메뉴 건너뛰기




Volumn 135, Issue 4, 2004, Pages 2318-2329

Novel regulation of aquaporins during osmotic stress

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; PLANTS (BOTANY); PROTEINS; STRESS ANALYSIS;

EID: 4444221804     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.104.044891     Document Type: Article
Times cited : (185)

References (58)
  • 1
    • 0242432461 scopus 로고    scopus 로고
    • Overexpression of a plasma membrane aquaporin in transgenic tobacco improves plant vigor under favorable growth conditions but not under drought or salt stress
    • Aharon R, Shahak Y, Wininger S, Bendov R, Kapulnik Y, Galili G (2003) Overexpression of a plasma membrane aquaporin in transgenic tobacco improves plant vigor under favorable growth conditions but not under drought or salt stress. Plant Cell 15: 439-447
    • (2003) Plant Cell , vol.15 , pp. 439-447
    • Aharon, R.1    Shahak, Y.2    Wininger, S.3    Bendov, R.4    Kapulnik, Y.5    Galili, G.6
  • 3
    • 0031722224 scopus 로고    scopus 로고
    • Glycosylation is not essential for vasopressin-dependent routing of aquaporin-2 in transfected Madison-Darby canine kidney cells
    • Baumgarten R, van de Pol MH, Wetzels JF, van Os CH, Deen PM (1998) Glycosylation is not essential for vasopressin-dependent routing of aquaporin-2 in transfected Madison-Darby canine kidney cells. J Am Soc Nephrol 9: 1553-1559
    • (1998) J Am Soc Nephrol , vol.9 , pp. 1553-1559
    • Baumgarten, R.1    Van De Pol, M.H.2    Wetzels, J.F.3    Van Os, C.H.4    Deen, P.M.5
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0029441250 scopus 로고
    • Methods in plant immunolight microscopy
    • DW Galbraith, HJ Bohnert, DP Bourque, eds, Academic Press, New York
    • Brown BE, Lemmon BE (1995) Methods in plant immunolight microscopy. In DW Galbraith, HJ Bohnert, DP Bourque, eds, Methods in Plant Cell Biology. Academic Press, New York, pp 85-107
    • (1995) Methods in Plant Cell Biology , pp. 85-107
    • Brown, B.E.1    Lemmon, B.E.2
  • 6
  • 7
    • 0031867912 scopus 로고    scopus 로고
    • Effects of N-glycosylation on the folding and structure of plant proteins
    • Ceriotti A, Duranti M, Bollini R (1998) Effects of N-glycosylation on the folding and structure of plant proteins. J Exp Bot 49: 1091-1103
    • (1998) J Exp Bot , vol.49 , pp. 1091-1103
    • Ceriotti, A.1    Duranti, M.2    Bollini, R.3
  • 8
    • 0033574449 scopus 로고    scopus 로고
    • Brefeldin A: The advantage of being uncompetitive
    • Chardin P, McCormick F (1999) Brefeldin A: the advantage of being uncompetitive. Cell 97: 153-155
    • (1999) Cell , vol.97 , pp. 153-155
    • Chardin, P.1    McCormick, F.2
  • 9
    • 0033996879 scopus 로고    scopus 로고
    • Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity
    • Chaumont F, Barrieu F, Jung R, Chrispeels MJ (2000) Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity. Plant Physiol 122: 1025-1034
    • (2000) Plant Physiol , vol.122 , pp. 1025-1034
    • Chaumont, F.1    Barrieu, F.2    Jung, R.3    Chrispeels, M.J.4
  • 10
    • 0035106823 scopus 로고    scopus 로고
    • Aquaporins constitute a large and highly divergent protein family in maize
    • Chaumont F, Barrieu F, Wojcik E, Chrispeels MJ, Jung R (2001) Aquaporins constitute a large and highly divergent protein family in maize. Plant Physiol 125: 1206-1215
    • (2001) Plant Physiol , vol.125 , pp. 1206-1215
    • Chaumont, F.1    Barrieu, F.2    Wojcik, E.3    Chrispeels, M.J.4    Jung, R.5
  • 11
    • 0033840913 scopus 로고    scopus 로고
    • Endoplasmic reticulum-derived compartments function in storage and as mediators of vacuolar remodeling via a new type of organelle, precursor protease vesicles
    • Chrispeels MJ, Herman EM (2000) Endoplasmic reticulum-derived compartments function in storage and as mediators of vacuolar remodeling via a new type of organelle, precursor protease vesicles. Plant Physiol 123: 1227-1233
    • (2000) Plant Physiol , vol.123 , pp. 1227-1233
    • Chrispeels, M.J.1    Herman, E.M.2
  • 12
    • 0029988965 scopus 로고    scopus 로고
    • cDNA sequence and expression of subunit e of the vacuolar H(+)-ATPase in the inducible Crassulacean acid metabolism plant Mesembryanthemum crystallinum
    • Dietz KJ, Arbinger B (1996) cDNA sequence and expression of subunit E of the vacuolar H(+)-ATPase in the inducible Crassulacean acid metabolism plant Mesembryanthemum crystallinum. Biochim Biophys Acta 1281: 134-138
    • (1996) Biochim Biophys Acta , vol.1281 , pp. 134-138
    • Dietz, K.J.1    Arbinger, B.2
  • 13
    • 0001069047 scopus 로고
    • Tonoplast and soluble vacuolar proteins are targeted by different mechanisms
    • Gomez L, Chrispeels MJ (1993) Tonoplast and soluble vacuolar proteins are targeted by different mechanisms. Plant Cell 5: 1113-1124
    • (1993) Plant Cell , vol.5 , pp. 1113-1124
    • Gomez, L.1    Chrispeels, M.J.2
  • 14
    • 0035040818 scopus 로고    scopus 로고
    • Regulation and role of adenylyl cyclase isoforms
    • Hanoune J, Defer N (2001) Regulation and role of adenylyl cyclase isoforms. Annu Rev Pharmacol Toxicol 41: 145-174
    • (2001) Annu Rev Pharmacol Toxicol , vol.41 , pp. 145-174
    • Hanoune, J.1    Defer, N.2
  • 15
    • 0035124916 scopus 로고    scopus 로고
    • Ultrastructural changes in the Malpighian tubules of the House Cricket, Acheta domesticus, at the onset of diuresis: A time study
    • Hazelton SR, Felgenhauer BE, Spring JH (2001) Ultrastructural changes in the Malpighian tubules of the House Cricket, Acheta domesticus, at the onset of diuresis: a time study. J Morphol 247: 80-92
    • (2001) J Morphol , vol.247 , pp. 80-92
    • Hazelton, S.R.1    Felgenhauer, B.E.2    Spring, J.H.3
  • 16
    • 0016368896 scopus 로고
    • Purification of a plasma membrane-bound triphosphate from plant roots
    • Hodges TK, Leonard RT (1974) Purification of a plasma membrane-bound triphosphate from plant roots. Methods Enzymol 321: 392-406
    • (1974) Methods Enzymol , vol.321 , pp. 392-406
    • Hodges, T.K.1    Leonard, R.T.2
  • 18
    • 0032711298 scopus 로고    scopus 로고
    • Tonoplast intrinsic protein isoforms as markers for vacuolar functions
    • Jauh G-Y, Phillips TE, Rogers JC (1999) Tonoplast intrinsic protein isoforms as markers for vacuolar functions. Plant Cell 11: 1867-1882
    • (1999) Plant Cell , vol.11 , pp. 1867-1882
    • Jauh, G.-Y.1    Phillips, T.E.2    Rogers, J.C.3
  • 20
    • 0032583163 scopus 로고    scopus 로고
    • Integral membrane protein sorting to vacuoles in plant cells: Evidence for two pathways
    • Jiang L, Rogers JC (1998) Integral membrane protein sorting to vacuoles in plant cells: evidence for two pathways. J Cell Biol 30: 1183-1199
    • (1998) J Cell Biol , vol.30 , pp. 1183-1199
    • Jiang, L.1    Rogers, J.C.2
  • 21
    • 0032054595 scopus 로고    scopus 로고
    • Significance of plasmalemma aquaporins for water-transport in Arabidopsis thaliana
    • Kaldenhoff R, Grote K, Zhu J-J, Zimmermann U (1998) Significance of plasmalemma aquaporins for water-transport in Arabidopsis thaliana. Plant J 14: 121-128
    • (1998) Plant J , vol.14 , pp. 121-128
    • Kaldenhoff, R.1    Grote, K.2    Zhu, J.-J.3    Zimmermann, U.4
  • 22
    • 0028278224 scopus 로고
    • Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport
    • Kim EJ, Zhen R-G, Rea PA (1994) Heterologous expression of plant vacuolar pyrophosphatase in yeast demonstrates sufficiency of the substrate-binding subunit for proton transport. Proc Natl Acad Sci USA 91: 6128-6132
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6128-6132
    • Kim, E.J.1    Zhen, R.-G.2    Rea, P.A.3
  • 24
    • 0030747394 scopus 로고    scopus 로고
    • Regulation of aquaporin-2 water channel trafficking by vasopressin
    • Knepper MA, Inoue T (1997) Regulation of aquaporin-2 water channel trafficking by vasopressin. Curr Opin Cell Biol 9: 560-564
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 560-564
    • Knepper, M.A.1    Inoue, T.2
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227: 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0345392686 scopus 로고    scopus 로고
    • Urea transport by nitrogen-regulated tonoplast intrinsic proteins in Arabidopsis
    • Liu LH, Ludewig U, Gasset B, Frommer WB, Von Wirén N (2003) Urea transport by nitrogen-regulated tonoplast intrinsic proteins in Arabidopsis. Plant Physiol 133: 1220-1228
    • (2003) Plant Physiol , vol.133 , pp. 1220-1228
    • Liu, L.H.1    Ludewig, U.2    Gasset, B.3    Frommer, W.B.4    Von Wirén, N.5
  • 30
    • 0032718565 scopus 로고    scopus 로고
    • Plant vacuoles
    • Marty F (1999) Plant vacuoles. Plant Cell 11: 587-599
    • (1999) Plant Cell , vol.11 , pp. 587-599
    • Marty, F.1
  • 31
    • 0028981718 scopus 로고
    • Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells
    • Matsuoka K, Bassham DC, Raikhel NV, Nakamura K (1995) Different sensitivity to wortmannin of two vacuolar sorting signals indicates the presence of distinct sorting machineries in tobacco cells. J Cell Biol 130: 1307-1318
    • (1995) J Cell Biol , vol.130 , pp. 1307-1318
    • Matsuoka, K.1    Bassham, D.C.2    Raikhel, N.V.3    Nakamura, K.4
  • 33
    • 0028997596 scopus 로고
    • Phosphorylation regulates the water channel activity of the seed-specific aquaporin α-TIP
    • Maurel C, Kado RT, Guern J, Chrispeels MJ (1995) Phosphorylation regulates the water channel activity of the seed-specific aquaporin α-TIP. EMBO J 14: 3028-3035
    • (1995) EMBO J , vol.14 , pp. 3028-3035
    • Maurel, C.1    Kado, R.T.2    Guern, J.3    Chrispeels, M.J.4
  • 34
    • 0027192036 scopus 로고
    • The vacuolar membrane protein α-TIP creates water specific channels in Xenopus oocytes
    • Maurel C, Reizer J, Schroeder JI, Chrispeels MJ (1993) The vacuolar membrane protein α-TIP creates water specific channels in Xenopus oocytes. EMBO J 12: 2241-2247
    • (1993) EMBO J , vol.12 , pp. 2241-2247
    • Maurel, C.1    Reizer, J.2    Schroeder, J.I.3    Chrispeels, M.J.4
  • 35
    • 0035964259 scopus 로고    scopus 로고
    • CAMP acts as a second messenger in pollen tube growth and reorientation
    • Moutinho A, Hussey PJ, Trewavas AJ, Malhó R (2001) CAMP acts as a second messenger in pollen tube growth and reorientation. Proc Natl Acad Sci USA 98: 10481-10486
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10481-10486
    • Moutinho, A.1    Hussey, P.J.2    Trewavas, A.J.3    Malhó, R.4
  • 36
    • 84982358134 scopus 로고
    • A revised medium for rapid growth and bioassay with tobacco tissue cultures
    • Murashige T, Skoog F (1962) A revised medium for rapid growth and bioassay with tobacco tissue cultures. Physiol Plant 15: 473-479
    • (1962) Physiol Plant , vol.15 , pp. 473-479
    • Murashige, T.1    Skoog, F.2
  • 37
    • 0031131643 scopus 로고    scopus 로고
    • Abundant accumulation of the calcium-binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana
    • Nelson DE, Glaunsinger B, Bohnert HJ (1997) Abundant accumulation of the calcium-binding molecular chaperone calreticulin in specific floral tissues of Arabidopsis thaliana. Plant Physiol 114: 29-37
    • (1997) Plant Physiol , vol.114 , pp. 29-37
    • Nelson, D.E.1    Glaunsinger, B.2    Bohnert, H.J.3
  • 38
    • 0032744079 scopus 로고    scopus 로고
    • Cyclic nucleotides in higher plants: The enduring paradox
    • Newton RP, Roef L, Witters E, Van Onckelen H (1999) Cyclic nucleotides in higher plants: the enduring paradox. New Phytol 143: 427-455
    • (1999) New Phytol , vol.143 , pp. 427-455
    • Newton, R.P.1    Roef, L.2    Witters, E.3    Van Onckelen, H.4
  • 39
    • 0028889112 scopus 로고
    • Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane
    • Nielsen S, Chou CL, Marples D, Christensen EI, Kishore BK, Knepper MA (1995) Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane. Proc Natl Acad Sci USA 92: 1013-1017
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1013-1017
    • Nielsen, S.1    Chou, C.L.2    Marples, D.3    Christensen, E.I.4    Kishore, B.K.5    Knepper, M.A.6
  • 40
    • 0024978315 scopus 로고
    • +-ATPase gene from the plant Arabidopsis thaliana
    • +-ATPase gene from the plant Arabidopsis thaliana. J Biol Chem 264: 8557-8562
    • (1989) J Biol Chem , vol.264 , pp. 8557-8562
    • Pardo, J.M.1    Serrano, R.2
  • 42
    • 0030014157 scopus 로고    scopus 로고
    • Plant cells contain two functionally distinct vacuolar compartments
    • Paris N, Stanley CM, Jones RL, Rogers JC (1996) Plant cells contain two functionally distinct vacuolar compartments. Cell 85: 563-572
    • (1996) Cell , vol.85 , pp. 563-572
    • Paris, N.1    Stanley, C.M.2    Jones, R.L.3    Rogers, J.C.4
  • 43
    • 0024317023 scopus 로고
    • +-ATPase reveal additional subunits: Revised subunit composition
    • +-ATPase reveal additional subunits: revised subunit composition. J Biol Chem 264: 20025-20032
    • (1989) J Biol Chem , vol.264 , pp. 20025-20032
    • Parry, R.V.1    Turner, J.C.2    Rea, P.A.3
  • 45
    • 0036007958 scopus 로고    scopus 로고
    • Reevaluation of the effects of brefeldin a on plant cells using tobacco bright yellow 2 cells expressing Golgi-targeted green fluorescent protein and COP1 antisera
    • Ritzenthaler C, Nebenführ A, Movafeghi A, Stussi-Garaud C, Behnia L, Pimpl P, Staehelin LA, Robinson DG (2002) Reevaluation of the effects of brefeldin A on plant cells using tobacco bright yellow 2 cells expressing Golgi-targeted green fluorescent protein and COP1 antisera. Plant Cell 14: 237-261
    • (2002) Plant Cell , vol.14 , pp. 237-261
    • Ritzenthaler, C.1    Nebenführ, A.2    Movafeghi, A.3    Stussi-Garaud, C.4    Behnia, L.5    Pimpl, P.6    Staehelin, L.A.7    Robinson, D.G.8
  • 46
    • 0000179989 scopus 로고    scopus 로고
    • PIP1 aquaporins are concentrated in plasmalemmasomes of Arabidopsis mesophyll
    • Robinson DG, Sieber H, Kammerloher W, Schäffner AR (1996) PIP1 aquaporins are concentrated in plasmalemmasomes of Arabidopsis mesophyll. Plant Physiol 111: 645-649
    • (1996) Plant Physiol , vol.111 , pp. 645-649
    • Robinson, D.G.1    Sieber, H.2    Kammerloher, W.3    Schäffner, A.R.4
  • 48
    • 0033677662 scopus 로고    scopus 로고
    • The high diversity of aquaporins reveals novel facets of plant membrane functions
    • Santoni V, Gerbeau P, Javot H, Maurel C (2000) The high diversity of aquaporins reveals novel facets of plant membrane functions. Curr Opin Plant Biol 3: 476-481
    • (2000) Curr Opin Plant Biol , vol.3 , pp. 476-481
    • Santoni, V.1    Gerbeau, P.2    Javot, H.3    Maurel, C.4
  • 49
    • 0035999374 scopus 로고    scopus 로고
    • PIP1 plasma membrane aquaporins in tobacco: From cellular effects to function in plants
    • Siefritz F, Tyree MT, Lovisolo C, Schubert A, Kaldenhoff R (2002) PIP1 plasma membrane aquaporins in tobacco: from cellular effects to function in plants. Plant Cell 14: 869-876
    • (2002) Plant Cell , vol.14 , pp. 869-876
    • Siefritz, F.1    Tyree, M.T.2    Lovisolo, C.3    Schubert, A.4    Kaldenhoff, R.5
  • 51
    • 0034486835 scopus 로고    scopus 로고
    • Misfolding and aggregation of vacuolar glycoproteins in plant cells
    • Sparvoli F, Faoro F, Daminati MG, Ceriotti A, Bollini R (2000) Misfolding and aggregation of vacuolar glycoproteins in plant cells. Plant J 24: 825-836
    • (2000) Plant J , vol.24 , pp. 825-836
    • Sparvoli, F.1    Faoro, F.2    Daminati, M.G.3    Ceriotti, A.4    Bollini, R.5
  • 52
    • 0032971712 scopus 로고    scopus 로고
    • Plant aquaporins: Their molecular biology, biophysics and significance for plant water relations
    • Tyerman SD, Bohnert HJ, Maurel C, Steudle E, Smith JAC (1999) Plant aquaporins: their molecular biology, biophysics and significance for plant water relations. J Exp Bot 50: 1055-1071
    • (1999) J Exp Bot , vol.50 , pp. 1055-1071
    • Tyerman, S.D.1    Bohnert, H.J.2    Maurel, C.3    Steudle, E.4    Smith, J.A.C.5
  • 53
    • 0036187202 scopus 로고    scopus 로고
    • Plant aquaporins: Multifunctional water and solute channels with expanding roles
    • Tyerman SD, Niemietz CM, Bramley H (2002) Plant aquaporins: multifunctional water and solute channels with expanding roles. Plant Cell Environ 25: 173-194
    • (2002) Plant Cell Environ , vol.25 , pp. 173-194
    • Tyerman, S.D.1    Niemietz, C.M.2    Bramley, H.3
  • 55
    • 0032917706 scopus 로고    scopus 로고
    • Salt stress in Mesembryanthemum crystallinum L. cell suspensions activates adaptive mechanisms similar to those observed in the whole plant
    • Vera-Estrella R, Barkla BJ, Bohnert HJ, Pantoja O (1999) Salt stress in Mesembryanthemum crystallinum L. cell suspensions activates adaptive mechanisms similar to those observed in the whole plant. Planta 207: 426-435
    • (1999) Planta , vol.207 , pp. 426-435
    • Vera-Estrella, R.1    Barkla, B.J.2    Bohnert, H.J.3    Pantoja, O.4
  • 57
    • 0008192518 scopus 로고
    • The actin cytoskeleton and polar water permeability in Characean cells
    • Wayne R, Tazawa M (1988) The actin cytoskeleton and polar water permeability in Characean cells. Protoplasma Suppl 2: 116-130
    • (1988) Protoplasma Suppl , vol.2 , pp. 116-130
    • Wayne, R.1    Tazawa, M.2
  • 58
    • 0028197377 scopus 로고
    • A comparison of demethoxyviridin and wortmannin as inhibitors of phosphatidylinositol 3-kinase
    • Woscholski R, Kodaki T, McKinnon M, Waterfield MD, Parker PJ (1994) A comparison of demethoxyviridin and wortmannin as inhibitors of phosphatidylinositol 3-kinase. FEBS Lett 342: 109-114
    • (1994) FEBS Lett , vol.342 , pp. 109-114
    • Woscholski, R.1    Kodaki, T.2    McKinnon, M.3    Waterfield, M.D.4    Parker, P.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.