메뉴 건너뛰기




Volumn 12, Issue 12, 2011, Pages 1774-1792

Identification of Sorting Motifs of AtβFruct4 for Trafficking from the ER to the Vacuole Through the Golgi and PVC

Author keywords

Arabidopsis; Central vacuole; Membrane protein; Targeting signal sequence; Trafficking of At Fruct4

Indexed keywords

ARABIDOPSIS PROTEIN; FRUCTOSIDASE; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 81055156762     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2011.01276.x     Document Type: Article
Times cited : (17)

References (71)
  • 1
    • 0033693481 scopus 로고    scopus 로고
    • Vacuoles and prevacuolar compartments.
    • Bethke PC, Jones RL. Vacuoles and prevacuolar compartments. Curr Opin Plant Biol 2000;3:469-475.
    • (2000) Curr Opin Plant Biol , vol.3 , pp. 469-475
    • Bethke, P.C.1    Jones, R.L.2
  • 2
    • 0026823307 scopus 로고
    • Sorting of proteins to the vacuoles of plant cells.
    • Vitale A, Chrispeels MJ. Sorting of proteins to the vacuoles of plant cells. Bioessays 1992;14:151-160.
    • (1992) Bioessays , vol.14 , pp. 151-160
    • Vitale, A.1    Chrispeels, M.J.2
  • 3
    • 8444223534 scopus 로고    scopus 로고
    • Membrane trafficking in plants.
    • Jurgens G. Membrane trafficking in plants. Annu Rev Cell Dev Biol 2004;20:481-504.
    • (2004) Annu Rev Cell Dev Biol , vol.20 , pp. 481-504
    • Jurgens, G.1
  • 4
    • 0027597740 scopus 로고
    • Determination of the functional elements within the vacuolar targeting signal of barley lectin.
    • Dombrowski JE, Schroeder MR, Bednarek SY, Raikhel NV. Determination of the functional elements within the vacuolar targeting signal of barley lectin. Plant Cell 1993;5:587-596.
    • (1993) Plant Cell , vol.5 , pp. 587-596
    • Dombrowski, J.E.1    Schroeder, M.R.2    Bednarek, S.Y.3    Raikhel, N.V.4
  • 5
    • 0001600705 scopus 로고
    • In vitro processing of aleurain, a barley vacuolar thiol protease.
    • Holwerda BC, Galvin NJ, Baranski TJ, Rogers JC. In vitro processing of aleurain, a barley vacuolar thiol protease. Plant Cell 1990;2:1091-1106.
    • (1990) Plant Cell , vol.2 , pp. 1091-1106
    • Holwerda, B.C.1    Galvin, N.J.2    Baranski, T.J.3    Rogers, J.C.4
  • 6
    • 0026023554 scopus 로고
    • Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting.
    • Matsuoka K, Nakamura K. Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting. Proc Natl Acad Sci U S A 1991;88:834-838.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 834-838
    • Matsuoka, K.1    Nakamura, K.2
  • 7
    • 0026828751 scopus 로고
    • Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions.
    • Holwerda BC, Padgett HS, Rogers JC. Proaleurain vacuolar targeting is mediated by short contiguous peptide interactions. Plant Cell 1992;4:307-318.
    • (1992) Plant Cell , vol.4 , pp. 307-318
    • Holwerda, B.C.1    Padgett, H.S.2    Rogers, J.C.3
  • 8
    • 0030162062 scopus 로고    scopus 로고
    • Interaction of a potential vacuolar targeting receptor with amino- and carboxyl-terminal targeting determinants.
    • Kirsch T, Saalbach G, Raikhel NV, Beevers L. Interaction of a potential vacuolar targeting receptor with amino- and carboxyl-terminal targeting determinants. Plant Physiol 1996;111:469-474.
    • (1996) Plant Physiol , vol.111 , pp. 469-474
    • Kirsch, T.1    Saalbach, G.2    Raikhel, N.V.3    Beevers, L.4
  • 10
    • 0033709686 scopus 로고    scopus 로고
    • Sorting of soluble proteins in the secretory pathway of plants.
    • Hadlington JL, Denecke J. Sorting of soluble proteins in the secretory pathway of plants. Curr Opin Plant Biol 2000;3:461-468.
    • (2000) Curr Opin Plant Biol , vol.3 , pp. 461-468
    • Hadlington, J.L.1    Denecke, J.2
  • 11
    • 0028201318 scopus 로고
    • Purification and initial characterization of a potential plant vacuolar targeting receptor.
    • Kirsch T, Paris N, Butler JM, Beevers L, Rogers JC. Purification and initial characterization of a potential plant vacuolar targeting receptor. Proc Natl Acad Sci U S A 1994;91:3403-3407.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3403-3407
    • Kirsch, T.1    Paris, N.2    Butler, J.M.3    Beevers, L.4    Rogers, J.C.5
  • 12
    • 0034717573 scopus 로고    scopus 로고
    • The plant vacuolar sorting receptor AtELP is involved in transport of NH(2)-terminal propeptide-containing vacuolar proteins in Arabidopsis thaliana.
    • Ahmed SU, Rojo E, Kovaleva V, Venkataraman S, Dombrowski JE, Matsuoka K, Raikhel NV. The plant vacuolar sorting receptor AtELP is involved in transport of NH(2)-terminal propeptide-containing vacuolar proteins in Arabidopsis thaliana. J Cell Biol 2000;149:1335-1344.
    • (2000) J Cell Biol , vol.149 , pp. 1335-1344
    • Ahmed, S.U.1    Rojo, E.2    Kovaleva, V.3    Venkataraman, S.4    Dombrowski, J.E.5    Matsuoka, K.6    Raikhel, N.V.7
  • 13
    • 0036909278 scopus 로고    scopus 로고
    • BP-80 as a vacuolar sorting receptor.
    • Paris N, Neuhaus JM. BP-80 as a vacuolar sorting receptor. Plant Mol Biol 2002;50:903-914.
    • (2002) Plant Mol Biol , vol.50 , pp. 903-914
    • Paris, N.1    Neuhaus, J.M.2
  • 14
    • 33749265140 scopus 로고    scopus 로고
    • Arabidopsis EPSIN1 plays an important role in vacuolar trafficking of soluble cargo proteins in plant cells via interactions with clathrin, AP-1, VTI11, and VSR1.
    • Song J, Lee MH, Lee GJ, Yoo CM, Hwang I. Arabidopsis EPSIN1 plays an important role in vacuolar trafficking of soluble cargo proteins in plant cells via interactions with clathrin, AP-1, VTI11, and VSR1. Plant Cell 2006;18:2258-2274.
    • (2006) Plant Cell , vol.18 , pp. 2258-2274
    • Song, J.1    Lee, M.H.2    Lee, G.J.3    Yoo, C.M.4    Hwang, I.5
  • 15
    • 57749091611 scopus 로고    scopus 로고
    • Sorting and anterograde trafficking at the Golgi apparatus.
    • Hwang I. Sorting and anterograde trafficking at the Golgi apparatus. Plant Physiol 2008;148:673-683.
    • (2008) Plant Physiol , vol.148 , pp. 673-683
    • Hwang, I.1
  • 16
    • 0034923482 scopus 로고    scopus 로고
    • A new dynamin-like protein, ADL6, is involved in trafficking from the trans-Golgi network to the central vacuole in Arabidopsis.
    • Jin JB, Kim YA, Kim SJ, Lee SH, Kim DH, Cheong GW, Hwang I. A new dynamin-like protein, ADL6, is involved in trafficking from the trans-Golgi network to the central vacuole in Arabidopsis. Plant Cell 2001;13:1511-1526.
    • (2001) Plant Cell , vol.13 , pp. 1511-1526
    • Jin, J.B.1    Kim, Y.A.2    Kim, S.J.3    Lee, S.H.4    Kim, D.H.5    Cheong, G.W.6    Hwang, I.7
  • 17
    • 0032088950 scopus 로고    scopus 로고
    • An Arabidopsis VPS45p homolog implicated in protein transport to the vacuole.
    • Bassham DC, Raikhel NV. An Arabidopsis VPS45p homolog implicated in protein transport to the vacuole. Plant Physiol 1998;117:407-415.
    • (1998) Plant Physiol , vol.117 , pp. 407-415
    • Bassham, D.C.1    Raikhel, N.V.2
  • 18
    • 0344690187 scopus 로고    scopus 로고
    • The plant vesicle-associated SNARE AtVTI1a likely mediates vesicle transport from the trans-Golgi network to the prevacuolar compartment.
    • Zheng H, von Mollard GF, Kovaleva V, Stevens TH, Raikhel NV. The plant vesicle-associated SNARE AtVTI1a likely mediates vesicle transport from the trans-Golgi network to the prevacuolar compartment. Mol Biol Cell 1999;10:2251-2264.
    • (1999) Mol Biol Cell , vol.10 , pp. 2251-2264
    • Zheng, H.1    von Mollard, G.F.2    Kovaleva, V.3    Stevens, T.H.4    Raikhel, N.V.5
  • 19
    • 0035661728 scopus 로고    scopus 로고
    • Interactions between syntaxins identify at least five SNARE complexes within the Golgi/prevacuolar system of the Arabidopsis cell.
    • Sanderfoot AA, Kovaleva V, Bassham DC, Raikhel NV. Interactions between syntaxins identify at least five SNARE complexes within the Golgi/prevacuolar system of the Arabidopsis cell. Mol Biol Cell 2001;12:3733-3743.
    • (2001) Mol Biol Cell , vol.12 , pp. 3733-3743
    • Sanderfoot, A.A.1    Kovaleva, V.2    Bassham, D.C.3    Raikhel, N.V.4
  • 20
    • 0038366776 scopus 로고    scopus 로고
    • The GTPase ARF1p controls the sequence-specific vacuolar sorting route to the lytic vacuole.
    • Pimpl P, Hanton SL, Taylor JP, Pinto-daSilva LL, Denecke J. The GTPase ARF1p controls the sequence-specific vacuolar sorting route to the lytic vacuole. Plant Cell 2003;15:1242-1256.
    • (2003) Plant Cell , vol.15 , pp. 1242-1256
    • Pimpl, P.1    Hanton, S.L.2    Taylor, J.P.3    Pinto-daSilva, L.L.4    Denecke, J.5
  • 22
    • 23644442920 scopus 로고    scopus 로고
    • Actin filaments play a critical role in vacuolar trafficking at the Golgi complex in plant cells.
    • Kim H, Park M, Kim SJ, Hwang I. Actin filaments play a critical role in vacuolar trafficking at the Golgi complex in plant cells. Plant Cell 2005;17:888-902.
    • (2005) Plant Cell , vol.17 , pp. 888-902
    • Kim, H.1    Park, M.2    Kim, S.J.3    Hwang, I.4
  • 23
    • 0039109678 scopus 로고    scopus 로고
    • A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3.
    • Honing S, Sandoval IV, von Figura K. A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J 1998;17:1304-1314.
    • (1998) EMBO J , vol.17 , pp. 1304-1314
    • Honing, S.1    Sandoval, I.V.2    von Figura, K.3
  • 24
    • 0030886261 scopus 로고    scopus 로고
    • The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole.
    • Cowles CR, Odorizzi G, Payne GS, Emr SD. The AP-3 adaptor complex is essential for cargo-selective transport to the yeast vacuole. Cell 1997;91:109-118.
    • (1997) Cell , vol.91 , pp. 109-118
    • Cowles, C.R.1    Odorizzi, G.2    Payne, G.S.3    Emr, S.D.4
  • 26
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes.
    • Bonifacino JS, Traub LM. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu Rev Biochem 2003;72:395-447.
    • (2003) Annu Rev Biochem , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 27
    • 1342289622 scopus 로고    scopus 로고
    • Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network.
    • Nakatsu F, Ohno H. Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network. Cell Struct Funct 2003;28:419-429.
    • (2003) Cell Struct Funct , vol.28 , pp. 419-429
    • Nakatsu, F.1    Ohno, H.2
  • 28
    • 0028445831 scopus 로고
    • Plant physiology. Virtue on both sides.
    • Ap Rees T. Plant physiology. Virtue on both sides. Curr Biol 1994;4:557-559.
    • (1994) Curr Biol , vol.4 , pp. 557-559
    • Ap Rees, T.1
  • 29
    • 0037241454 scopus 로고    scopus 로고
    • Roles of cell-wall invertases and monosaccharide transporters in the growth and development of Arabidopsis.
    • Sherson SM, Alford HL, Forbes SM, Wallace G, Smith SM. Roles of cell-wall invertases and monosaccharide transporters in the growth and development of Arabidopsis. J Exp Bot 2003;54:525-531.
    • (2003) J Exp Bot , vol.54 , pp. 525-531
    • Sherson, S.M.1    Alford, H.L.2    Forbes, S.M.3    Wallace, G.4    Smith, S.M.5
  • 30
    • 0038610799 scopus 로고    scopus 로고
    • Cyanobacterial alkaline/neutral invertases. Origin of sucrose hydrolysis in the plant cytosol?
    • Vargas W, Cumino A, Salerno GL. Cyanobacterial alkaline/neutral invertases. Origin of sucrose hydrolysis in the plant cytosol? Planta 2003;216:951-960.
    • (2003) Planta , vol.216 , pp. 951-960
    • Vargas, W.1    Cumino, A.2    Salerno, G.L.3
  • 31
    • 0032406453 scopus 로고    scopus 로고
    • Expression of the Arabidopsis thaliana invertase gene family.
    • Tymowska-Lalanne Z, Kreis M. Expression of the Arabidopsis thaliana invertase gene family. Planta 1998;207:259-265.
    • (1998) Planta , vol.207 , pp. 259-265
    • Tymowska-Lalanne, Z.1    Kreis, M.2
  • 32
    • 15744385479 scopus 로고    scopus 로고
    • The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins.
    • Carter C, Pan S, Zouhar J, Avila EL, Girke T, Raikhel NV. The vegetative vacuole proteome of Arabidopsis thaliana reveals predicted and unexpected proteins. Plant Cell 2004;16:3285-3303.
    • (2004) Plant Cell , vol.16 , pp. 3285-3303
    • Carter, C.1    Pan, S.2    Zouhar, J.3    Avila, E.L.4    Girke, T.5    Raikhel, N.V.6
  • 33
    • 79955091756 scopus 로고    scopus 로고
    • A soluble acid invertase is directed to the vacuole by a signal anchor mechanism.
    • Rae AL, Casu RE, Perroux JM, Jackson MA, Grof CP. A soluble acid invertase is directed to the vacuole by a signal anchor mechanism. J Plant Physiol 2011;168:983-989.
    • (2011) J Plant Physiol , vol.168 , pp. 983-989
    • Rae, A.L.1    Casu, R.E.2    Perroux, J.M.3    Jackson, M.A.4    Grof, C.P.5
  • 34
    • 0038808989 scopus 로고    scopus 로고
    • A unique mechanism for protein processing and degradation in Arabidopsis thaliana.
    • Rojo E, Zouhar J, Carter C, Kovaleva V, Raikhel NV. A unique mechanism for protein processing and degradation in Arabidopsis thaliana. Proc Natl Acad Sci U S A 2003;100:7389-7394.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 7389-7394
    • Rojo, E.1    Zouhar, J.2    Carter, C.3    Kovaleva, V.4    Raikhel, N.V.5
  • 35
    • 0035098276 scopus 로고    scopus 로고
    • Trafficking of phosphatidylinositol 3-phosphate from the trans-Golgi network to the lumen of the central vacuole in plant cells.
    • Kim DH, Eu YJ, Yoo CM, Kim YW, Pih KT, Jin JB, Kim SJ, Stenmark H, Hwang I. Trafficking of phosphatidylinositol 3-phosphate from the trans-Golgi network to the lumen of the central vacuole in plant cells. Plant Cell 2001;13:287-301.
    • (2001) Plant Cell , vol.13 , pp. 287-301
    • Kim, D.H.1    Eu, Y.J.2    Yoo, C.M.3    Kim, Y.W.4    Pih, K.T.5    Jin, J.B.6    Kim, S.J.7    Stenmark, H.8    Hwang, I.9
  • 36
    • 77957790020 scopus 로고    scopus 로고
    • The cytosolic tail dipeptide Ile-Met of the pea receptor BP80 is required for recycling from the prevacuole and for endocytosis.
    • Saint-Jean B, Seveno-Carpentier E, Alcon C, Neuhaus JM, Paris N. The cytosolic tail dipeptide Ile-Met of the pea receptor BP80 is required for recycling from the prevacuole and for endocytosis. Plant Cell 2010;22:2825-2837.
    • (2010) Plant Cell , vol.22 , pp. 2825-2837
    • Saint-Jean, B.1    Seveno-Carpentier, E.2    Alcon, C.3    Neuhaus, J.M.4    Paris, N.5
  • 37
    • 0032583163 scopus 로고    scopus 로고
    • Integral membrane protein sorting to vacuoles in plant cells: evidence for two pathways.
    • Jiang L, Rogers JC. Integral membrane protein sorting to vacuoles in plant cells: evidence for two pathways. J Cell Biol 1998;143:1183-1199.
    • (1998) J Cell Biol , vol.143 , pp. 1183-1199
    • Jiang, L.1    Rogers, J.C.2
  • 40
    • 1342265970 scopus 로고    scopus 로고
    • Identification of the protein storage vacuole and protein targeting to the vacuole in leaf cells of three plant species.
    • Park M, Kim SJ, Vitale A, Hwang I. Identification of the protein storage vacuole and protein targeting to the vacuole in leaf cells of three plant species. Plant Physiol 2004;134:625-639.
    • (2004) Plant Physiol , vol.134 , pp. 625-639
    • Park, M.1    Kim, S.J.2    Vitale, A.3    Hwang, I.4
  • 41
    • 0033838323 scopus 로고    scopus 로고
    • A dominant negative mutant of sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells.
    • Takeuchi M, Ueda T, Sato K, Abe H, Nagata T, Nakano A. A dominant negative mutant of sar1 GTPase inhibits protein transport from the endoplasmic reticulum to the Golgi apparatus in tobacco and Arabidopsis cultured cells. Plant J 2000;23:517-525.
    • (2000) Plant J , vol.23 , pp. 517-525
    • Takeuchi, M.1    Ueda, T.2    Sato, K.3    Abe, H.4    Nagata, T.5    Nakano, A.6
  • 42
    • 75649114551 scopus 로고    scopus 로고
    • Mechanism and components of endoplasmic reticulum-associated degradation.
    • Hoseki J, Ushioda R, Nagata K. Mechanism and components of endoplasmic reticulum-associated degradation. J Biochem 2010;147:19-25.
    • (2010) J Biochem , vol.147 , pp. 19-25
    • Hoseki, J.1    Ushioda, R.2    Nagata, K.3
  • 43
    • 0020698663 scopus 로고
    • Latrunculins: novel marine toxins that disrupt microfilament organization in cultured cells.
    • Spector I, Shochet NR, Kashman Y, Groweiss A. Latrunculins: novel marine toxins that disrupt microfilament organization in cultured cells. Science 1983;219:493-495.
    • (1983) Science , vol.219 , pp. 493-495
    • Spector, I.1    Shochet, N.R.2    Kashman, Y.3    Groweiss, A.4
  • 45
    • 7944222351 scopus 로고    scopus 로고
    • The Arabidopsis rab5 homologs rha1 and ara7 localize to the prevacuolar compartment.
    • Lee GJ, Sohn EJ, Lee MH, Hwang I. The Arabidopsis rab5 homologs rha1 and ara7 localize to the prevacuolar compartment. Plant Cell Physiol 2004;45:1211-1220.
    • (2004) Plant Cell Physiol , vol.45 , pp. 1211-1220
    • Lee, G.J.1    Sohn, E.J.2    Lee, M.H.3    Hwang, I.4
  • 46
    • 0346037065 scopus 로고    scopus 로고
    • An endoplasmic reticulum-derived structure that is induced under stress conditions in Arabidopsis.
    • Matsushima R, Hayashi Y, Kondo M, Shimada T, Nishimura M, Hara-Nishimura I. An endoplasmic reticulum-derived structure that is induced under stress conditions in Arabidopsis. Plant Physiol 2002;130:1807-1814.
    • (2002) Plant Physiol , vol.130 , pp. 1807-1814
    • Matsushima, R.1    Hayashi, Y.2    Kondo, M.3    Shimada, T.4    Nishimura, M.5    Hara-Nishimura, I.6
  • 47
    • 20544465126 scopus 로고    scopus 로고
    • Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane.
    • Traub LM. Common principles in clathrin-mediated sorting at the Golgi and the plasma membrane. Biochim Biophys Acta 2005;1744:415-437.
    • (2005) Biochim Biophys Acta , vol.1744 , pp. 415-437
    • Traub, L.M.1
  • 48
    • 0032522517 scopus 로고    scopus 로고
    • Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site.
    • Rapoport I, Chen YC, Cupers P, Shoelson SE, Kirchhausen T. Dileucine-based sorting signals bind to the beta chain of AP-1 at a site distinct and regulated differently from the tyrosine-based motif-binding site. EMBO J 1998;17:2148-2155.
    • (1998) EMBO J , vol.17 , pp. 2148-2155
    • Rapoport, I.1    Chen, Y.C.2    Cupers, P.3    Shoelson, S.E.4    Kirchhausen, T.5
  • 49
    • 33645968400 scopus 로고    scopus 로고
    • Diacidic motifs influence the export of transmembrane proteins from the endoplasmic reticulum in plant cells.
    • Hanton SL, Renna L, Bortolotti LE, Chatre L, Stefano G, Brandizzi F. Diacidic motifs influence the export of transmembrane proteins from the endoplasmic reticulum in plant cells. Plant Cell 2005;17:3081-3093.
    • (2005) Plant Cell , vol.17 , pp. 3081-3093
    • Hanton, S.L.1    Renna, L.2    Bortolotti, L.E.3    Chatre, L.4    Stefano, G.5    Brandizzi, F.6
  • 51
    • 8844224911 scopus 로고    scopus 로고
    • Differential use of two AP-3-mediated pathways by lysosomal membrane proteins.
    • Ihrke G, Kyttala A, Russell MRG, Rous BA, Luzio JP. Differential use of two AP-3-mediated pathways by lysosomal membrane proteins. Traffic 2004;5:946-962.
    • (2004) Traffic , vol.5 , pp. 946-962
    • Ihrke, G.1    Kyttala, A.2    Russell, M.R.G.3    Rous, B.A.4    Luzio, J.P.5
  • 52
    • 0028241858 scopus 로고
    • Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion.
    • Chang XB, Hou YX, Jensen TJ, Riordan JR. Mapping of cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion. J Biol Chem 1994;269:18572-18575.
    • (1994) J Biol Chem , vol.269 , pp. 18572-18575
    • Chang, X.B.1    Hou, Y.X.2    Jensen, T.J.3    Riordan, J.R.4
  • 53
    • 0032488983 scopus 로고    scopus 로고
    • Influence of N-glycosylation and N-glycan trimming on the activity and intracellular traffic of GD3 synthase.
    • Martina JA, Daniotti JL, Maccioni HJ. Influence of N-glycosylation and N-glycan trimming on the activity and intracellular traffic of GD3 synthase. J Biol Chem 1998;273:3725-3731.
    • (1998) J Biol Chem , vol.273 , pp. 3725-3731
    • Martina, J.A.1    Daniotti, J.L.2    Maccioni, H.J.3
  • 54
    • 70350393229 scopus 로고    scopus 로고
    • ER export of KAT1 is correlated to the number of acidic residues within a triacidic motif.
    • Mikosch M, Kaberich K, Homann U. ER export of KAT1 is correlated to the number of acidic residues within a triacidic motif. Traffic 2009;10:1481-1487.
    • (2009) Traffic , vol.10 , pp. 1481-1487
    • Mikosch, M.1    Kaberich, K.2    Homann, U.3
  • 55
    • 0032711298 scopus 로고    scopus 로고
    • Tonoplast intrinsic protein isoforms as markers for vacuolar functions.
    • Jauh GY, Phillips TE, Rogers JC. Tonoplast intrinsic protein isoforms as markers for vacuolar functions. Plant Cell 1999;11:1867-1882.
    • (1999) Plant Cell , vol.11 , pp. 1867-1882
    • Jauh, G.Y.1    Phillips, T.E.2    Rogers, J.C.3
  • 56
    • 33244474619 scopus 로고    scopus 로고
    • Expression of the vacuolar Ca2+/H+ exchanger, OsCAX1a, in rice: cell and age specificity of expression, and enhancement by Ca2+.
    • Kamiya T, Akahori T, Ashikari M, Maeshima M. Expression of the vacuolar Ca2+/H+ exchanger, OsCAX1a, in rice: cell and age specificity of expression, and enhancement by Ca2+. Plant Cell Physiol 2006;47:96-106.
    • (2006) Plant Cell Physiol , vol.47 , pp. 96-106
    • Kamiya, T.1    Akahori, T.2    Ashikari, M.3    Maeshima, M.4
  • 57
    • 0031408332 scopus 로고    scopus 로고
    • The yeast adaptor protein complex, AP-3, is essential for the efficient delivery of alkaline phosphatase by the alternate pathway to the vacuole.
    • Stepp JD, Huang K, Lemmon SK. The yeast adaptor protein complex, AP-3, is essential for the efficient delivery of alkaline phosphatase by the alternate pathway to the vacuole. J Cell Biol 1997;139:1761-1774.
    • (1997) J Cell Biol , vol.139 , pp. 1761-1774
    • Stepp, J.D.1    Huang, K.2    Lemmon, S.K.3
  • 58
    • 0032516807 scopus 로고    scopus 로고
    • Multiple sorting pathways between the late Golgi and the vacuole in yeast.
    • Conibear E, Stevens TH. Multiple sorting pathways between the late Golgi and the vacuole in yeast. Biochim Biophys Acta 1998;1404:211-230.
    • (1998) Biochim Biophys Acta , vol.1404 , pp. 211-230
    • Conibear, E.1    Stevens, T.H.2
  • 59
    • 0030852699 scopus 로고    scopus 로고
    • The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway.
    • Piper RC, Bryant NJ, Stevens TH. The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway. J Cell Biol 1997;138:531-545.
    • (1997) J Cell Biol , vol.138 , pp. 531-545
    • Piper, R.C.1    Bryant, N.J.2    Stevens, T.H.3
  • 60
    • 33846821654 scopus 로고    scopus 로고
    • A conserved dileucine motif mediates clathrin and AP-2-dependent endocytosis of the HIV-1 envelope protein.
    • Byland R, Vance PJ, Hoxie JA, Marsh M. A conserved dileucine motif mediates clathrin and AP-2-dependent endocytosis of the HIV-1 envelope protein. Mol Biol Cell 2007;18:414-425.
    • (2007) Mol Biol Cell , vol.18 , pp. 414-425
    • Byland, R.1    Vance, P.J.2    Hoxie, J.A.3    Marsh, M.4
  • 61
    • 0346102461 scopus 로고    scopus 로고
    • Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigma1 and AP-3 delta-sigma3 hemicomplexes.
    • Janvier K, Kato Y, Boehm M, Rose JR, Martina JA, Kim BY, Venkatesan S, Bonifacino JS. Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 gamma-sigma1 and AP-3 delta-sigma3 hemicomplexes. J Cell Biol 2003;163:1281-1290.
    • (2003) J Cell Biol , vol.163 , pp. 1281-1290
    • Janvier, K.1    Kato, Y.2    Boehm, M.3    Rose, J.R.4    Martina, J.A.5    Kim, B.Y.6    Venkatesan, S.7    Bonifacino, J.S.8
  • 62
    • 0033959784 scopus 로고    scopus 로고
    • Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs.
    • Sevier CS, Weisz OA, Davis M, Machamer CE. Efficient export of the vesicular stomatitis virus G protein from the endoplasmic reticulum requires a signal in the cytoplasmic tail that includes both tyrosine-based and di-acidic motifs. Mol Biol Cell 2000;11:13-22.
    • (2000) Mol Biol Cell , vol.11 , pp. 13-22
    • Sevier, C.S.1    Weisz, O.A.2    Davis, M.3    Machamer, C.E.4
  • 63
    • 0031450221 scopus 로고    scopus 로고
    • The recycling of ERGIC-53 in the early secretory pathway-ERGIC-53 carries a cytosolic endoplasmic reticulum exit determinant interacting with COPII.
    • Kappeler F, Klopfenstein DRC, Foguet M, Paccaud JP, Hauri HP. The recycling of ERGIC-53 in the early secretory pathway-ERGIC-53 carries a cytosolic endoplasmic reticulum exit determinant interacting with COPII. J Biol Chem 1997;272:31801-31808.
    • (1997) J Biol Chem , vol.272 , pp. 31801-31808
    • Kappeler, F.1    Klopfenstein, D.R.C.2    Foguet, M.3    Paccaud, J.P.4    Hauri, H.P.5
  • 64
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum.
    • Nishimura N, Balch WE. A di-acidic signal required for selective export from the endoplasmic reticulum. Science 1997;277:556-558.
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 65
    • 0141521617 scopus 로고    scopus 로고
    • Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1.
    • Giraudo CG, Maccioni HJ. Endoplasmic reticulum export of glycosyltransferases depends on interaction of a cytoplasmic dibasic motif with Sar1. Mol Biol Cell 2003;14:3753-3766.
    • (2003) Mol Biol Cell , vol.14 , pp. 3753-3766
    • Giraudo, C.G.1    Maccioni, H.J.2
  • 66
    • 12444339783 scopus 로고    scopus 로고
    • Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat.
    • Contreras I, Yang Y, Robinson DG, Aniento F. Sorting signals in the cytosolic tail of plant p24 proteins involved in the interaction with the COPII coat. Plant Cell Physiol 2004;45:1779-1786.
    • (2004) Plant Cell Physiol , vol.45 , pp. 1779-1786
    • Contreras, I.1    Yang, Y.2    Robinson, D.G.3    Aniento, F.4
  • 67
    • 12744261335 scopus 로고    scopus 로고
    • Membrane-anchored prolyl hydroxylase with an export signal from the endoplasmic reticulum.
    • Yuasa K, Toyooka K, Fukuda H, Matsuoka K. Membrane-anchored prolyl hydroxylase with an export signal from the endoplasmic reticulum. Plant J 2005;41:81-94.
    • (2005) Plant J , vol.41 , pp. 81-94
    • Yuasa, K.1    Toyooka, K.2    Fukuda, H.3    Matsuoka, K.4
  • 68
    • 0035803582 scopus 로고    scopus 로고
    • An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export.
    • Votsmeier C, Gallwitz D. An acidic sequence of a putative yeast Golgi membrane protein binds COPII and facilitates ER export. EMBO J 2001;20:6742-6750.
    • (2001) EMBO J , vol.20 , pp. 6742-6750
    • Votsmeier, C.1    Gallwitz, D.2
  • 69
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles.
    • Miller EA, Beilharz TH, Malkus PN, Lee MC, Hamamoto S, Orci L, Schekman R. Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 2003;114:497-509.
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1    Beilharz, T.H.2    Malkus, P.N.3    Lee, M.C.4    Hamamoto, S.5    Orci, L.6    Schekman, R.7
  • 70
    • 0032561464 scopus 로고    scopus 로고
    • Inhibition of the interaction between tyrosine-based motifs and the medium chain subunit of the AP-2 adaptor complex by specific tyrphostins.
    • Crump CM, Williams JL, Stephens DJ, Banting G. Inhibition of the interaction between tyrosine-based motifs and the medium chain subunit of the AP-2 adaptor complex by specific tyrphostins. J Biol Chem 1998;273:28073-28077.
    • (1998) J Biol Chem , vol.273 , pp. 28073-28077
    • Crump, C.M.1    Williams, J.L.2    Stephens, D.J.3    Banting, G.4
  • 71
    • 33745456532 scopus 로고    scopus 로고
    • Targeting of the plant vacuolar sorting receptor BP80 is dependent on multiple sorting signals in the cytosolic tail.
    • daSilva LL, Foresti O, Denecke J. Targeting of the plant vacuolar sorting receptor BP80 is dependent on multiple sorting signals in the cytosolic tail. Plant Cell 2006;18:1477-1497.
    • (2006) Plant Cell , vol.18 , pp. 1477-1497
    • daSilva, L.L.1    Foresti, O.2    Denecke, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.