon, Y.1    Rothe, A.2    Conibear, E.3    Stevens, T.H.4
  • 37
    • 0037323502 scopus 로고    scopus 로고
    • Mammalian ykt6 is a neuronal SNARE targeted to a specialized compartment by its profilin-like amino terminal domain
    • H. Hasegawa, S. Zinsser, Y. Rhee, E.O. Vik-Mo, S. Davanger, and J.C. Hay Mammalian ykt6 is a neuronal SNARE targeted to a specialized compartment by its profilin-like amino terminal domain Mol Biol Cell 14 2003 698 720
    • (2003) Mol Biol Cell , vol.14 , pp. 698-720
    • Hasegawa, H.1    Zinsser, S.2    Rhee, Y.3    Vik-Mo, E.O.4    Davanger, S.5    Hay, J.C.6
  • 38
    • 0036829078 scopus 로고    scopus 로고
    • Protein farnesyltransferase and protein prenylation in Plasmodium falciparum
    • D. Chakrabarti, T. Da Silva, and J. Barger Protein farnesyltransferase and protein prenylation in Plasmodium falciparum J Biol Chem 277 2002 42066 42073
    • (2002) J Biol Chem , vol.277 , pp. 42066-42073
    • Chakrabarti, D.1    Da Silva, T.2    Barger, J.3
  • 40
    • 0035920124 scopus 로고    scopus 로고
    • Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport
    • T. Zhang, and W. Hong Ykt6 forms a SNARE complex with syntaxin 5, GS28, and Bet1 and participates in a late stage in endoplasmic reticulum-Golgi transport J Biol Chem 276 2001 27480 27487
    • (2001) J Biol Chem , vol.276 , pp. 27480-27487
    • Zhang, T.1    Hong, W.2
  • 41
    • 12144290286 scopus 로고    scopus 로고
    • Countercurrent distribution of two distinct SNARE complexes mediating transport within the Golgi stack
    • A. Volchuk, M. Ravazzola, and A. Perrelet Countercurrent distribution of two distinct SNARE complexes mediating transport within the Golgi stack Mol Biol Cell 15 2004 1506 1518
    • (2004) Mol Biol Cell , vol.15 , pp. 1506-1518
    • Volchuk, A.1    Ravazzola, M.2    Perrelet, A.3
  • 42
    • 20444418161 scopus 로고    scopus 로고
    • YKT6 is a core constituent of membrane fusion machineries at the Arabidopsis trans-Golgi network
    • Y. Chen, Y.K. Shin, and D.C. Bassham YKT6 is a core constituent of membrane fusion machineries at the Arabidopsis trans-Golgi network J Mol Biol 350 2005 92 101
    • (2005) J Mol Biol , vol.350 , pp. 92-101
    • Chen, Y.1    Shin, Y.K.2    Bassham, D.C.3
  • 43
    • 40849097419 scopus 로고    scopus 로고
    • Farnesylation of the SNARE protein Ykt6 increases its stability and helical folding
    • O. Pylypenko, A. Schonichen, and D. Ludwig Farnesylation of the SNARE protein Ykt6 increases its stability and helical folding J Mol Biol 377 2008 1334 1345
    • (2008) J Mol Biol , vol.377 , pp. 1334-1345
    • Pylypenko, O.1    Schonichen, A.2    Ludwig, D.3
  • 44
  • 45
    • 47349089381 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors: A detailed chemical view on an elusive biological problem
    • S.F. Sousa, P.A. Fernandes, and M.J. Ramos Farnesyltransferase inhibitors: a detailed chemical view on an elusive biological problem Curr Med Chem 15 2008 1478 1492
    • (2008) Curr Med Chem , vol.15 , pp. 1478-1492
    • Sousa, S.F.1    Fernandes, P.A.2    Ramos, M.J.3
  • 46
    • 0034722890 scopus 로고    scopus 로고
    • Farnesyltransferase and geranylgeranyltransferase i inhibitors and cancer therapy: Lessons from mechanism and bench-to-bedside translational studies
    • S.M. Sebti, and A.D. Hamilton Farnesyltransferase and geranylgeranyltransferase I inhibitors and cancer therapy: lessons from mechanism and bench-to-bedside translational studies Oncogene 19 2000 6584 6593
    • (2000) Oncogene , vol.19 , pp. 6584-6593
    • Sebti, S.M.1    Hamilton, A.D.2
  • 47
    • 0025829655 scopus 로고
    • Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product
    • A.A. Finegold, D.I. Johnson, and C.C. Farnsworth Protein geranylgeranyltransferase of Saccharomyces cerevisiae is specific for Cys-Xaa-Xaa-Leu motif proteins and requires the CDC43 gene product but not the DPR1 gene product Proc Natl Acad Sci USA 88 1991 4448 4452
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4448-4452
    • Finegold, A.A.1    Johnson, D.I.2    Farnsworth, C.C.3
  • 48
    • 0026001936 scopus 로고
    • A protein geranylgeranyltransferase from bovine brain: Implications for protein prenylation specificity
    • K. Yokoyama, G.W. Goodwin, F. Ghomashchi, J.A. Glomset, and M.H. Gelb A protein geranylgeranyltransferase from bovine brain: implications for protein prenylation specificity Proc Natl Acad Sci USA 88 1991 5302 5306
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5302-5306
    • Yokoyama, K.1    Goodwin, G.W.2    Ghomashchi, F.3    Glomset, J.A.4    Gelb, M.H.5
  • 49
    • 20144373679 scopus 로고    scopus 로고
    • Protein farnesyltransferase inhibitors exhibit potent antimalarial activity
    • L. Nallan, K.D. Bauer, and P. Bendale Protein farnesyltransferase inhibitors exhibit potent antimalarial activity J Med Chem 48 2005 3704 3713
    • (2005) J Med Chem , vol.48 , pp. 3704-3713
    • Nallan, L.1    Bauer, K.D.2    Bendale, P.3
  • 50
    • 0025277259 scopus 로고
    • Prenyl proteins in eukaryotic cells: A new type of membrane anchor
    • J.A. Glomset, M.H. Gelb, and C.C. Farnsworth Prenyl proteins in eukaryotic cells: a new type of membrane anchor Trends Biochem Sci 15 1990 139 142
    • (1990) Trends Biochem Sci , vol.15 , pp. 139-142
    • Glomset, J.A.1    Gelb, M.H.2    Farnsworth, C.C.3
  • 51
    • 0028170814 scopus 로고
    • Role of protein modification reactions in programming interactions between ras-related GTPases and cell membranes
    • J.A. Glomset, and C.C. Farnsworth Role of protein modification reactions in programming interactions between ras-related GTPases and cell membranes Annu Rev Cell Biol 10 1994 181 205
    • (1994) Annu Rev Cell Biol , vol.10 , pp. 181-205
    • Glomset, J.A.1    Farnsworth, C.C.2
  • 53
    • 0030952552 scopus 로고    scopus 로고
    • Inhibition of the prenylation of K-Ras, but not H- or N-Ras, is highly resistant to CAAX peptidomimetics and requires both a farnesyltransferase and a geranylgeranyltransferase i inhibitor in human tumor cell lines
    • E.C. Lerner, T.T. Zhang, D.B. Knowles, Y. Qian, A.D. Hamilton, and S.M. Sebti Inhibition of the prenylation of K-Ras, but not H- or N-Ras, is highly resistant to CAAX peptidomimetics and requires both a farnesyltransferase and a geranylgeranyltransferase I inhibitor in human tumor cell lines Oncogene 15 1997 1283 1288
    • (1997) Oncogene , vol.15 , pp. 1283-1288
    • Lerner, E.C.1    Zhang, T.T.2    Knowles, D.B.3    Qian, Y.4    Hamilton, A.D.5    Sebti, S.M.6
  • 54
    • 0042355181 scopus 로고    scopus 로고
    • Protein prenyltransferases: Anchor size, pseudogenes and parasites
    • S. Maurer-Stroh, S. Washietl, and F. Eisenhaber Protein prenyltransferases: anchor size, pseudogenes and parasites Biol Chem 384 2003 977 989
    • (2003) Biol Chem , vol.384 , pp. 977-989
    • Maurer-Stroh, S.1    Washietl, S.2    Eisenhaber, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.