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Volumn 35, Issue 1, 2008, Pages 1-14

Expanding roles of plant aquaporins in plasma membranes and cell organelles

Author keywords

ER; Flower; Fruit; Structure function relationship; Vacuolar membrane; Water channel; Water transport

Indexed keywords

CARBON DIOXIDE; GAS PERMEABILITY; OSMOSIS; PHOSPHORYLATION; PLANT CELL CULTURE; PROTEINS;

EID: 38549100799     PISSN: 14454408     EISSN: None     Source Type: Journal    
DOI: 10.1071/FP07130     Document Type: Review
Times cited : (86)

References (148)
  • 1
    • 4544353285 scopus 로고    scopus 로고
    • Aquaporin water channels (Nobel Lecture)
    • doi: 10.1002/anie. 200460804
    • Agre P (2004) Aquaporin water channels (Nobel Lecture). Angewandte Chemie International Edition 43, 4278-4290. doi: 10.1002/anie. 200460804
    • (2004) Angewandte Chemie International Edition , vol.43 , pp. 4278-4290
    • Agre, P.1
  • 2
    • 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
    • doi: 10.1105/tpc.009225
    • 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. The Plant Cell 15, 439-447. doi: 10.1105/tpc.009225
    • (2003) The 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
    • 18744396394 scopus 로고    scopus 로고
    • The role of aquaporins and membrane damage in chilling and hydrogen peroxide induced changes in the hydraulic conductance of maize roots
    • doi: 10.1104/pp.104.051045
    • Aroca R, Amodeo G, Fernández-Illescas S, Herman EM, Chaumont F, Chrispeels MJ (2005) The role of aquaporins and membrane damage in chilling and hydrogen peroxide induced changes in the hydraulic conductance of maize roots. Plant Physiology 137, 341-353. doi: 10.1104/pp.104.051045
    • (2005) Plant Physiology , vol.137 , pp. 341-353
    • Aroca, R.1    Amodeo, G.2    Fernández-Illescas, S.3    Herman, E.M.4    Chaumont, F.5    Chrispeels, M.J.6
  • 4
    • 2942711718 scopus 로고    scopus 로고
    • Phosphorylation of plasma membrane aquaporin regulates temperature-dependent opening of tulip petals
    • doi: 10.1093/pcp/pch069
    • Azad AK, Sawa Y, Ishikawa T, Shibata H (2004) Phosphorylation of plasma membrane aquaporin regulates temperature-dependent opening of tulip petals. Plant & Cell Physiology 45, 608-617. doi: 10.1093/pcp/pch069
    • (2004) Plant & Cell Physiology , vol.45 , pp. 608-617
    • Azad, A.K.1    Sawa, Y.2    Ishikawa, T.3    Shibata, H.4
  • 5
    • 38549101634 scopus 로고    scopus 로고
    • Functional and expression analysis of four homologues of tulip plasma membrane aquaporins: A putative homologue to be regulated by phosphorylation
    • In press
    • Azad AK, Katsuhara M, Ishikawa T, Sawa Y, Ishikawa T, Shibata H (2007) Functional and expression analysis of four homologues of tulip plasma membrane aquaporins: a putative homologue to be regulated by phosphorylation. Plant & Cell Physiology (In press).
    • (2007) Plant & Cell Physiology
    • Azad, A.K.1    Katsuhara, M.2    Ishikawa, T.3    Sawa, Y.4    Ishikawa, T.5    Shibata, H.6
  • 8
    • 0036919076 scopus 로고    scopus 로고
    • Temperature response of mesophyll conductance: Implications for the determination of Rubisco enzyme kinetics and for limitations to photosynthesis in vivo
    • doi: 10.1104/pp.008250
    • Bernacchi CJ, Portis AR, Nakano H, von Caemmerer S, Long SP (2002) Temperature response of mesophyll conductance: implications for the determination of Rubisco enzyme kinetics and for limitations to photosynthesis in vivo. Plant Physiology 130, 1992-1998. doi: 10.1104/pp.008250
    • (2002) Plant Physiology , vol.130 , pp. 1992-1998
    • Bernacchi, C.J.1    Portis, A.R.2    Nakano, H.3    von Caemmerer, S.4    Long, S.P.5
  • 10
    • 33644659755 scopus 로고    scopus 로고
    • Early effects of salinity on water transport in Arabidopsis roots. Molecular and cellular features of aquaporin expression
    • doi: 10.1104/pp.105.065029
    • Boursiac Y, Chen S, Luu DT, Sorieul M, van den Dries N, Maurel C (2005) Early effects of salinity on water transport in Arabidopsis roots. Molecular and cellular features of aquaporin expression. Plant Physiology 139, 790-805. doi: 10.1104/pp.105.065029
    • (2005) Plant Physiology , vol.139 , pp. 790-805
    • Boursiac, Y.1    Chen, S.2    Luu, D.T.3    Sorieul, M.4    van den Dries, N.5    Maurel, C.6
  • 11
    • 0037398066 scopus 로고    scopus 로고
    • 2] to estimate diffusional and non-diffusional limitations of photosynthetic capacity of salt-stressed olive saplings
    • doi: 10.1046/j.1365-3040.2003.00993.x
    • 2] to estimate diffusional and non-diffusional limitations of photosynthetic capacity of salt-stressed olive saplings. Plant, Cell & Environment 26, 585-594. doi: 10.1046/j.1365-3040.2003.00993.x
    • (2003) Plant, Cell & Environment , vol.26 , pp. 585-594
    • Centritto, M.1    Loreto, F.2    Chartzoulaks, K.3
  • 12
    • 0033996879 scopus 로고    scopus 로고
    • Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity
    • doi: 10.1104/pp.122.4.1025
    • 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 Physiology 122, 1025-1034. doi: 10.1104/pp.122.4.1025
    • (2000) Plant Physiology , vol.122 , pp. 1025-1034
    • Chaumont, F.1    Barrieu, F.2    Jung, R.3    Chrispeels, M.J.4
  • 13
    • 0035106823 scopus 로고    scopus 로고
    • Aquaporins constitute a large and highly divergent protein family in maize
    • doi: 10.1104/pp.125.3.1206
    • Chaumont F, Barrieu F, Wojcik E, Chrispeels MJ, Jung R (2001) Aquaporins constitute a large and highly divergent protein family in maize. Plant Physiology 125, 1206-1215. doi: 10.1104/pp.125.3.1206
    • (2001) Plant Physiology , vol.125 , pp. 1206-1215
    • Chaumont, F.1    Barrieu, F.2    Wojcik, E.3    Chrispeels, M.J.4    Jung, R.5
  • 14
    • 26944462019 scopus 로고    scopus 로고
    • Regulation of plant aquaporin activity
    • doi: 10.1042/BC20040133
    • Chaumont F, Moshelion M, Daniels MK (2005) Regulation of plant aquaporin activity. Biology of the Cell 97, 749-764. doi: 10.1042/BC20040133
    • (2005) Biology of the Cell , vol.97 , pp. 749-764
    • Chaumont, F.1    Moshelion, M.2    Daniels, M.K.3
  • 15
    • 0035038056 scopus 로고    scopus 로고
    • Inhibiting expression of a tomato ripening-associated membrane protein increases organic acids and reduces sugar levels of fruit
    • doi: 10.1007/s004250000431
    • Chen G, Wilson ID, Kim SH, Grierson D (2001) Inhibiting expression of a tomato ripening-associated membrane protein increases organic acids and reduces sugar levels of fruit. Planta 212, 799-807. doi: 10.1007/s004250000431
    • (2001) Planta , vol.212 , pp. 799-807
    • Chen, G.1    Wilson, I.D.2    Kim, S.H.3    Grierson, D.4
  • 18
    • 0033579547 scopus 로고    scopus 로고
    • Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography
    • doi: 10.1006/jmbi.1999.3293
    • Daniels MJ, Chrispeels MJ, Yeager M (1999) Projection structure of a plant vacuole membrane aquaporin by electron cryo-crystallography. Journal of Molecular Biology 294, 1337-1349. doi: 10.1006/jmbi.1999.3293
    • (1999) Journal of Molecular Biology , vol.294 , pp. 1337-1349
    • Daniels, M.J.1    Chrispeels, M.J.2    Yeager, M.3
  • 19
    • 0442314368 scopus 로고    scopus 로고
    • The relative limitation of photosynthesis by mesophyll conductance in co-occurring species in a temperate rainforest dominated by the conifer Dacrydium cupressinum
    • doi: 10.1071/FP03141
    • De Lucia EH, Whitehead D, Clearwater MJ (2003) The relative limitation of photosynthesis by mesophyll conductance in co-occurring species in a temperate rainforest dominated by the conifer Dacrydium cupressinum. Functional Plant Biology 30, 1197-1204. doi: 10.1071/FP03141
    • (2003) Functional Plant Biology , vol.30 , pp. 1197-1204
    • De Lucia, E.H.1    Whitehead, D.2    Clearwater, M.J.3
  • 20
    • 1242299060 scopus 로고    scopus 로고
    • Overexpression of a lily PIP1 gene in tobacco increased the osmotic water permeability of leaf cells
    • doi: 10.1046/j.0016-8025.2003. 01130.x
    • Ding X, Iwasaki I, Kitagawa Y (2004) Overexpression of a lily PIP1 gene in tobacco increased the osmotic water permeability of leaf cells. Plant, Cell & Environment 27, 177-186. doi: 10.1046/j.0016-8025.2003. 01130.x
    • (2004) Plant, Cell & Environment , vol.27 , pp. 177-186
    • Ding, X.1    Iwasaki, I.2    Kitagawa, Y.3
  • 21
    • 0842291747 scopus 로고    scopus 로고
    • Interactions between plasma membrane aquaporins modulate their water channel activity
    • doi: 10.1105/tpc.017194
    • Fetter K, Wider VV, Moshelion M, Chaumont F (2004) Interactions between plasma membrane aquaporins modulate their water channel activity. The Plant Cell 16, 215-228. doi: 10.1105/tpc.017194
    • (2004) The Plant Cell , vol.16 , pp. 215-228
    • Fetter, K.1    Wider, V.V.2    Moshelion, M.3    Chaumont, F.4
  • 23
    • 23944485708 scopus 로고    scopus 로고
    • The distribution of aquaporin subtypes (PIP1, PIP2 and γ-TIP) is tissue dependent in soybean (Glycine max) root nodules
    • doi: 10.1093/aob/mci195
    • Fleurat-Lessard P, Michonneau P, Maeshima M, Drevon JJ, Serraj R (2005) The distribution of aquaporin subtypes (PIP1, PIP2 and γ-TIP) is tissue dependent in soybean (Glycine max) root nodules. Annals of Botany 96, 457-460. doi: 10.1093/aob/mci195
    • (2005) Annals of Botany , vol.96 , pp. 457-460
    • Fleurat-Lessard, P.1    Michonneau, P.2    Maeshima, M.3    Drevon, J.J.4    Serraj, R.5
  • 24
    • 0036335502 scopus 로고    scopus 로고
    • Effects of drought on photosynthesis in grapevines under field conditions: An evaluation of stomatal and mesophyll limitations
    • doi: 10.1071/PP01119
    • Flexas J, Bota J, Escalona JM, Sampol B, Medrano H (2002) Effects of drought on photosynthesis in grapevines under field conditions: an evaluation of stomatal and mesophyll limitations. Functional Plant Biology 29, 461-471. doi: 10.1071/PP01119
    • (2002) Functional Plant Biology , vol.29 , pp. 461-471
    • Flexas, J.1    Bota, J.2    Escalona, J.M.3    Sampol, B.4    Medrano, H.5
  • 29
    • 0034746073 scopus 로고    scopus 로고
    • Expression and distribution of vacuolar aquaporin in young and mature leaf tissues of Brassica napus in relation to water fluxes
    • doi: 10.1007/s004250000390
    • Frangne N, Maeshima M, Schäffner AR, Mandel T, Martinoia E, Bonnemain JL (2001) Expression and distribution of vacuolar aquaporin in young and mature leaf tissues of Brassica napus in relation to water fluxes. Planta 212, 270-278. doi: 10.1007/s004250000390
    • (2001) Planta , vol.212 , pp. 270-278
    • Frangne, N.1    Maeshima, M.2    Schäffner, A.R.3    Mandel, T.4    Martinoia, E.5    Bonnemain, J.L.6
  • 30
    • 0028371413 scopus 로고
    • Nucleotide sequence and expression of a ripening and water stress-related cDNA from tomato with homology to the MIP class of membrane channel proteins
    • doi: 10.1007/BF00024122
    • Fray RG, Wallace A, Grierson D, Lycett GW (1994) Nucleotide sequence and expression of a ripening and water stress-related cDNA from tomato with homology to the MIP class of membrane channel proteins. Plant Molecular Biology 24, 539-543. doi: 10.1007/BF00024122
    • (1994) Plant Molecular Biology , vol.24 , pp. 539-543
    • Fray, R.G.1    Wallace, A.2    Grierson, D.3    Lycett, G.W.4
  • 31
    • 0036011030 scopus 로고    scopus 로고
    • The water permeability of Arabidopsis plasma membrane is regulated by divalent cations and pH
    • doi: 10.1046/j.1365-313X.2002.01268.x
    • Gerbeau P, Amodeo G, Henzler T, Santoni V, Ripoche P, Maurel C (2002) The water permeability of Arabidopsis plasma membrane is regulated by divalent cations and pH. The Plant Journal 30, 71-81. doi: 10.1046/j.1365-313X.2002.01268.x
    • (2002) The Plant Journal , vol.30 , pp. 71-81
    • Gerbeau, P.1    Amodeo, G.2    Henzler, T.3    Santoni, V.4    Ripoche, P.5    Maurel, C.6
  • 32
    • 28444450878 scopus 로고    scopus 로고
    • Lipid-protein interactions in double-layered two-dimensional AQP0 crystals
    • doi: 10.1038/nature04321
    • Gonen T, Cheng Y, Sliz P, Hiroaki Y, Fujiyoshi Y, Harrison SC, Walz T (2005) Lipid-protein interactions in double-layered two-dimensional AQP0 crystals. Nature 438, 633-638. doi: 10.1038/nature04321
    • (2005) Nature , vol.438 , pp. 633-638
    • Gonen, T.1    Cheng, Y.2    Sliz, P.3    Hiroaki, Y.4    Fujiyoshi, Y.5    Harrison, S.C.6    Walz, T.7
  • 33
    • 33644537059 scopus 로고    scopus 로고
    • Phloem hydrostatic pressure relates to solute loading rate: A direct test of the Münch hypothesis
    • doi: 10.1071/FP05036
    • Gould N, Thorpe MR, Koroleva O, Minchin PEH (2005) Phloem hydrostatic pressure relates to solute loading rate: a direct test of the Münch hypothesis. Functional Plant Biology 32, 1019-1026. doi: 10.1071/FP05036
    • (2005) Functional Plant Biology , vol.32 , pp. 1019-1026
    • Gould, N.1    Thorpe, M.R.2    Koroleva, O.3    Minchin, P.E.H.4
  • 34
    • 0037394367 scopus 로고    scopus 로고
    • Phosphorylation of soybean nodulin 26 on serine-262 enhances water permeability and is regulated developmentally and by osmotic signals
    • doi: 10.1105/tpc.009787
    • Guenther JF, Chanmanivone N, Galetovic MP, Wallace IS, Cobb JA, Roberts DM (2003) Phosphorylation of soybean nodulin 26 on serine-262 enhances water permeability and is regulated developmentally and by osmotic signals. The Plant Cell 15, 981-991. doi: 10.1105/tpc.009787
    • (2003) The Plant Cell , vol.15 , pp. 981-991
    • Guenther, J.F.1    Chanmanivone, N.2    Galetovic, M.P.3    Wallace, I.S.4    Cobb, J.A.5    Roberts, D.M.6
  • 35
    • 33748538734 scopus 로고    scopus 로고
    • Localisation and quantification of plasma membrane aquaporin expression in maize primary root: A clue to understanding their role as cellular plumbers
    • doi: 10.1007/s11103-006-9022-1
    • Hachez C, Moshelion M, Zelazny E, Cavez D, Chaumont F (2006a) Localisation and quantification of plasma membrane aquaporin expression in maize primary root: a clue to understanding their role as cellular plumbers. Plant Molecular Biology 62, 305-323. doi: 10.1007/s11103-006-9022-1
    • (2006) Plant Molecular Biology , vol.62 , pp. 305-323
    • Hachez, C.1    Moshelion, M.2    Zelazny, E.3    Cavez, D.4    Chaumont, F.5
  • 36
    • 33748563984 scopus 로고    scopus 로고
    • Modulating the expression of aquaporin genes in planta: A key to understand their physiological functions?
    • doi: 10.1016/j.bbamem.2006.02.017
    • Hachez C, Zelazny E, Chaumont F (2006b) Modulating the expression of aquaporin genes in planta: a key to understand their physiological functions? Biochimica et Biophysica Acta 1758, 1142-1156. doi: 10.1016/j.bbamem.2006.02.017
    • (2006) Biochimica et Biophysica Acta , vol.1758 , pp. 1142-1156
    • Hachez, C.1    Zelazny, E.2    Chaumont, F.3
  • 37
    • 0036319916 scopus 로고    scopus 로고
    • The effect of growth irradiance on leaf anatomy and photosynthesis in Acer species differing in light adaptation
    • doi: 10.1046/j.1365-3040.2002.00881.x
    • Hanba YT, Kogami H, Terashima I (2002) The effect of growth irradiance on leaf anatomy and photosynthesis in Acer species differing in light adaptation. Plant, Cell & Environment 25, 1021-1030. doi: 10.1046/j.1365-3040.2002.00881.x
    • (2002) Plant, Cell & Environment , vol.25 , pp. 1021-1030
    • Hanba, Y.T.1    Kogami, H.2    Terashima, I.3
  • 40
    • 33645968400 scopus 로고    scopus 로고
    • Diacidic motifs influence the export of transmembrane proteins from the endoplasmic reticulum in plant cells
    • doi: 10.1105/tpc.105.034900
    • Hanton SL, Renna L, Bortolotti LE, Chatre L, Stefano G, Brandizzi F (2005) Diacidic motifs influence the export of transmembrane proteins from the endoplasmic reticulum in plant cells. The Plant Cell 17, 3081-3093. doi: 10.1105/tpc.105.034900
    • (2005) The 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
  • 41
    • 0034671791 scopus 로고    scopus 로고
    • Orchestrated transcription of key pathways in Arabidopsis by the circadian clock
    • doi: 10.1126/science.290.5499.2110
    • Harmer SL, Hogenesch JB, Straume M, Chang H-S, Han B, Zhu T, Wang X, Kreps JA, Kay SA (2000) Orchestrated transcription of key pathways in Arabidopsis by the circadian clock. Science 290, 2110-2113. doi: 10.1126/science.290.5499.2110
    • (2000) Science , vol.290 , pp. 2110-2113
    • Harmer, S.L.1    Hogenesch, J.B.2    Straume, M.3    Chang, H.-S.4    Han, B.5    Zhu, T.6    Wang, X.7    Kreps, J.A.8    Kay, S.A.9
  • 43
    • 0033407429 scopus 로고    scopus 로고
    • Diurnal variations in hydraulic conductivity and root pressure can be correlated with the expression of putative aquaporins in the roots of Lotus japonicus
    • doi: 10.1007/s004250050653
    • Henzler T, Waterhouse RN, Smyth AJ, Carvajal M, Cooke DT, Schäffner AR, Steudle E, Clarkson DT (1999) Diurnal variations in hydraulic conductivity and root pressure can be correlated with the expression of putative aquaporins in the roots of Lotus japonicus. Planta 210, 50-60. doi: 10.1007/s004250050653
    • (1999) Planta , vol.210 , pp. 50-60
    • Henzler, T.1    Waterhouse, R.N.2    Smyth, A.J.3    Carvajal, M.4    Cooke, D.T.5    Schäffner, A.R.6    Steudle, E.7    Clarkson, D.T.8
  • 44
    • 0032169820 scopus 로고    scopus 로고
    • Molecular cloning, water channel activity and tissue specific expression of two isoforms of radish vacuolar aquaporin
    • Higuchi T, Suga S, Tsuchiya T, Hisada H, Morishima S, Okada Y, Maeshima M (1998) Molecular cloning, water channel activity and tissue specific expression of two isoforms of radish vacuolar aquaporin. Plant & Cell Physiology 39, 905-913.
    • (1998) Plant & Cell Physiology , vol.39 , pp. 905-913
    • Higuchi, T.1    Suga, S.2    Tsuchiya, T.3    Hisada, H.4    Morishima, S.5    Okada, Y.6    Maeshima, M.7
  • 45
    • 33749239436 scopus 로고    scopus 로고
    • Refilling of embolised conduits as a consequence of 'Münch water' circulation
    • doi: 10.1071/FP06108
    • Höltta T, Vesala T, Perämäki M, Nikinmaa E (2006) Refilling of embolised conduits as a consequence of 'Münch water' circulation. Functional Plant Biology 33, 949-959. doi: 10.1071/FP06108
    • (2006) Functional Plant Biology , vol.33 , pp. 949-959
    • Höltta, T.1    Vesala, T.2    Perämäki, M.3    Nikinmaa, E.4
  • 46
    • 0042877151 scopus 로고    scopus 로고
    • Putative PIP1 genes isolated from apple: Expression analyses during fruit development and under osmotic stress
    • doi: 10.1093/jxb/erg238
    • Hu CG, Hao YJ, Honda C, Kita M, Moriguchi T (2003) Putative PIP1 genes isolated from apple: expression analyses during fruit development and under osmotic stress. Journal of Experimental Botany 54, 2193-2194. doi: 10.1093/jxb/erg238
    • (2003) Journal of Experimental Botany , vol.54 , pp. 2193-2194
    • Hu, C.G.1    Hao, Y.J.2    Honda, C.3    Kita, M.4    Moriguchi, T.5
  • 47
    • 26844545473 scopus 로고    scopus 로고
    • Three SIP aquaporins of Arabidopsis are localised in the ER membrane and expressed in a tissue- and cell-specific manner
    • Ishikawa F, Suga S, Uemura T, Sato MH, Maeshima M (2005) Three SIP aquaporins of Arabidopsis are localised in the ER membrane and expressed in a tissue- and cell-specific manner. FEBS Letters 579, 5814-5820.
    • (2005) FEBS Letters , vol.579 , pp. 5814-5820
    • Ishikawa, F.1    Suga, S.2    Uemura, T.3    Sato, M.H.4    Maeshima, M.5
  • 48
    • 33748560815 scopus 로고    scopus 로고
    • Aquaporin subfamily with unusual NPA boxes
    • doi: 10.1016/j.bbamem.2006.02.024
    • Ishibashi K (2006) Aquaporin subfamily with unusual NPA boxes. Biochimica et Biophysica Acta 1758, 989-993. doi: 10.1016/j.bbamem.2006.02.024
    • (2006) Biochimica et Biophysica Acta , vol.1758 , pp. 989-993
    • Ishibashi, K.1
  • 50
    • 12444323669 scopus 로고    scopus 로고
    • An expression analysis of a gene family encoding plasma membrane aquaporins in response to abiotic stresses in Arabidopsis thaliana
    • doi: 10.1023/B:PLAN.0000040900.61345.a6
    • Jang JY, Kim DG, Kim YO, Kim JS, Kang H (2004) An expression analysis of a gene family encoding plasma membrane aquaporins in response to abiotic stresses in Arabidopsis thaliana. Plant Molecular Biology 54, 713-725. doi: 10.1023/B:PLAN.0000040900.61345.a6
    • (2004) Plant Molecular Biology , vol.54 , pp. 713-725
    • Jang, J.Y.1    Kim, D.G.2    Kim, Y.O.3    Kim, J.S.4    Kang, H.5
  • 51
    • 0037327613 scopus 로고    scopus 로고
    • Role of a single aquaporin isoform in root water uptake
    • doi: 10.1105/tpc.008888
    • Javot H, Lauvergeat V, Santoni V, Martin-Laurent F, Guclu J, et al. (2003) Role of a single aquaporin isoform in root water uptake. The Plant Cell 15, 509-522. doi: 10.1105/tpc.008888
    • (2003) The Plant Cell , vol.15 , pp. 509-522
    • Javot, H.1    Lauvergeat, V.2    Santoni, V.3    Martin-Laurent, F.4    Guclu, J.5
  • 54
    • 0032029335 scopus 로고    scopus 로고
    • Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation
    • doi: 10.2307/3870601
    • Johansson I, Karlsson M, Shukla VK, Chrispeels MJ, Larsson C, Kjellbom P (1998) Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation. The Plant Cell 10, 451-459. doi: 10.2307/3870601
    • (1998) The Plant Cell , vol.10 , pp. 451-459
    • Johansson, I.1    Karlsson, M.2    Shukla, V.K.3    Chrispeels, M.J.4    Larsson, C.5    Kjellbom, P.6
  • 55
    • 0034870819 scopus 로고    scopus 로고
    • The complete set of genes encoding major intrinsic proteins in Arabidopsis provides a framework for new nomenclature for major intrinsic proteins in plants
    • doi: 10.1104/pp.126.4.1358
    • Johanson U, Karlsson M, Johansson I, Gustavsson S, Sjövall S, Fraysse L, Weig AR, Kjellbom P (2001) The complete set of genes encoding major intrinsic proteins in Arabidopsis provides a framework for new nomenclature for major intrinsic proteins in plants. Plant Physiology 126, 1358-1369. doi: 10.1104/pp.126.4.1358
    • (2001) Plant Physiology , vol.126 , pp. 1358-1369
    • Johanson, U.1    Karlsson, M.2    Johansson, I.3    Gustavsson, S.4    Sjövall, S.5    Fraysse, L.6    Weig, A.R.7    Kjellbom, P.8
  • 56
    • 0001222337 scopus 로고
    • Tonoplast-bound protein-kinase phosphorylates tonoplast intrinsic protein
    • Johnson KD, Chrispeels MJ (1992) Tonoplast-bound protein-kinase phosphorylates tonoplast intrinsic protein. Plant Physiology 100, 1787-1795.
    • (1992) Plant Physiology , vol.100 , pp. 1787-1795
    • Johnson, K.D.1    Chrispeels, M.J.2
  • 57
    • 0001438180 scopus 로고
    • An abundant, highly conserved tonoplast protein in seeds
    • Johnson KD, Herman EM, Chrispeels MJ (1989) An abundant, highly conserved tonoplast protein in seeds. Plant Physiology 91, 1006-1013.
    • (1989) Plant Physiology , vol.91 , pp. 1006-1013
    • Johnson, K.D.1    Herman, E.M.2    Chrispeels, M.J.3
  • 58
    • 0032054595 scopus 로고    scopus 로고
    • Significance of plasmalemma aquaporins for water transport in Arabidopsis thaliana
    • doi: 10.1046/j.1365-313X.1998.00111.x
    • Kaldenhoff R, Grote K, Zhu J-J, Zimmermann U (1998) Significance of plasmalemma aquaporins for water transport in Arabidopsis thaliana. The Plant Journal 14, 121-128. doi: 10.1046/j.1365-313X.1998.00111.x
    • (1998) The Plant Journal , vol.14 , pp. 121-128
    • Kaldenhoff, R.1    Grote, K.2    Zhu, J.-J.3    Zimmermann, U.4
  • 59
    • 33748625436 scopus 로고    scopus 로고
    • Functional aquaporin diversity in plants
    • doi: 10.1016/j.bbamem.2006.03.012
    • Kaldenhoff R, Fischer M (2006a) Functional aquaporin diversity in plants. Biochimica et Biophysica Acta 1758, 1134-1141. doi: 10.1016/j.bbamem.2006.03.012
    • (2006) Biochimica et Biophysica Acta , vol.1758 , pp. 1134-1141
    • Kaldenhoff, R.1    Fischer, M.2
  • 60
    • 33744792311 scopus 로고    scopus 로고
    • Aquaporins in plants
    • doi: 10.1111/j.1748-1716.2006.01563.x
    • Kaldenhoff R, Fischer M (2006b) Aquaporins in plants. Acta Physiologica 187, 169-176. doi: 10.1111/j.1748-1716.2006.01563.x
    • (2006) Acta Physiologica , vol.187 , pp. 169-176
    • Kaldenhoff, R.1    Fischer, M.2
  • 63
    • 0347031175 scopus 로고    scopus 로고
    • Expression of an aquaporin at night in relation to the growth and root water permeability in barley seedlings
    • Katsuhara M, Koshio K, Shibasaka M, Kasamo K (2003a) Expression of an aquaporin at night in relation to the growth and root water permeability in barley seedlings. Soil Science and Plant Nutrition 49, 883-888.
    • (2003) Soil Science and Plant Nutrition , vol.49 , pp. 883-888
    • Katsuhara, M.1    Koshio, K.2    Shibasaka, M.3    Kasamo, K.4
  • 64
    • 0742305477 scopus 로고    scopus 로고
    • Over-expression of a barely aquaporin increased the shoot/root ratio and raised salt sensitivity in transgenic rice plants
    • doi: 10.1093/pcp/pcg167
    • Katsuhara M, Koshio K, Shibasaka M, Hayashi Y, Hayakawa T, Kasamo K (2003b) Over-expression of a barely aquaporin increased the shoot/root ratio and raised salt sensitivity in transgenic rice plants. Plant & Cell Physiology 44, 1378-1383. doi: 10.1093/pcp/pcg167
    • (2003) Plant & Cell Physiology , vol.44 , pp. 1378-1383
    • Katsuhara, M.1    Koshio, K.2    Shibasaka, M.3    Hayashi, Y.4    Hayakawa, T.5    Kasamo, K.6
  • 65
    • 4644220261 scopus 로고    scopus 로고
    • Mechanism of ammonia transport by Amt/MEP/Rh: Structure of AmtB at 1.35 Å
    • doi: 10.1126/science.1101952
    • Khademi S, O'Connell J III, Remis J, Robles-Colmenares Y, Miercke LJW, Stroud RM (2004) Mechanism of ammonia transport by Amt/MEP/Rh: structure of AmtB at 1.35 Å. Science 305, 1587-1594. doi: 10.1126/science.1101952
    • (2004) Science , vol.305 , pp. 1587-1594
    • Khademi, S.1    O'Connell III, J.2    Remis, J.3    Robles-Colmenares, Y.4    Miercke, L.J.W.5    Stroud, R.M.6
  • 67
    • 0038643780 scopus 로고    scopus 로고
    • A defect in the yeast plasma membrane urea transporter Dur3p is complemented by CpNIP1, a Nod26-like protein from zucchini (Cucurbita pepo L.), and by Arabidopsis thaliana δ-TIP or γ-TIP
    • doi: 10.1016/S0014-5793(03)00671-9
    • Klebl F, Wolf M, Sauer N (2003) A defect in the yeast plasma membrane urea transporter Dur3p is complemented by CpNIP1, a Nod26-like protein from zucchini (Cucurbita pepo L.), and by Arabidopsis thaliana δ-TIP or γ-TIP. FEBS Letters 547, 69-74. doi: 10.1016/S0014-5793(03)00671-9
    • (2003) FEBS Letters , vol.547 , pp. 69-74
    • Klebl, F.1    Wolf, M.2    Sauer, N.3
  • 68
    • 33646121272 scopus 로고    scopus 로고
    • Immunochemical analysis of aquaporin isoforms in Arabidopsis suspension cultured cells
    • doi: 10.1271/bbb.70.980
    • Kobae Y, Mizutani M, Segami S, Maeshima M (2006) Immunochemical analysis of aquaporin isoforms in Arabidopsis suspension cultured cells. Bioscience, Biotechnology, and Biochemistry 70, 980-987. doi: 10.1271/bbb.70.980
    • (2006) Bioscience, Biotechnology, and Biochemistry , vol.70 , pp. 980-987
    • Kobae, Y.1    Mizutani, M.2    Segami, S.3    Maeshima, M.4
  • 70
    • 0031424702 scopus 로고    scopus 로고
    • Genetic variation in photosynthetic capacity, carbon isotope discrimination and mesophyll conductance in provenances of Castanea sativa adapted to different environments
    • doi: 10.1046/j.1365-2435.1997. 00140.x
    • Lauteri M, Scartazza A, Guido MC, Brugnoli E (1997) Genetic variation in photosynthetic capacity, carbon isotope discrimination and mesophyll conductance in provenances of Castanea sativa adapted to different environments. Functional Ecology 11, 675-683. doi: 10.1046/j.1365-2435.1997. 00140.x
    • (1997) Functional Ecology , vol.11 , pp. 675-683
    • Lauteri, M.1    Scartazza, A.2    Guido, M.C.3    Brugnoli, E.4
  • 71
    • 4043084181 scopus 로고    scopus 로고
    • Rapid accumulation of hydrogen peroxide in cucumber roots due to exposure to low temperature appears to mediate decreases in water transport
    • doi: 10.1093/jxb/erh189
    • Lee SH, Singh AP, Chung GC (2004) Rapid accumulation of hydrogen peroxide in cucumber roots due to exposure to low temperature appears to mediate decreases in water transport. Journal of Experimental Botany 55, 1733-1741. doi: 10.1093/jxb/erh189
    • (2004) Journal of Experimental Botany , vol.55 , pp. 1733-1741
    • Lee, S.H.1    Singh, A.P.2    Chung, G.C.3
  • 72
    • 38549159626 scopus 로고    scopus 로고
    • Abiotic stress modulate expression of genes encoding the tonoplast intrinsic proteins in barley
    • Ligaba A, Katsuhara M (2007) Abiotic stress modulate expression of genes encoding the tonoplast intrinsic proteins in barley. Plant & Cell Physiology 48(supplement), s19.
    • (2007) Plant & Cell Physiology , vol.48 , Issue.SUPPL.EMENT
    • Ligaba, A.1    Katsuhara, M.2
  • 73
    • 0345392686 scopus 로고    scopus 로고
    • Urea transport by nitrogen-regulated tonoplast intrinsic proteins in Arabidopsis
    • doi: 10.1104/pp.103.027409
    • Liu LH, Ludewig U, Gassert B, Frommer WB, von Wiren N (2003) Urea transport by nitrogen-regulated tonoplast intrinsic proteins in Arabidopsis. Plant Physiology 133, 1220-1228. doi: 10.1104/pp.103.027409
    • (2003) Plant Physiology , vol.133 , pp. 1220-1228
    • Liu, L.H.1    Ludewig, U.2    Gassert, B.3    Frommer, W.B.4    von Wiren, N.5
  • 74
    • 84989134679 scopus 로고
    • 2 diffusion from stomata to the site of carboxylation in leaves of woody species
    • doi: 10.1111/j.1365-3040.1992.tb01021.x
    • 2 diffusion from stomata to the site of carboxylation in leaves of woody species. Plant, Cell & Environment 15, 873-899. doi: 10.1111/j.1365-3040.1992.tb01021.x
    • (1992) Plant, Cell & Environment , vol.15 , pp. 873-899
    • Lloyd, J.1    Syvertsen, J.P.2    Kriedemann, P.E.3    Farquhar, G.D.4
  • 76
    • 0037396923 scopus 로고    scopus 로고
    • Photosynthetic limitations in olive cultivars with different sensitivity to salt stress
    • doi: 10.1046/j.1365-3040.2003.00994.x
    • Loreto F, Centritto M, Chartzoulakis K (2003) Photosynthetic limitations in olive cultivars with different sensitivity to salt stress. Plant, Cell & Environment 26, 595-601. doi: 10.1046/j.1365-3040.2003.00994.x
    • (2003) Plant, Cell & Environment , vol.26 , pp. 595-601
    • Loreto, F.1    Centritto, M.2    Chartzoulakis, K.3
  • 78
    • 34447328403 scopus 로고    scopus 로고
    • Expression of PIP1 and PIP2 aquaporins is enhanced in olive dwarf genotypes and is related to root and leaf hydraulic conductance
    • doi: 10.1111/j.1399-3054.2007.00902.x
    • Lovisolo C, Secchi F, Nardini A, Salleo S, Buffa R, Schubert A (2007) Expression of PIP1 and PIP2 aquaporins is enhanced in olive dwarf genotypes and is related to root and leaf hydraulic conductance. Physiologia Plantarum 130, 543-551. doi: 10.1111/j.1399-3054.2007.00902.x
    • (2007) Physiologia Plantarum , vol.130 , pp. 543-551
    • Lovisolo, C.1    Secchi, F.2    Nardini, A.3    Salleo, S.4    Buffa, R.5    Schubert, A.6
  • 79
    • 38549112038 scopus 로고    scopus 로고
    • Computational and experimental analysis of aquaporins
    • Ludewig U, Dynowski M, Mayer M (2006) Computational and experimental analysis of aquaporins. Plant & Cell Physiology 47(supplement) , s19.
    • (2006) Plant & Cell Physiology , vol.47 , Issue.SUPPL.EMENT
    • Ludewig, U.1    Dynowski, M.2    Mayer, M.3
  • 80
    • 12444298048 scopus 로고    scopus 로고
    • Aquaporins in a challenging environment: Molecular gears for adjusting plant water status
    • doi: 10.1111/j.1365-3040.2004.01295.x
    • Luu DT, Maurel C (2005) Aquaporins in a challenging environment: molecular gears for adjusting plant water status. Plant, Cell & Environment 28, 85-96. doi: 10.1111/j.1365-3040.2004.01295.x
    • (2005) Plant, Cell & Environment , vol.28 , pp. 85-96
    • Luu, D.T.1    Maurel, C.2
  • 83
    • 11144248492 scopus 로고    scopus 로고
    • Loss of TIP1;1 aquaporin in Arabidopsis leads to cell and plant death
    • doi: 10.1111/j.1365-313X.2004.02265.x
    • Ma S, Quist TM, Ulanov A, Joly R, Bohnert HJ (2004) Loss of TIP1;1 aquaporin in Arabidopsis leads to cell and plant death. The Plant Journal 40, 845-859. doi: 10.1111/j.1365-313X.2004.02265.x
    • (2004) The Plant Journal , vol.40 , pp. 845-859
    • Ma, S.1    Quist, T.M.2    Ulanov, A.3    Joly, R.4    Bohnert, H.J.5
  • 84
    • 0001411554 scopus 로고
    • Characterisation of the major integral protein of vacuolar membrane
    • Maeshima M (1992) Characterisation of the major integral protein of vacuolar membrane. Plant Physiology 98, 1248-1254.
    • (1992) Plant Physiology , vol.98 , pp. 1248-1254
    • Maeshima, M.1
  • 85
    • 0035781089 scopus 로고    scopus 로고
    • Tonoplast transporters: Organisation and function
    • doi: 10.1146/annurev.arplant.52.1.469
    • Maeshima M (2001) Tonoplast transporters: organisation and function. Annual Review of Plant Physiology and Plant Molecular Biology 52, 469-497. doi: 10.1146/annurev.arplant.52.1.469
    • (2001) Annual Review of Plant Physiology and Plant Molecular Biology , vol.52 , pp. 469-497
    • Maeshima, M.1
  • 86
    • 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. The EMBO Journal 14, 3028-3035.
    • (1995) The EMBO Journal , vol.14 , pp. 3028-3035
    • Maurel, C.1    Kado, R.T.2    Guern, J.3    Chrispeels, M.J.4
  • 88
    • 0026721375 scopus 로고
    • Topology and phosphorylation of soybean nodulin-26, an intrinsic protein of the peribacteroid membrane
    • doi: 10.1083/jcb.118.2.481
    • Miao GH, Hong Z, Verma DP (1992) Topology and phosphorylation of soybean nodulin-26, an intrinsic protein of the peribacteroid membrane. Journal of Cell Biology 118, 481-490. doi: 10.1083/jcb.118.2.481
    • (1992) Journal of Cell Biology , vol.118 , pp. 481-490
    • Miao, G.H.1    Hong, Z.2    Verma, D.P.3
  • 89
    • 33750276372 scopus 로고    scopus 로고
    • Isolation of cDNA clones corresponding to genes differentially expressed in pericarp of mume (Prunus mume) in response to ripening, ethylene and wounding signals
    • doi: 10.1111/j.1399-3054.2006.00749.x
    • Mita S, Nagai Y, Asai T (2006) Isolation of cDNA clones corresponding to genes differentially expressed in pericarp of mume (Prunus mume) in response to ripening, ethylene and wounding signals. Physiologia Plantarum 128, 531-545. doi: 10.1111/j.1399-3054.2006.00749.x
    • (2006) Physiologia Plantarum , vol.128 , pp. 531-545
    • Mita, S.1    Nagai, Y.2    Asai, T.3
  • 90
    • 33750597729 scopus 로고    scopus 로고
    • Aquaporin NIP2;1 is mainly localised to the ER membrane and shows root-specific accumulation in Arabidopsis thaliana
    • doi: 10.1093/pcp/pcl004
    • Mizutani M, Watanabe S, Nakagawa T, Maeshima M (2006) Aquaporin NIP2;1 is mainly localised to the ER membrane and shows root-specific accumulation in Arabidopsis thaliana. Plant & Cell Physiology 47, 1420-1426. doi: 10.1093/pcp/pcl004
    • (2006) Plant & Cell Physiology , vol.47 , pp. 1420-1426
    • Mizutani, M.1    Watanabe, S.2    Nakagawa, T.3    Maeshima, M.4
  • 91
    • 23844498483 scopus 로고    scopus 로고
    • Disruption of aquaporin-11 produces polycystic kidneys following vacuolisation of the proximal tubule
    • doi: 10.1128/MCB.25.17.7770-7779.2005
    • Morishita Y, Matsuzaki T, Hara-Chikuma M, Andoo A, Shimono M, et al. (2005) Disruption of aquaporin-11 produces polycystic kidneys following vacuolisation of the proximal tubule. Molecular and Cellular Biology 25, 7770-7779. doi: 10.1128/MCB.25.17.7770-7779.2005
    • (2005) Molecular and Cellular Biology , vol.25 , pp. 7770-7779
    • Morishita, Y.1    Matsuzaki, T.2    Hara-Chikuma, M.3    Andoo, A.4    Shimono, M.5
  • 93
    • 4444271852 scopus 로고    scopus 로고
    • Dynamic changes in the osmotic water permeability of protoplast plasma membrane
    • doi: 10.1104/pp.104.043000
    • Moshelion M, Moran N, Chaumont F (2004) Dynamic changes in the osmotic water permeability of protoplast plasma membrane. Plant Physiology 135, 2301-2317. doi: 10.1104/pp.104.043000
    • (2004) Plant Physiology , vol.135 , pp. 2301-2317
    • Moshelion, M.1    Moran, N.2    Chaumont, F.3
  • 94
    • 33947243835 scopus 로고    scopus 로고
    • Osmotic water permeability of plasma and vacuolar membranes in protoplasts. I. High osmotic water permeability in radish (Raphanus sativus) root cells as measured by a new method
    • doi: 10.1007/s10265-006- 0035-2
    • Murai-Hatano M, Kuwagata T (2007) Osmotic water permeability of plasma and vacuolar membranes in protoplasts. I. High osmotic water permeability in radish (Raphanus sativus) root cells as measured by a new method. Journal of Plant Research 120, 175-189. doi: 10.1007/s10265-006- 0035-2
    • (2007) Journal of Plant Research , vol.120 , pp. 175-189
    • Murai-Hatano, M.1    Kuwagata, T.2
  • 96
    • 0033964857 scopus 로고    scopus 로고
    • Channel-mediated permeation of ammonia gas through the peribacteroid membrane of soybean nodules
    • doi: 10.1016/S0014-5793(99)01729-9
    • Niemietz CM, Tyerman SD (2000) Channel-mediated permeation of ammonia gas through the peribacteroid membrane of soybean nodules. FEBS Letters 465, 110-114. doi: 10.1016/S0014-5793(99)01729-9
    • (2000) FEBS Letters , vol.465 , pp. 110-114
    • Niemietz, C.M.1    Tyerman, S.D.2
  • 98
    • 33748568155 scopus 로고    scopus 로고
    • Regulation of aquaporin-2 trafficking and its binding protein complex
    • doi: 10.1016/j.bbamem.2006.03.004
    • Noda Y, Sasaki S (2006) Regulation of aquaporin-2 trafficking and its binding protein complex. Biochimica et Biophysica Acta 1758, 1117-1125. doi: 10.1016/j.bbamem.2006.03.004
    • (2006) Biochimica et Biophysica Acta , vol.1758 , pp. 1117-1125
    • Noda, Y.1    Sasaki, S.2
  • 99
    • 0034754544 scopus 로고    scopus 로고
    • Low aquaporin content and low osmotic water permeability of the plasma and vacuolar membranes of a CAM plant Graptopetalum paraguayense: Comparison with radish
    • doi: 10.1093/pcp/pce141
    • Ohshima Y, Iwasaki I, Suga S, Murakami M, Inoue K, Maeshima M (2001) Low aquaporin content and low osmotic water permeability of the plasma and vacuolar membranes of a CAM plant Graptopetalum paraguayense: comparison with radish. Plant & Cell Physiology 42, 1119-1129. doi: 10.1093/pcp/pce141
    • (2001) Plant & Cell Physiology , vol.42 , pp. 1119-1129
    • Ohshima, Y.1    Iwasaki, I.2    Suga, S.3    Murakami, M.4    Inoue, K.5    Maeshima, M.6
  • 100
    • 0041629006 scopus 로고    scopus 로고
    • Cloning and expression of two plasma membrane aquaporins expressed during the ripening of grape berry
    • doi: 10.1071/FP02116
    • Picaud S, Becq F, Dedaldechamp F, Ageorges A, Delrot S (2003) Cloning and expression of two plasma membrane aquaporins expressed during the ripening of grape berry. Functional Plant Biology 30, 621-630. doi: 10.1071/FP02116
    • (2003) Functional Plant Biology , vol.30 , pp. 621-630
    • Picaud, S.1    Becq, F.2    Dedaldechamp, F.3    Ageorges, A.4    Delrot, S.5
  • 101
    • 0026503030 scopus 로고    scopus 로고
    • Preston GM, Carroll TP, Guggino WB, Agre P (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256, 385-387. doi: 10.1126/science.256.5055.385
    • Preston GM, Carroll TP, Guggino WB, Agre P (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256, 385-387. doi: 10.1126/science.256.5055.385
  • 102
    • 0000179989 scopus 로고    scopus 로고
    • PIP1 aquaporins are concentrated in plasmalemmasomes of Arabidopsis thaliana mesophyll
    • Robinson DG, Sieber H, Kammerloher W, Schaffner AR (1996) PIP1 aquaporins are concentrated in plasmalemmasomes of Arabidopsis thaliana mesophyll. Plant Physiology 111, 645-649.
    • (1996) Plant Physiology , vol.111 , pp. 645-649
    • Robinson, D.G.1    Sieber, H.2    Kammerloher, W.3    Schaffner, A.R.4
  • 103
    • 0036008575 scopus 로고    scopus 로고
    • A complex and mobile structure forms a distinct subregion within the continuous vacuolar membrane in young cotyledons of Arabidopsis
    • doi: 10.1046/j.0960-7412.2001.01189.x
    • Saito C, Ueda T, Abe H, Wada Y, Kuroiwa T, Hisada A, Furuya M, Nakano A (2002) A complex and mobile structure forms a distinct subregion within the continuous vacuolar membrane in young cotyledons of Arabidopsis. The Plant Journal 29, 245-255. doi: 10.1046/j.0960-7412.2001.01189.x
    • (2002) The Plant Journal , vol.29 , pp. 245-255
    • Saito, C.1    Ueda, T.2    Abe, H.3    Wada, Y.4    Kuroiwa, T.5    Hisada, A.6    Furuya, M.7    Nakano, A.8
  • 104
    • 26444617525 scopus 로고    scopus 로고
    • Identification of 33 rice aquaporin genes and analysis of their expression and function
    • doi: 10.1093/pcp/pci172
    • Sakurai J, Ishikawa F, Yamaguchi T, Uemura M, Maeshima M (2005) Identification of 33 rice aquaporin genes and analysis of their expression and function. Plant & Cell Physiology 46, 1568-1577. doi: 10.1093/pcp/pci172
    • (2005) Plant & Cell Physiology , vol.46 , pp. 1568-1577
    • Sakurai, J.1    Ishikawa, F.2    Yamaguchi, T.3    Uemura, M.4    Maeshima, M.5
  • 105
    • 0033677662 scopus 로고    scopus 로고
    • The high diversity of aquaporins reveals novel facets of plant membrane functions
    • doi: 10.1016/S1369-5266(00)00116-3
    • Santoni V, Gerbeau P, Javot H, Maurel C (2000) The high diversity of aquaporins reveals novel facets of plant membrane functions. Current Opinion in Plant Biology 3, 476-481. doi: 10.1016/S1369-5266(00)00116-3
    • (2000) Current Opinion in Plant Biology , vol.3 , pp. 476-481
    • Santoni, V.1    Gerbeau, P.2    Javot, H.3    Maurel, C.4
  • 106
    • 0037667409 scopus 로고    scopus 로고
    • A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots
    • doi: 10.1042/BJ20030159
    • Santoni V, Vinh J, Pflieger D, Sommerer N, Maurel C (2003) A proteomic study reveals novel insights into the diversity of aquaporin forms expressed in the plasma membrane of plant roots. The Biochemical Journal 373, 289-296. doi: 10.1042/BJ20030159
    • (2003) The Biochemical Journal , vol.373 , pp. 289-296
    • Santoni, V.1    Vinh, J.2    Pflieger, D.3    Sommerer, N.4    Maurel, C.5
  • 108
    • 9644254148 scopus 로고    scopus 로고
    • Identification of genes regulated by dark adaptation and far-red light illumination in roots of Arabidopsis thaliana
    • doi: 10.1111/j.1365-3040.2004.01241. x
    • Sato-Nara K, Nagasaka A, Yamashita H, Ishida J, Enju A, Seki M, Shinozaki K, Suzuki H (2004) Identification of genes regulated by dark adaptation and far-red light illumination in roots of Arabidopsis thaliana. Plant, Cell & Environment 27, 1387-1394. doi: 10.1111/j.1365-3040.2004.01241. x
    • (2004) Plant, Cell & Environment , vol.27 , pp. 1387-1394
    • Sato-Nara, K.1    Nagasaka, A.2    Yamashita, H.3    Ishida, J.4    Enju, A.5    Seki, M.6    Shinozaki, K.7    Suzuki, H.8
  • 109
    • 0344316017 scopus 로고    scopus 로고
    • Aquaporin function, structure, and expression: Are there more surprise to surface in water relations?
    • doi: 10.1007/s004250050239
    • Schäffner AR (1998) Aquaporin function, structure, and expression: are there more surprise to surface in water relations? Planta 204, 131-139. doi: 10.1007/s004250050239
    • (1998) Planta , vol.204 , pp. 131-139
    • Schäffner, A.R.1
  • 110
    • 1942442451 scopus 로고    scopus 로고
    • Schuurmans JAMJ, Dongen JT, Rutjens BPW, Boonman A, Pieterse CMJ, Borstlap AC (2003) Members of the aquaporin family in the developing pea seed coat include representatives of the PIP, TIP, and NIP subfamilies. Plant Molecular Biology 53, 655-667. doi: 10.1023/B:PLAN.0000019070.60954. 77
    • Schuurmans JAMJ, Dongen JT, Rutjens BPW, Boonman A, Pieterse CMJ, Borstlap AC (2003) Members of the aquaporin family in the developing pea seed coat include representatives of the PIP, TIP, and NIP subfamilies. Plant Molecular Biology 53, 655-667. doi: 10.1023/B:PLAN.0000019070.60954. 77
  • 111
    • 33646912492 scopus 로고    scopus 로고
    • Expression analysis of genes encoding plasma membrane aquaporins during seed and fruit development in tomato
    • doi: 10.1016/j.plantsci.2006.03.021
    • Shiota H, Sudoh T, Tanaka I (2006) Expression analysis of genes encoding plasma membrane aquaporins during seed and fruit development in tomato. Plant Science 171, 277-285. doi: 10.1016/j.plantsci.2006.03.021
    • (2006) Plant Science , vol.171 , pp. 277-285
    • Shiota, H.1    Sudoh, T.2    Tanaka, I.3
  • 113
    • 0031238570 scopus 로고    scopus 로고
    • +-pumps and a tonoplast intrinsic protein of vacuolar membranes during the development of pear fruit
    • +-pumps and a tonoplast intrinsic protein of vacuolar membranes during the development of pear fruit. Plant & Cell Physiology 38, 1039-1045.
    • (1997) Plant & Cell Physiology , vol.38 , pp. 1039-1045
    • Shiratake, K.1    Kanayama, Y.2    Maeshima, M.3    Yamaki, S.4
  • 114
    • 0031876103 scopus 로고    scopus 로고
    • Changes in tonoplast protein and density with the development of pear fruit
    • doi: 10.1034/j.1399-3054.1998.1030303.x
    • Shiratake K, Kanayama Y, Maeshima M, Yamaki S (1998) Changes in tonoplast protein and density with the development of pear fruit. Physiologia Plantarum 103, 312-319. doi: 10.1034/j.1399-3054.1998.1030303.x
    • (1998) Physiologia Plantarum , vol.103 , pp. 312-319
    • Shiratake, K.1    Kanayama, Y.2    Maeshima, M.3    Yamaki, S.4
  • 117
    • 0035999374 scopus 로고    scopus 로고
    • PIP1 plasma membrane aquaporins in tobacco: From cellular effects to function in plants
    • doi: 10.1105/tpc.000901
    • Siefritz F, Tyree TM, Lovisolo C, Schubert A, Kaldenhoff R (2002) PIP1 plasma membrane aquaporins in tobacco: from cellular effects to function in plants. The Plant Cell 14, 869-876. doi: 10.1105/tpc.000901
    • (2002) The Plant Cell , vol.14 , pp. 869-876
    • Siefritz, F.1    Tyree, T.M.2    Lovisolo, C.3    Schubert, A.4    Kaldenhoff, R.5
  • 119
    • 0035130184 scopus 로고    scopus 로고
    • Specificity of the accumulation of mRNAs and proteins of the plasma membrane and tonoplast aquaporins in radish organs
    • doi: 10.1007/s004250000396
    • Suga S, Imagawa S, Maeshima M (2001) Specificity of the accumulation of mRNAs and proteins of the plasma membrane and tonoplast aquaporins in radish organs. Planta 212, 294-304. doi: 10.1007/s004250000396
    • (2001) Planta , vol.212 , pp. 294-304
    • Suga, S.1    Imagawa, S.2    Maeshima, M.3
  • 120
    • 0036808135 scopus 로고    scopus 로고
    • Aquaporin isoforms responsive to salt and water stresses and phytohormones in radish seedlings
    • doi: 10.1093/pcp/pcf148
    • Suga S, Komatsu S, Maeshima M (2002) Aquaporin isoforms responsive to salt and water stresses and phytohormones in radish seedlings. Plant & Cell Physiology 43, 1229-1237. doi: 10.1093/pcp/pcf148
    • (2002) Plant & Cell Physiology , vol.43 , pp. 1229-1237
    • Suga, S.1    Komatsu, S.2    Maeshima, M.3
  • 121
    • 0345382696 scopus 로고    scopus 로고
    • Differences in aquaporin levels among cell types of radish and measurement of osmotic water permeability of individual protoplasts
    • doi: 10.1093/pcp/pcg032
    • Suga S, Murai M, Kuwagata T, Maeshima M (2003) Differences in aquaporin levels among cell types of radish and measurement of osmotic water permeability of individual protoplasts. Plant & Cell Physiology 44, 277-286. doi: 10.1093/pcp/pcg032
    • (2003) Plant & Cell Physiology , vol.44 , pp. 277-286
    • Suga, S.1    Murai, M.2    Kuwagata, T.3    Maeshima, M.4
  • 122
    • 4344636281 scopus 로고    scopus 로고
    • Water channel activity of radish plasma membrane aquaporins heterologously expressed in yeast and their modification by site-directed mutagenesis
    • doi: 10.1093/pcp/pch120
    • Suga S, Maeshima M (2004) Water channel activity of radish plasma membrane aquaporins heterologously expressed in yeast and their modification by site-directed mutagenesis. Plant & Cell Physiology 45, 823-830. doi: 10.1093/pcp/pch120
    • (2004) Plant & Cell Physiology , vol.45 , pp. 823-830
    • Suga, S.1    Maeshima, M.2
  • 123
    • 0035652013 scopus 로고    scopus 로고
    • Isolation and expression analysis of a gene encoding a vacuolar-type water channel protein in peach fruit
    • Sugaya S, Gemma H, Iwahori S (2001) Isolation and expression analysis of a gene encoding a vacuolar-type water channel protein in peach fruit. Journal of the Japanese Society for Horticultural Science 70, 716-718.
    • (2001) Journal of the Japanese Society for Horticultural Science , vol.70 , pp. 716-718
    • Sugaya, S.1    Gemma, H.2    Iwahori, S.3
  • 124
    • 28044464281 scopus 로고    scopus 로고
    • Tonoplast vesicles of Beta vulgaris storage root show functional aquaporins regulated by protons
    • doi: 10.1042/BC20040121
    • Sutka M, Alleva K, Parisi M, Amodeo G (2005) Tonoplast vesicles of Beta vulgaris storage root show functional aquaporins regulated by protons. Biology of the Cell 97, 837-846. doi: 10.1042/BC20040121
    • (2005) Biology of the Cell , vol.97 , pp. 837-846
    • Sutka, M.1    Alleva, K.2    Parisi, M.3    Amodeo, G.4
  • 125
    • 33745442045 scopus 로고    scopus 로고
    • The Arabidopsis major intrinsic protein NIP5;1 is essential for efficient boron uptake and plant development under boron limitation
    • doi: 10.1105/tpc.106.041640
    • Takano J, Wada M, Ludewig U, Schaaf G, Wirén N, Fujiwara T (2006) The Arabidopsis major intrinsic protein NIP5;1 is essential for efficient boron uptake and plant development under boron limitation. The Plant Cell 18, 1498-1509. doi: 10.1105/tpc.106.041640
    • (2006) The Plant Cell , vol.18 , pp. 1498-1509
    • Takano, J.1    Wada, M.2    Ludewig, U.3    Schaaf, G.4    Wirén, N.5    Fujiwara, T.6
  • 126
    • 23644442412 scopus 로고    scopus 로고
    • Water channel activities of Mimosa pudica plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation
    • doi: 10.1016/j.febslet.2005.06.082
    • Temmei Y, Uchida S, Hoshino D, Kanzawa N, Kuwahara M, Sasaki S, Tsuchiya T (2005) Water channel activities of Mimosa pudica plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation. FEBS Letters 579, 4417-4422. doi: 10.1016/j.febslet.2005.06.082
    • (2005) FEBS Letters , vol.579 , pp. 4417-4422
    • Temmei, Y.1    Uchida, S.2    Hoshino, D.3    Kanzawa, N.4    Kuwahara, M.5    Sasaki, S.6    Tsuchiya, T.7
  • 127
    • 0036008346 scopus 로고    scopus 로고
    • 2 diffusion across the plasma membrane
    • doi: 10.1093/pcp/pcf001
    • 2 diffusion across the plasma membrane. Plant & Cell Physiology 43, 70-78. doi: 10.1093/pcp/pcf001
    • (2002) Plant & Cell Physiology , vol.43 , pp. 70-78
    • Terashima, I.1    Ono, K.2
  • 130
    • 0141484616 scopus 로고    scopus 로고
    • Cytosolic pH regulates root water transport during anoxic stress through gating of aquaporins
    • doi: 10.1038/nature01853
    • Tournaire-Roux C, Sutka M, Javot H, Gout E, Gerbeau P, Luu DFT, Bligny R, Maurel C (2003) Cytosolic pH regulates root water transport during anoxic stress through gating of aquaporins. Nature 425, 393-397. doi: 10.1038/nature01853
    • (2003) Nature , vol.425 , pp. 393-397
    • Tournaire-Roux, C.1    Sutka, M.2    Javot, H.3    Gout, E.4    Gerbeau, P.5    Luu, D.F.T.6    Bligny, R.7    Maurel, C.8
  • 131
    • 0032971712 scopus 로고    scopus 로고
    • Plant aquaporins: Their molecular biology, biophysics and significance for plant water relations
    • doi: 10.1093/jexbot/50.suppl 1.1055
    • Tyerman SD, Bohnert H, Maurel C, Steudle E, Smith JAC (1999) Plant aquaporins: their molecular biology, biophysics and significance for plant water relations. Journal of Experimental Botany 50, 1055-1071. doi: 10.1093/jexbot/50.suppl 1.1055
    • (1999) Journal of Experimental Botany , vol.50 , pp. 1055-1071
    • Tyerman, S.D.1    Bohnert, H.2    Maurel, C.3    Steudle, E.4    Smith, J.A.C.5
  • 132
    • 0036187202 scopus 로고    scopus 로고
    • Plant aquaporins: Multifunctional water and solute channels with expanding roles
    • doi: 10.1046/j.0016-8025.2001.00791.x
    • Tyerman SD, Niemietz CM, Bramly H (2002) Plant aquaporins: multifunctional water and solute channels with expanding roles. Plant, Cell & Environment 25, 173-194. doi: 10.1046/j.0016-8025.2001.00791.x
    • (2002) Plant, Cell & Environment , vol.25 , pp. 173-194
    • Tyerman, S.D.1    Niemietz, C.M.2    Bramly, H.3
  • 134
    • 25444457492 scopus 로고    scopus 로고
    • Roles of aquaporins in root responses to irrigation
    • doi: 10.1007/s11104-004-8070-z
    • Vandeleur R, Niemietz C, Tilbrook J, Tyerman SD (2005) Roles of aquaporins in root responses to irrigation. Plant and Soil 274, 141-161. doi: 10.1007/s11104-004-8070-z
    • (2005) Plant and Soil , vol.274 , pp. 141-161
    • Vandeleur, R.1    Niemietz, C.2    Tilbrook, J.3    Tyerman, S.D.4
  • 135
    • 4444221804 scopus 로고    scopus 로고
    • Novel regulation of aquaporins during osmotic stress
    • doi: 10.1104/pp.104.044891
    • Vera-Estrella R, Brown J, Bohnert HJ, Pantoja O (2004) Novel regulation of aquaporins during osmotic stress. Plant Physiology 135, 2318-2329. doi: 10.1104/pp.104.044891
    • (2004) Plant Physiology , vol.135 , pp. 2318-2329
    • Vera-Estrella, R.1    Brown, J.2    Bohnert, H.J.3    Pantoja, O.4
  • 136
    • 33748536401 scopus 로고    scopus 로고
    • The structure, function and regulation of the nodulin 26-like intrinsic protein family of plant aquaglyceroporins
    • doi: 10.1016/j.bbamem.2006.03.024
    • Wallace IS, Choi WG, Roberts DM (2006) The structure, function and regulation of the nodulin 26-like intrinsic protein family of plant aquaglyceroporins. Biochimica et Biophysica Acta 1758, 1165-1175. doi: 10.1016/j.bbamem.2006.03.024
    • (2006) Biochimica et Biophysica Acta , vol.1758 , pp. 1165-1175
    • Wallace, I.S.1    Choi, W.G.2    Roberts, D.M.3
  • 137
    • 33646446759 scopus 로고    scopus 로고
    • 2 movement
    • doi: 10.1071/FP05298
    • 2 movement. Functional Plant Biology 33, 431-442. doi: 10.1071/FP05298
    • (2006) Functional Plant Biology , vol.33 , pp. 431-442
    • Warren, C.1
  • 138
    • 0026646048 scopus 로고
    • Determination of the site of phosphorylation of nodulin-26 by the calcium-dependent protein-kinase from soybean nodules
    • doi: 10.1021/bi00152a035
    • Weaver CD, Roberts DM (1992) Determination of the site of phosphorylation of nodulin-26 by the calcium-dependent protein-kinase from soybean nodules. Biochemistry 31, 8954-8959. doi: 10.1021/bi00152a035
    • (1992) Biochemistry , vol.31 , pp. 8954-8959
    • Weaver, C.D.1    Roberts, D.M.2
  • 139
    • 0034703362 scopus 로고    scopus 로고
    • Functional identification of the glycerol permease activity of Arabidopsis thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces cerevisiae
    • doi: 10.1016/S0014-5793(00)02027-5
    • Weig AR, Jakob C (2000) Functional identification of the glycerol permease activity of Arabidopsis thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces cerevisiae. FEBS Letters 481, 293-298. doi: 10.1016/S0014-5793(00)02027-5
    • (2000) FEBS Letters , vol.481 , pp. 293-298
    • Weig, A.R.1    Jakob, C.2
  • 140
    • 0034850787 scopus 로고    scopus 로고
    • Characterisation of two tomato aquaporins and expression during the incompatible interaction of tomato with the plant parasite Cuscuta reflexa
    • doi: 10.1007/s004250100533
    • Werner M, Uehlein N, Proksch P, Kaldenhoff R (2001) Characterisation of two tomato aquaporins and expression during the incompatible interaction of tomato with the plant parasite Cuscuta reflexa. Planta 213, 550-555. doi: 10.1007/s004250100533
    • (2001) Planta , vol.213 , pp. 550-555
    • Werner, M.1    Uehlein, N.2    Proksch, P.3    Kaldenhoff, R.4
  • 141
    • 0037353653 scopus 로고    scopus 로고
    • Proteome analysis: Novel proteins identified at the peribacteroid membrane from Lotus japonicus root nodules
    • doi: 10.1104/pp.102.015362
    • Wienkoop S, Saalbach G (2003) Proteome analysis: novel proteins identified at the peribacteroid membrane from Lotus japonicus root nodules. Plant Physiology 131, 1080-1090. doi: 10.1104/pp.102.015362
    • (2003) Plant Physiology , vol.131 , pp. 1080-1090
    • Wienkoop, S.1    Saalbach, G.2
  • 143
    • 33749033887 scopus 로고    scopus 로고
    • Effects of internal conductance on the temperature dependence of the photosynthetic rate in spinach leaves from contrasting growth temperatures
    • doi: 10.1093/pcp/pcj077
    • Yamori W, Noguchi K, Hanba YT, Terashima I (2006) Effects of internal conductance on the temperature dependence of the photosynthetic rate in spinach
    • (2006) Plant & Cell Physiology , vol.47 , pp. 1069-1080
    • Yamori, W.1    Noguchi, K.2    Hanba, Y.T.3    Terashima, I.4
  • 144
    • 0034723202 scopus 로고    scopus 로고
    • Carbon dioxide permeability of aquaporin-1 measured in erythrocytes and lung of aquaporin-1 null mice and in reconstituted proteoliposomes
    • doi: 10.1074/jbc.275.4.2686
    • Yang X, Fukuda N, van Hoek A, Matthay MA, Ma TH, Verkman AS (2000) Carbon dioxide permeability of aquaporin-1 measured in erythrocytes and lung of aquaporin-1 null mice and in reconstituted proteoliposomes. Journal of Biological Chemistry 275, 2686-2692. doi: 10.1074/jbc.275.4.2686
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 2686-2692
    • Yang, X.1    Fukuda, N.2    van Hoek, A.3    Matthay, M.A.4    Ma, T.H.5    Verkman, A.S.6
  • 145
    • 1142306039 scopus 로고    scopus 로고
    • A cohesion/tension mechanism explains the gating of water channels (aquaporins) in Chara internodes by high concentration
    • doi: 10.1093/jxb/erh040
    • Ye Q, Wiera B, Steudle E (2004) A cohesion/tension mechanism explains the gating of water channels (aquaporins) in Chara internodes by high concentration. Journal of Experimental Botany 55, 449-461. doi: 10.1093/jxb/erh040
    • (2004) Journal of Experimental Botany , vol.55 , pp. 449-461
    • Ye, Q.1    Wiera, B.2    Steudle, E.3
  • 148
    • 27144525535 scopus 로고    scopus 로고
    • Differential responses of maize MIP genes to salt stress and ABA
    • doi: 10.1093/jxb/eri294
    • Zhu C, Schraut D, Hartung W, Schäffner AR (2005) Differential responses of maize MIP genes to salt stress and ABA. Journal of Experimental Botany 56, 2971-2981. doi: 10.1093/jxb/eri294
    • (2005) Journal of Experimental Botany , vol.56 , pp. 2971-2981
    • Zhu, C.1    Schraut, D.2    Hartung, W.3    Schäffner, A.R.4


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