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Volumn 9, Issue 5, 2008, Pages 770-785

In vivo trafficking and localization of p24 proteins in plant cells

Author keywords

COPI; COPII; ER export; Golgi to ER recycling; p24 proteins; Prevacuolar compartment; Vacuole

Indexed keywords

ARABIDOPSIS PROTEIN; COAT PROTEIN COMPLEX I; COAT PROTEIN COMPLEX II; GAG PROTEIN; LYSINE; PROTEIN SUBUNIT; RED FLUORESCENT PROTEIN;

EID: 41849085580     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2008.00719.x     Document Type: Article
Times cited : (60)

References (75)
  • 2
    • 0030443308 scopus 로고    scopus 로고
    • A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding
    • Sohn K, Orci L, Ravazzola M, Amherdt M, Brunner M, Kahn RA, Rothman JE. A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding. J Cell Biol 1996; 135: 1239-1248.
    • (1996) J Cell Biol , vol.135 , pp. 1239-1248
    • Sohn, K.1    Orci, L.2    Ravazzola, M.3    Amherdt, M.4    Brunner, M.5    Kahn, R.A.6    Rothman, J.E.7
  • 4
    • 0030868332 scopus 로고    scopus 로고
    • p23, a major COPI-vesicle membrane protein, constitutively cycles through the early secretory pathway
    • Nickel W, Sohn K, Bunning C, Wieland F. p23, a major COPI-vesicle membrane protein, constitutively cycles through the early secretory pathway. Proc Natl Acad Sci U S A 1997; 94: 11393-11398.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11393-11398
    • Nickel, W.1    Sohn, K.2    Bunning, C.3    Wieland, F.4
  • 7
    • 0039517273 scopus 로고    scopus 로고
    • Localization and recycling of gp27 (hp24g3): Complex formation with other p24 family members
    • Füllerkrug J, Suganuma T, Tang BL, Hong W, Storrie B, Nilsson T. Localization and recycling of gp27 (hp24g3): Complex formation with other p24 family members. Mol Biol Cell 1999; 10: 1939-1955.
    • (1999) Mol Biol Cell , vol.10 , pp. 1939-1955
    • Füllerkrug, J.1    Suganuma, T.2    Tang, B.L.3    Hong, W.4    Storrie, B.5    Nilsson, T.6
  • 8
    • 0032971476 scopus 로고    scopus 로고
    • p24 and p23, the major transmembrane proteins of COPI-coated vesicles, form hetero-oligomeric complexes and cycle between organelles of the early secretory pathway
    • Gommel D, Orci L, Emig EM, Hannah MJ, Ravazzola M, Nickel W, Helms JB, Wieland FT, Sohn K. p24 and p23, the major transmembrane proteins of COPI-coated vesicles, form hetero-oligomeric complexes and cycle between organelles of the early secretory pathway. FEBS Lett 1999; 447: 179-185.
    • (1999) FEBS Lett , vol.447 , pp. 179-185
    • Gommel, D.1    Orci, L.2    Emig, E.M.3    Hannah, M.J.4    Ravazzola, M.5    Nickel, W.6    Helms, J.B.7    Wieland, F.T.8    Sohn, K.9
  • 9
    • 0033895196 scopus 로고    scopus 로고
    • Coupled transport of p24 family members
    • Emery G, Rojo M, Gruenberg J. Coupled transport of p24 family members. J Cell Sci 2000; 113: 2507-2516.
    • (2000) J Cell Sci , vol.113 , pp. 2507-2516
    • Emery, G.1    Rojo, M.2    Gruenberg, J.3
  • 10
    • 0034033881 scopus 로고    scopus 로고
    • The transmembrane protein p23 contributes to the organization of the Golgi apparatus
    • Rojo M, Emery G, Marjomäki V, McDowall A, Parton RG, Gruenberg J. The transmembrane protein p23 contributes to the organization of the Golgi apparatus. J Cell Sci 2000; 113: 1043-1057.
    • (2000) J Cell Sci , vol.113 , pp. 1043-1057
    • Rojo, M.1    Emery, G.2    Marjomäki, V.3    McDowall, A.4    Parton, R.G.5    Gruenberg, J.6
  • 11
    • 0035644194 scopus 로고    scopus 로고
    • Localization of p24 putative cargo receptors in the early secretory pathway depends on the biosynthetic activity of the cell
    • Kuiper RP, Bouw G, Janssen KP, Rotter J, van Herp F, Martens GJ. Localization of p24 putative cargo receptors in the early secretory pathway depends on the biosynthetic activity of the cell. Biochem J 2001; 360: 421-429.
    • (2001) Biochem J , vol.360 , pp. 421-429
    • Kuiper, R.P.1    Bouw, G.2    Janssen, K.P.3    Rotter, J.4    van Herp, F.5    Martens, G.J.6
  • 12
    • 0030055357 scopus 로고    scopus 로고
    • Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal membranes, are members of a protein family involved in vesicular trafficking
    • Blum R, Feick P, Puype M, Vandekerckhove J, Klengel R, Nastainczyk W, Schulz I. Tmp21 and p24A, two type I proteins enriched in pancreatic microsomal membranes, are members of a protein family involved in vesicular trafficking. J Biol Chem 1996; 271: 17183-17189.
    • (1996) J Biol Chem , vol.271 , pp. 17183-17189
    • Blum, R.1    Feick, P.2    Puype, M.3    Vandekerckhove, J.4    Klengel, R.5    Nastainczyk, W.6    Schulz, I.7
  • 13
    • 0032988896 scopus 로고    scopus 로고
    • The p24 family of transmembrane proteins at the interface between endoplasmic reticulum and Golgi apparatus
    • Emery G, Gruenberg J, Rojo M. The p24 family of transmembrane proteins at the interface between endoplasmic reticulum and Golgi apparatus. Protoplasma 1999; 207: 24-30.
    • (1999) Protoplasma , vol.207 , pp. 24-30
    • Emery, G.1    Gruenberg, J.2    Rojo, M.3
  • 14
    • 2442566675 scopus 로고    scopus 로고
    • p24 proteins, intracellular trafficking, and behaviour: Drosophila melanogaster provides insights and opportunities
    • Carney GE, Bowen NJ. p24 proteins, intracellular trafficking, and behaviour: Drosophila melanogaster provides insights and opportunities. Biol Cell 2004; 96: 271-278.
    • (2004) Biol Cell , vol.96 , pp. 271-278
    • Carney, G.E.1    Bowen, N.J.2
  • 16
    • 0037195867 scopus 로고    scopus 로고
    • Oligomeric state and stoichiometry of p24 proteins in the early secretory pathway
    • Jenne N, Frey K, Brügger B, Wieland FT. Oligomeric state and stoichiometry of p24 proteins in the early secretory pathway. J Biol Chem 2002; 277: 46504-46511.
    • (2002) J Biol Chem , vol.277 , pp. 46504-46511
    • Jenne, N.1    Frey, K.2    Brügger, B.3    Wieland, F.T.4
  • 17
    • 0034708445 scopus 로고    scopus 로고
    • Identification of a lumenal sequence specifying the assembly of Emp24p into p24 complexes in the yeast secretory pathway
    • Ciufo LF, Boyd A. Identification of a lumenal sequence specifying the assembly of Emp24p into p24 complexes in the yeast secretory pathway. J Biol Chem 2000; 275: 8382-8388.
    • (2000) J Biol Chem , vol.275 , pp. 8382-8388
    • Ciufo, L.F.1    Boyd, A.2
  • 18
    • 0242398591 scopus 로고    scopus 로고
    • How to make a vesicle: Coat protein-membrane interactions
    • In: Robinson DG, editor. Oxford: Blackwell Publishing
    • Aniento F, Helms B, Memon A. How to make a vesicle: Coat protein-membrane interactions. In: Robinson DG, editor. The Golgi Apparatus and the Plant Secretory Pathway. Oxford: Blackwell Publishing; 2003, pp. 36-62.
    • (2003) The Golgi Apparatus and the Plant Secretory Pathway , pp. 36-62
    • Aniento, F.1    Helms, B.2    Memon, A.3
  • 19
    • 34547639689 scopus 로고    scopus 로고
    • ER-to-Golgi transport: The COPII-pathway
    • In: Robinson DG, editor. Berlin-Heidelberg: Springer-Verlag
    • Aniento F, Matsuoka K, Robinson DG. ER-to-Golgi transport: The COPII-pathway. In: Robinson DG, editor. The Plant Endoplasmic Reticulum. Berlin-Heidelberg: Springer-Verlag; 2006, pp. 99-124.
    • (2006) The Plant Endoplasmic Reticulum , pp. 99-124
    • Aniento, F.1    Matsuoka, K.2    Robinson, D.G.3
  • 21
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson P, Letourneur F. Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 1994; 263: 1629-1631.
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 23
    • 0029796074 scopus 로고    scopus 로고
    • Bimodal interaction of coatomer with the p24 family of putative cargo receptors
    • Fiedler K, Veit M, Stamnes MA, Rothman JE. Bimodal interaction of coatomer with the p24 family of putative cargo receptors. Science 1996; 273: 1396-1399.
    • (1996) Science , vol.273 , pp. 1396-1399
    • Fiedler, K.1    Veit, M.2    Stamnes, M.A.3    Rothman, J.E.4
  • 24
    • 33750344792 scopus 로고    scopus 로고
    • Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins
    • Béthune J, Kol M, Hoffmann J, Reckmann I, Brügger B, Wieland F. Coatomer, the coat protein of COPI transport vesicles, discriminates endoplasmic reticulum residents from p24 proteins. Mol Cell Biol 2006; 26: 8011-8021.
    • (2006) Mol Cell Biol , vol.26 , pp. 8011-8021
    • Béthune, J.1    Kol, M.2    Hoffmann, J.3    Reckmann, I.4    Brügger, B.5    Wieland, F.6
  • 25
    • 0028964475 scopus 로고
    • The absence of Em24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi
    • Schimmöller F, Singer-Krüger B, Schröder S, Krüger U, Barlowe C, Riezman H. The absence of Em24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi. EMBO J 1995; 14: 1329-1339.
    • (1995) EMBO J , vol.14 , pp. 1329-1339
    • Schimmöller, F.1    Singer-Krüger, B.2    Schröder, S.3    Krüger, U.4    Barlowe, C.5    Riezman, H.6
  • 26
    • 0029910214 scopus 로고    scopus 로고
    • Erv25p, a component of COP II-coated vesicles, forms a complex with Emp24 that is required for efficient endoplasmic reticulum to Golgi transport
    • Belden WJ, Barlowe C. Erv25p, a component of COP II-coated vesicles, forms a complex with Emp24 that is required for efficient endoplasmic reticulum to Golgi transport. J Biol Chem 1996; 271: 26939-26946.
    • (1996) J Biol Chem , vol.271 , pp. 26939-26946
    • Belden, W.J.1    Barlowe, C.2
  • 29
    • 0035900761 scopus 로고    scopus 로고
    • Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex
    • Belden WJ, Barlowe C. Distinct roles for the cytoplasmic tail sequences of Emp24p and Erv25p in transport between the endoplasmic reticulum and Golgi complex. J Biol Chem 2001; 276: 43040-43048.
    • (2001) J Biol Chem , vol.276 , pp. 43040-43048
    • Belden, W.J.1    Barlowe, C.2
  • 30
    • 0034611009 scopus 로고    scopus 로고
    • The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles
    • Muniz M, Nuoffer C, Hauri HP, Riezman H. The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles. J Cell Biol 2000; 148: 925-930.
    • (2000) J Cell Biol , vol.148 , pp. 925-930
    • Muniz, M.1    Nuoffer, C.2    Hauri, H.P.3    Riezman, H.4
  • 31
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muniz M, Morsomme P, Riezman H. Protein sorting upon exit from the endoplasmic reticulum. Cell 2001; 104: 313-320.
    • (2001) Cell , vol.104 , pp. 313-320
    • Muniz, M.1    Morsomme, P.2    Riezman, H.3
  • 32
    • 0030015550 scopus 로고    scopus 로고
    • Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations
    • Elrod-Erickson MJ, Kaiser CA. Genes that control the fidelity of endoplasmic reticulum to Golgi transport identified as suppressors of vesicle budding mutations. Mol Biol Cell 1996; 7: 1043-1058.
    • (1996) Mol Biol Cell , vol.7 , pp. 1043-1058
    • Elrod-Erickson, M.J.1    Kaiser, C.A.2
  • 33
    • 0033553858 scopus 로고    scopus 로고
    • p24 proteins and quality control of LIN-12 and GLP-1 trafficking in Caenorhabditis elegans
    • Wen C, Greenwald I. p24 proteins and quality control of LIN-12 and GLP-1 trafficking in Caenorhabditis elegans. J Cell Biol 1999; 145: 1165-1175.
    • (1999) J Cell Biol , vol.145 , pp. 1165-1175
    • Wen, C.1    Greenwald, I.2
  • 34
    • 0034677633 scopus 로고    scopus 로고
    • Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex
    • Goldberg J. Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex. Cell 2000; 100: 671-679.
    • (2000) Cell , vol.100 , pp. 671-679
    • Goldberg, J.1
  • 36
    • 0037101946 scopus 로고    scopus 로고
    • Vesicular transport: The core machinery of COPI recruitment and budding
    • Nickel W, Brugger B, Wieland F. Vesicular transport: The core machinery of COPI recruitment and budding. J Cell Sci 2002; 115: 3235-3240.
    • (2002) J Cell Sci , vol.115 , pp. 3235-3240
    • Nickel, W.1    Brugger, B.2    Wieland, F.3
  • 38
    • 0033553388 scopus 로고    scopus 로고
    • GTP-dependent binding of ADP- ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23
    • Zhao L, Helms JB, Brunner J, Wieland FT. GTP-dependent binding of ADP- ribosylation factor to coatomer in close proximity to the binding site for dilysine retrieval motifs and p23. J Biol Chem 1999; 274: 14198-14203.
    • (1999) J Biol Chem , vol.274 , pp. 14198-14203
    • Zhao, L.1    Helms, J.B.2    Brunner, J.3    Wieland, F.T.4
  • 39
    • 0032478277 scopus 로고    scopus 로고
    • Reversible dissociation of coatomer: Functional characterization of a β/δ-coat protein subcomplex
    • Pavel J, Harter C, Wieland FT. Reversible dissociation of coatomer: functional characterization of a β/δ-coat protein subcomplex. Proc Natl Acad Sci U S A 1998; 95: 2140-2145.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 2140-2145
    • Pavel, J.1    Harter, C.2    Wieland, F.T.3
  • 40
    • 0035407522 scopus 로고    scopus 로고
    • KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: Measurements in living cells using FRET
    • Majoul I, Straub M, Hell SW, Duden R, Soling HD. KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET. Dev Cell 2001; 1: 139-153.
    • (2001) Dev Cell , vol.1 , pp. 139-153
    • Majoul, I.1    Straub, M.2    Hell, S.W.3    Duden, R.4    Soling, H.D.5
  • 41
    • 2542632045 scopus 로고    scopus 로고
    • Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer
    • Contreras I, Ortiz-Zapater E, Aniento F. Sorting signals in the cytosolic tail of membrane proteins involved in the interaction with plant ARF1 and coatomer. Plant J 2004; 38: 685-698.
    • (2004) Plant J , vol.38 , pp. 685-698
    • Contreras, I.1    Ortiz-Zapater, E.2    Aniento, F.3
  • 43
    • 0347382331 scopus 로고    scopus 로고
    • The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics
    • Emery G, Parton RG, Rojo M, Gruenberg J. The trans-membrane protein p25 forms highly specialized domains that regulate membrane composition and dynamics. J Cell Sci 2003; 116: 4821-4832.
    • (2003) J Cell Sci , vol.116 , pp. 4821-4832
    • Emery, G.1    Parton, R.G.2    Rojo, M.3    Gruenberg, J.4
  • 44
    • 12444339783 scopus 로고    scopus 로고
    • Plant COPI and COPII coat proteins show a differential affinity for p24 cytosolic tails
    • Contreras I, Yang Y, Robinson DG, Aniento F. Plant COPI and COPII coat proteins show a differential affinity for p24 cytosolic tails. 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
  • 45
    • 34447269976 scopus 로고    scopus 로고
    • Reticulon-like proteins in Arabidopsis thaliana: Structural organization and ER localization
    • Nziengui H, Bouhidel K, Pillon D, Der C, Marty F, Schoefs B. Reticulon-like proteins in Arabidopsis thaliana: Structural organization and ER localization. FEBS Lett 2007; 581: 3356-3362.
    • (2007) FEBS Lett , vol.581 , pp. 3356-3362
    • Nziengui, H.1    Bouhidel, K.2    Pillon, D.3    Der, C.4    Marty, F.5    Schoefs, B.6
  • 48
    • 1542370795 scopus 로고    scopus 로고
    • Identification of multivesicular bodies as prevacuolar compartments in Nicotiana tabacum BY-2 cells
    • Tse YC, Mo B, Hillmer S, Zhao M, Lo SW, Robinson DG, Jiang L. Identification of multivesicular bodies as prevacuolar compartments in Nicotiana tabacum BY-2 cells. Plant Cell 2004; 16: 672-693.
    • (2004) Plant Cell , vol.16 , pp. 672-693
    • Tse, Y.C.1    Mo, B.2    Hillmer, S.3    Zhao, M.4    Lo, S.W.5    Robinson, D.G.6    Jiang, L.7
  • 49
    • 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
  • 50
    • 0032213954 scopus 로고    scopus 로고
    • A GFP-mouse talin fusion protein labels plant actin filaments in vivo and visualizes the actin cytoskeleton in growing pollen tubes
    • Kost B, Spielhofer P, Chua NH. A GFP-mouse talin fusion protein labels plant actin filaments in vivo and visualizes the actin cytoskeleton in growing pollen tubes. Plant J 1998; 16: 393-401.
    • (1998) Plant J , vol.16 , pp. 393-401
    • Kost, B.1    Spielhofer, P.2    Chua, N.H.3
  • 51
    • 33645737420 scopus 로고    scopus 로고
    • Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway
    • Pimpl P, Taylor JP, Snowden C, Hillmer S, Robinson DG, Denecke J. Golgi-mediated vacuolar sorting of the endoplasmic reticulum chaperone BiP may play an active role in quality control within the secretory pathway. Plant Cell 2006; 18: 198-211.
    • (2006) Plant Cell , vol.18 , pp. 198-211
    • Pimpl, P.1    Taylor, J.P.2    Snowden, C.3    Hillmer, S.4    Robinson, D.G.5    Denecke, J.6
  • 53
    • 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
  • 54
    • 0034636026 scopus 로고    scopus 로고
    • Thinking about p24 proteins and how transport vesicles select their cargo
    • Kaiser C. Thinking about p24 proteins and how transport vesicles select their cargo. Proc Natl Acad Sci U S A 2000; 97: 3783-3785.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 3783-3785
    • Kaiser, C.1
  • 56
    • 0024982237 scopus 로고
    • Protein secretion in plant cells can occur via a default pathway
    • Denecke J, Botterman J, Deblaere R. Protein secretion in plant cells can occur via a default pathway. Plant Cell 1990; 2: 51-59.
    • (1990) Plant Cell , vol.2 , pp. 51-59
    • Denecke, J.1    Botterman, J.2    Deblaere, R.3
  • 57
    • 0028795584 scopus 로고
    • +] ATPase: A novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole
    • +] ATPase: A novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole. J Cell Biol 1995; 128: 39-49.
    • (1995) J Cell Biol , vol.128 , pp. 39-49
    • Chang, A.1    Fink, G.R.2
  • 58
    • 0026727566 scopus 로고
    • Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default compartment
    • Roberts CJ, Nothwehr SF, Stevens TH. Membrane protein sorting in the yeast secretory pathway: Evidence that the vacuole may be the default compartment. J Cell Biol 1992; 119: 69-83.
    • (1992) J Cell Biol , vol.119 , pp. 69-83
    • Roberts, C.J.1    Nothwehr, S.F.2    Stevens, T.H.3
  • 59
    • 0030990121 scopus 로고    scopus 로고
    • Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae
    • Roberg KJ, Rowley N, Kaiser CA. Physiological regulation of membrane protein sorting late in the secretory pathway of Saccharomyces cerevisiae. J Cell Biol 1997; 137: 1469-1482.
    • (1997) J Cell Biol , vol.137 , pp. 1469-1482
    • Roberg, K.J.1    Rowley, N.2    Kaiser, C.A.3
  • 60
    • 0028029829 scopus 로고
    • Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast
    • Gaynor EC, Heesen ST, Graham TR, Aebi M, Emr SD. Signal-mediated retrieval of a membrane protein from the Golgi to the ER in yeast. J Cell Biol 1994; 127: 653-665.
    • (1994) J Cell Biol , vol.127 , pp. 653-665
    • Gaynor, E.C.1    Heesen, S.T.2    Graham, T.R.3    Aebi, M.4    Emr, S.D.5
  • 61
    • 0026903856 scopus 로고
    • Protein sorting to the vacuolar membrane
    • Höfte H, Chrispeels MJ. Protein sorting to the vacuolar membrane. Plant Cell 1992; 4: 995-1004.
    • (1992) Plant Cell , vol.4 , pp. 995-1004
    • Höfte, H.1    Chrispeels, M.J.2
  • 62
    • 0033180595 scopus 로고    scopus 로고
    • Delivery of a secreted soluble protein to the vacuole via a membrane anchor
    • Barrieu F, Chrispeels MJ. Delivery of a secreted soluble protein to the vacuole via a membrane anchor. Plant Physiol 1999; 120: 961-968.
    • (1999) Plant Physiol , vol.120 , pp. 961-968
    • Barrieu, F.1    Chrispeels, M.J.2
  • 63
    • 0036016439 scopus 로고    scopus 로고
    • The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain
    • Brandizzi F, Frangne N, Marc-Martin S, Hawes C, Neuhaus JM, Paris N. The destination for single-pass membrane proteins is influenced markedly by the length of the hydrophobic domain. Plant Cell 2002; 14: 1077-1092.
    • (2002) Plant Cell , vol.14 , pp. 1077-1092
    • Brandizzi, F.1    Frangne, N.2    Marc-Martin, S.3    Hawes, C.4    Neuhaus, J.M.5    Paris, N.6
  • 64
    • 0033883172 scopus 로고    scopus 로고
    • The C-terminal dilysine motif confers endoplasmic reticulum localization to type I membrane proteins in plants
    • Benghezal M, Wasteneys GO, Jones DA. The C-terminal dilysine motif confers endoplasmic reticulum localization to type I membrane proteins in plants. Plant Cell 2000; 12: 1179-1201.
    • (2000) Plant Cell , vol.12 , pp. 1179-1201
    • Benghezal, M.1    Wasteneys, G.O.2    Jones, D.A.3
  • 65
    • 34249787044 scopus 로고    scopus 로고
    • Rice SCAMP1 defines clathrin-coated, trans-golgi-located tubular-vesicular structures as an early endosome in tobacco BY-2 cells
    • Lam SK, Siu CL, Hillmer S, Jang S, An G, Robinson DG, Jiang L. Rice SCAMP1 defines clathrin-coated, trans-golgi-located tubular-vesicular structures as an early endosome in tobacco BY-2 cells. Plant Cell 2007; 19: 296-319.
    • (2007) Plant Cell , vol.19 , pp. 296-319
    • Lam, S.K.1    Siu, C.L.2    Hillmer, S.3    Jang, S.4    An, G.5    Robinson, D.G.6    Jiang, L.7
  • 67
    • 33745453426 scopus 로고    scopus 로고
    • Plant retromer, localized to the prevacuolar compartment and microvesicles in Arabidopsis, may interact with vacuolar sorting receptors
    • Oliviusson P, Heinzerling O, Hillmer S, Hinz G, Tse YC, Jiang L, Robinson DG. Plant retromer, localized to the prevacuolar compartment and microvesicles in Arabidopsis, may interact with vacuolar sorting receptors. Plant Cell 2006; 18: 1239-1252.
    • (2006) Plant Cell , vol.18 , pp. 1239-1252
    • Oliviusson, P.1    Heinzerling, O.2    Hillmer, S.3    Hinz, G.4    Tse, Y.C.5    Jiang, L.6    Robinson, D.G.7
  • 68
    • 33646832927 scopus 로고    scopus 로고
    • In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery
    • Stefano G, Renna L, Chatre L, Hanton SL, Moreau P, Hawes C, Brandizzi F. In tobacco leaf epidermal cells, the integrity of protein export from the endoplasmic reticulum and of ER export sites depends on active COPI machinery. Plant J 2006; 46: 95-110.
    • (2006) Plant J , vol.46 , pp. 95-110
    • Stefano, G.1    Renna, L.2    Chatre, L.3    Hanton, S.L.4    Moreau, P.5    Hawes, C.6    Brandizzi, F.7
  • 70
    • 0015914077 scopus 로고
    • Streptomycin-resistant plants from callus culture of haploid tobacco
    • Maliga P, Breznovits A, Marton L. Streptomycin-resistant plants from callus culture of haploid tobacco. Nature 1973; 244: 29-30.
    • (1973) Nature , vol.244 , pp. 29-30
    • Maliga, P.1    Breznovits, A.2    Marton, L.3
  • 71
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassays with tobacco tissue cultures
    • Murashige R, Skoog F. A revised medium for rapid growth and bioassays with tobacco tissue cultures. Physiol Plant 1962; 15: 473-497.
    • (1962) Physiol Plant , vol.15 , pp. 473-497
    • Murashige, R.1    Skoog, F.2
  • 72
    • 33749262307 scopus 로고    scopus 로고
    • Overexpression of the Arabidopsis syntaxin PEP12/SYP21 inhibits transport from the prevacuolar compartment to the lytic vacuole in vivo
    • Foresti O, daSilva LL, Denecke J. Overexpression of the Arabidopsis syntaxin PEP12/SYP21 inhibits transport from the prevacuolar compartment to the lytic vacuole in vivo. Plant Cell 2006; 18: 2275-2293.
    • (2006) Plant Cell , vol.18 , pp. 2275-2293
    • Foresti, O.1    daSilva, L.L.2    Denecke, J.3
  • 73
    • 0000520177 scopus 로고
    • A protocol for transient gene expressión in Arabidopsis thaliana protoplasts isolated from cell suspensión cultures
    • Axelos M, Curie C, Mazzolini L, Bardet C, Lescure B. A protocol for transient gene expressión in Arabidopsis thaliana protoplasts isolated from cell suspensión cultures. Plant Physiol Biochem 1992; 30: 123-128.
    • (1992) Plant Physiol Biochem , vol.30 , pp. 123-128
    • Axelos, M.1    Curie, C.2    Mazzolini, L.3    Bardet, C.4    Lescure, B.5
  • 74
    • 4043088477 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic shuttling of the beet necrotic yellow vein virus RNA-3-encoded p25 protein
    • Vetter G, Hily JM, Klein E, Schmidlin L, Haas M, Merkle T, Gilmer D. Nucleo-cytoplasmic shuttling of the beet necrotic yellow vein virus RNA-3-encoded p25 protein. J Gen Virol 2004; 85: 2459-2469.
    • (2004) J Gen Virol , vol.85 , pp. 2459-2469
    • Vetter, G.1    Hily, J.M.2    Klein, E.3    Schmidlin, L.4    Haas, M.5    Merkle, T.6    Gilmer, D.7


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