메뉴 건너뛰기




Volumn 1758, Issue 8, 2006, Pages 1134-1141

Functional aquaporin diversity in plants

Author keywords

Aquaporin; Gas transport; Plant; Water channel

Indexed keywords

AQUAPORIN; ISOPROTEIN; NODULIN 26 LIKE INTRINSIC PROTEIN; PLASMA MEMBRANE INTRINSIC PROTEIN; PLASMA MEMBRANE INTRINSIC PROTEIN1; PLASMA MEMBRANE INTRINSIC PROTEIN2; PROTEIN; SMALL BASIC INTRINSIC PROTEIN; TONOPLAST INTRINSIC PROTEIN; UNCLASSIFIED DRUG; WATER;

EID: 33748625436     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.03.012     Document Type: Review
Times cited : (178)

References (82)
  • 1
    • 0034870819 scopus 로고    scopus 로고
    • The complete set of genes encoding major intrinsic proteins in Arabidopsis provides a framework for a new nomenclature for major intrinsic proteins in plants
    • Johanson U., Karlsson M., Johansson I., Gustavsson S., Sjovall S., Fraysse L., Weig A.R., and Kjellbom P. The complete set of genes encoding major intrinsic proteins in Arabidopsis provides a framework for a new nomenclature for major intrinsic proteins in plants. Plant Physiol. 126 (2001) 1358-1369
    • (2001) Plant Physiol. , vol.126 , pp. 1358-1369
    • Johanson, U.1    Karlsson, M.2    Johansson, I.3    Gustavsson, S.4    Sjovall, S.5    Fraysse, L.6    Weig, A.R.7    Kjellbom, P.8
  • 2
    • 0035106823 scopus 로고    scopus 로고
    • Aquaporins constitute a large and highly divergent protein family in maize
    • Chaumont F., Barrieu F., Wojcik E., Chrispeels M.J., and Jung R. Aquaporins constitute a large and highly divergent protein family in maize. Plant Physiol. 125 (2001) 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
  • 3
    • 21044445996 scopus 로고    scopus 로고
    • Phylogeny and evolution of the major intrinsic protein family
    • Zardoya R. Phylogeny and evolution of the major intrinsic protein family. Biol. Cell 97 (2005) 397-414
    • (2005) Biol. Cell , vol.97 , pp. 397-414
    • Zardoya, R.1
  • 4
    • 0036221680 scopus 로고    scopus 로고
    • A new subfamily of major intrinsic proteins in plants
    • Johanson U., and Gustavsson S. A new subfamily of major intrinsic proteins in plants. Mol. Biol. Evol. 19 (2002) 456-461
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 456-461
    • Johanson, U.1    Gustavsson, S.2
  • 5
    • 0027192036 scopus 로고
    • The vacuolar membrane protein gamma-TIP creates water specific channels in Xenopus oocytes
    • Maurel C., Reizer J., Schroeder J.I., and Chrispeels M.J. The vacuolar membrane protein gamma-TIP creates water specific channels in Xenopus oocytes. EMBO J. 12 (1993) 2241-2247
    • (1993) EMBO J. , vol.12 , pp. 2241-2247
    • Maurel, C.1    Reizer, J.2    Schroeder, J.I.3    Chrispeels, M.J.4
  • 6
    • 0025443895 scopus 로고
    • An intrinsic tonoplast protein of protein storage vacuoles in seeds is structurally related to a bacterial solute transporter (GIpF)
    • Johnson K.D., Hofte H., and Chrispeels M.J. An intrinsic tonoplast protein of protein storage vacuoles in seeds is structurally related to a bacterial solute transporter (GIpF). Plant Cell 2 (1990) 525-532
    • (1990) Plant Cell , vol.2 , pp. 525-532
    • Johnson, K.D.1    Hofte, H.2    Chrispeels, M.J.3
  • 7
    • 0030917014 scopus 로고    scopus 로고
    • Purified vesicles of tobacco cell vacuolar and plasma membranes exhibit dramatically different water permeability and water channel activity
    • Maurel C., Tacnet F., Guclu J., Guern J., and Ripoche P. Purified vesicles of tobacco cell vacuolar and plasma membranes exhibit dramatically different water permeability and water channel activity. Proc. Natl. Acad Sci. U. S. A. 94 (1997) 7103-7108
    • (1997) Proc. Natl. Acad Sci. U. S. A. , vol.94 , pp. 7103-7108
    • Maurel, C.1    Tacnet, F.2    Guclu, J.3    Guern, J.4    Ripoche, P.5
  • 8
    • 0033457898 scopus 로고    scopus 로고
    • Osmotic water permeability of isolated vacuoles
    • Morillon R., and Lassalles J.P. Osmotic water permeability of isolated vacuoles. Planta 210 (1999) 80-84
    • (1999) Planta , vol.210 , pp. 80-84
    • Morillon, R.1    Lassalles, J.P.2
  • 9
    • 0031403878 scopus 로고    scopus 로고
    • Characterization of water channels in wheat root membrane vesicles
    • Niemietz C.M., and Tyerman S.D. Characterization of water channels in wheat root membrane vesicles. Plant Physiol. 115 (1997) 561-567
    • (1997) Plant Physiol. , vol.115 , pp. 561-567
    • Niemietz, C.M.1    Tyerman, S.D.2
  • 10
    • 33644659755 scopus 로고    scopus 로고
    • Early effects of salinity on water transport in Arabidopsis roots, Molecular and cellular features of aquaporin expression
    • Boursiac Y., Chen S., Luu D.T., Sorieul M., van den Dries N., and Maurel C. Early effects of salinity on water transport in Arabidopsis roots, Molecular and cellular features of aquaporin expression. Plant Physiol. 139 (2005) 790-805
    • (2005) Plant Physiol. , 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
    • 0039251522 scopus 로고    scopus 로고
    • Aquaporin Nt-TIPa can account for the high permeability of tobacco cell vacuolar membrane to small neutral solutes
    • Gerbeau P., Guclu J., Ripoche P., and Maurel C. Aquaporin Nt-TIPa can account for the high permeability of tobacco cell vacuolar membrane to small neutral solutes. Plant J. 18 (1999) 577-587
    • (1999) Plant J. , vol.18 , pp. 577-587
    • Gerbeau, P.1    Guclu, J.2    Ripoche, P.3    Maurel, C.4
  • 12
    • 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 delta-TIP or gamma-TIP
    • Klebl F., Wolf M., and Sauer N. 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 delta-TIP or gamma-TIP. FEBS Lett. 547 (2003) 69-74
    • (2003) FEBS Lett. , vol.547 , pp. 69-74
    • Klebl, F.1    Wolf, M.2    Sauer, N.3
  • 13
    • 0345392686 scopus 로고    scopus 로고
    • Urea transport by nitrogen-regulated tonoplast intrinsic proteins in Arabidopsis
    • Liu L.H., Ludewig U., Gassert B., Frommer W.B., and von Wiren N. Urea transport by nitrogen-regulated tonoplast intrinsic proteins in Arabidopsis. Plant Physiol. 133 (2003) 1220-1228
    • (2003) Plant Physiol. , vol.133 , pp. 1220-1228
    • Liu, L.H.1    Ludewig, U.2    Gassert, B.3    Frommer, W.B.4    von Wiren, N.5
  • 16
    • 19044393297 scopus 로고    scopus 로고
    • Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3 transport into the vacuole
    • Loque D., Ludewig U., Yuan L., and von Wiren N. Tonoplast intrinsic proteins AtTIP2;1 and AtTIP2;3 facilitate NH3 transport into the vacuole. Plant Physiol. 137 (2005) 671-680
    • (2005) Plant Physiol. , vol.137 , pp. 671-680
    • Loque, D.1    Ludewig, U.2    Yuan, L.3    von Wiren, N.4
  • 17
    • 0036853025 scopus 로고    scopus 로고
    • Functional analysis of an Arabidopsis T-DNA "knockout" of the high-affinity NH4(+) transporter AtAMT1;1
    • Kaiser B.N., Rawat S.R., Siddiqi M.Y., Masle J., and Glass A.D. Functional analysis of an Arabidopsis T-DNA "knockout" of the high-affinity NH4(+) transporter AtAMT1;1. Plant Physiol. 130 (2002) 1263-1275
    • (2002) Plant Physiol. , vol.130 , pp. 1263-1275
    • Kaiser, B.N.1    Rawat, S.R.2    Siddiqi, M.Y.3    Masle, J.4    Glass, A.D.5
  • 18
    • 2942638465 scopus 로고    scopus 로고
    • Regulatory levels for the transport of ammonium in plant roots
    • Loque D., and von Wiren N. Regulatory levels for the transport of ammonium in plant roots. J. Exp. Bot. 55 (2004) 1293-1305
    • (2004) J. Exp. Bot. , vol.55 , pp. 1293-1305
    • Loque, D.1    von Wiren, N.2
  • 20
    • 0037272472 scopus 로고    scopus 로고
    • Molecular and cellular characterisation of LjAMT2;1, an ammonium transporter from the model legume Lotus japonicus
    • Simon-Rosin U., Wood C., and Udvardi M.K. Molecular and cellular characterisation of LjAMT2;1, an ammonium transporter from the model legume Lotus japonicus. Plant Mol. Biol. 51 (2003) 99-108
    • (2003) Plant Mol. Biol. , vol.51 , pp. 99-108
    • Simon-Rosin, U.1    Wood, C.2    Udvardi, M.K.3
  • 21
    • 3042583806 scopus 로고    scopus 로고
    • Homology modeling of representative subfamilies of Arabidopsis major intrinsic proteins, Classification based on the aromatic/arginine selectivity filter
    • Wallace I.S., and Roberts D.M. Homology modeling of representative subfamilies of Arabidopsis major intrinsic proteins, Classification based on the aromatic/arginine selectivity filter. Plant Physiol. 135 (2004) 1059-1068
    • (2004) Plant Physiol. , vol.135 , pp. 1059-1068
    • Wallace, I.S.1    Roberts, D.M.2
  • 22
    • 0033964857 scopus 로고    scopus 로고
    • Channel-mediated permeation of ammonia gas through the peribacteroid membrane of soybean nodules
    • Niemietz C.M., and Tyerman S.D. Channel-mediated permeation of ammonia gas through the peribacteroid membrane of soybean nodules. FEBS Lett. 465 (2000) 110-114
    • (2000) FEBS Lett. , vol.465 , pp. 110-114
    • Niemietz, C.M.1    Tyerman, S.D.2
  • 23
    • 0001222337 scopus 로고
    • Tonoplast-bound protein kinase phosphorylates tonoplast intrinsic protein
    • Johnson K.D.A.C., and M.J. Tonoplast-bound protein kinase phosphorylates tonoplast intrinsic protein. Plant Physiol. 100 (1992) 1787-1795
    • (1992) Plant Physiol. , vol.100 , pp. 1787-1795
    • Johnson, K.D.A.C.1    M.J2
  • 24
    • 0028997596 scopus 로고
    • Phosphorylation regulates the water channel activity of the seed-specific aquaporin alpha-TIP
    • Maurel C., Kado R.T., Guern J., and Chrispeels M.J. Phosphorylation regulates the water channel activity of the seed-specific aquaporin alpha-TIP. EMBO J. 14 (1995) 3028-3035
    • (1995) EMBO J. , vol.14 , pp. 3028-3035
    • Maurel, C.1    Kado, R.T.2    Guern, J.3    Chrispeels, M.J.4
  • 25
    • 27644442731 scopus 로고    scopus 로고
    • Phosphorylation of aquaporin PvTIP3;1 defined by mass spectrometry and molecular modeling
    • Daniels M.J., and Yeager M. Phosphorylation of aquaporin PvTIP3;1 defined by mass spectrometry and molecular modeling. Biochemistry 44 (2005) 14443-14454
    • (2005) Biochemistry , vol.44 , pp. 14443-14454
    • Daniels, M.J.1    Yeager, M.2
  • 28
    • 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 B.J., Bohnert H.J., and Pantoja O. Salt stress in Mesembryanthemum crystallinum L. cell suspensions activates adaptive mechanisms similar to those observed in the whole plant. Planta 207 (1999) 426-435
    • (1999) Planta , vol.207 , pp. 426-435
    • Vera-Estrella, R.1    Barkla, B.J.2    Bohnert, H.J.3    Pantoja, O.4
  • 29
    • 0028369219 scopus 로고
    • Cloning of two gibberellin-regulated cDNAs from Arabidopsis thaliana by subtractive hybridization: expression of the tonoplast water channel, gamma-TIP, is increased by GA3
    • Phillips A.L., and Huttly A.K. Cloning of two gibberellin-regulated cDNAs from Arabidopsis thaliana by subtractive hybridization: expression of the tonoplast water channel, gamma-TIP, is increased by GA3. Plant Mol. Biol. 24 (1994) 603-615
    • (1994) Plant Mol. Biol. , vol.24 , pp. 603-615
    • Phillips, A.L.1    Huttly, A.K.2
  • 31
    • 0030985888 scopus 로고    scopus 로고
    • Functional analysis of nodulin 26, an aquaporin in soybean root nodule symbiosomes
    • Rivers R.L., Dean R.M., Chandy G., Hall J.E., Roberts D.M., and Zeidel M.L. Functional analysis of nodulin 26, an aquaporin in soybean root nodule symbiosomes. J. Biol. Chem. 272 (1997) 16256-16261
    • (1997) J. Biol. Chem. , vol.272 , pp. 16256-16261
    • Rivers, R.L.1    Dean, R.M.2    Chandy, G.3    Hall, J.E.4    Roberts, D.M.5    Zeidel, M.L.6
  • 32
    • 0033524436 scopus 로고    scopus 로고
    • Purification and functional reconstitution of soybean nodulin 26, An aquaporin with water and glycerol transport properties
    • Dean R.M., Rivers R.L., Zeidel M.L., and Roberts D.M. Purification and functional reconstitution of soybean nodulin 26, An aquaporin with water and glycerol transport properties. Biochemistry 38 (1999) 347-353
    • (1999) Biochemistry , vol.38 , pp. 347-353
    • Dean, R.M.1    Rivers, R.L.2    Zeidel, M.L.3    Roberts, D.M.4
  • 33
    • 0037125208 scopus 로고    scopus 로고
    • Functional selectivity for glycerol of the nodulin 26 subfamily of plant membrane intrinsic proteins
    • Wallace I.S., Wills D.M., Guenther J.F., and Roberts D.M. Functional selectivity for glycerol of the nodulin 26 subfamily of plant membrane intrinsic proteins. FEBS Lett. 523 (2002) 109-112
    • (2002) FEBS Lett. , vol.523 , pp. 109-112
    • Wallace, I.S.1    Wills, D.M.2    Guenther, J.F.3    Roberts, D.M.4
  • 34
    • 0034060156 scopus 로고    scopus 로고
    • Water-selective and multifunctional aquaporins from Lotus japonicus nodules
    • Guenther J.F., and Roberts D.M. Water-selective and multifunctional aquaporins from Lotus japonicus nodules. Planta 210 (2000) 741-748
    • (2000) Planta , vol.210 , pp. 741-748
    • Guenther, J.F.1    Roberts, D.M.2
  • 35
    • 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
    • Weig A.R., and Jakob C. Functional identification of the glycerol permease activity of Arabidopsis thaliana NLM1 and NLM2 proteins by heterologous expression in Saccharomyces cerevisiae. FEBS Lett. 481 (2000) 293-298
    • (2000) FEBS Lett. , vol.481 , pp. 293-298
    • Weig, A.R.1    Jakob, C.2
  • 36
    • 26844545473 scopus 로고    scopus 로고
    • Novel type aquaporin SIPs are mainly localized to the ER membrane and show cell-specific expression in Arabidopsis thaliana
    • Ishikawa F., Suga S., Uemura T., Sato M.H., and Maeshima M. Novel type aquaporin SIPs are mainly localized to the ER membrane and show cell-specific expression in Arabidopsis thaliana. FEBS Lett. 579 (2005) 5814-5820
    • (2005) FEBS Lett. , vol.579 , pp. 5814-5820
    • Ishikawa, F.1    Suga, S.2    Uemura, T.3    Sato, M.H.4    Maeshima, M.5
  • 37
    • 0035999374 scopus 로고    scopus 로고
    • PIP1 plasma membrane aquaporins in tobacco: from cellular effects to function in plants
    • Siefritz F., Tyree M.T., Lovisolo C., Schubert A., and Kaldenhoff R. PIP1 plasma membrane aquaporins in tobacco: from cellular effects to function in plants. Plant Cell 14 (2002) 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
  • 38
    • 1642441941 scopus 로고    scopus 로고
    • The plasma membrane aquaporin NtAQP1 is a key component of the leaf unfolding mechanism in tobacco
    • Siefritz F., Otto B., Bienert G.P., van der Krol A., and Kaldenhoff R. The plasma membrane aquaporin NtAQP1 is a key component of the leaf unfolding mechanism in tobacco. Plant J. 37 (2004) 147-155
    • (2004) Plant J. , vol.37 , pp. 147-155
    • Siefritz, F.1    Otto, B.2    Bienert, G.P.3    van der Krol, A.4    Kaldenhoff, R.5
  • 39
    • 0142246438 scopus 로고    scopus 로고
    • The tobacco aquaporin NtAQP1 is a membrane CO2 pore with physiological functions
    • Uehlein N., Lovisolo C., Siefritz F., and Kaldenhoff R. The tobacco aquaporin NtAQP1 is a membrane CO2 pore with physiological functions. Nature 425 (2003) 734-737
    • (2003) Nature , vol.425 , pp. 734-737
    • Uehlein, N.1    Lovisolo, C.2    Siefritz, F.3    Kaldenhoff, R.4
  • 40
    • 1942442451 scopus 로고    scopus 로고
    • Members of the aquaporin family in the developing pea seed coat include representatives of the PIP, TIP, and NIP subfamilies
    • Schuurmans J.A., van Dongen J.T., Rutjens B.P., Boonman A., Pieterse C.M., and Borstlap A.C. Members of the aquaporin family in the developing pea seed coat include representatives of the PIP, TIP, and NIP subfamilies. Plant Mol. Biol. 53 (2003) 633-645
    • (2003) Plant Mol. Biol. , vol.53 , pp. 633-645
    • Schuurmans, J.A.1    van Dongen, J.T.2    Rutjens, B.P.3    Boonman, A.4    Pieterse, C.M.5    Borstlap, A.C.6
  • 41
    • 0028486220 scopus 로고
    • Water channels in the plant plasma membrane cloned by immunoselection from a mammalian expression system
    • Kammerloher W., Fischer U., Piechottka G.P., and Schaffner A.R. Water channels in the plant plasma membrane cloned by immunoselection from a mammalian expression system. Plant J. 6 (1994) 187-199
    • (1994) Plant J. , vol.6 , pp. 187-199
    • Kammerloher, W.1    Fischer, U.2    Piechottka, G.P.3    Schaffner, A.R.4
  • 43
    • 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., and Galili G. 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 (2003) 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
  • 44
    • 0141484616 scopus 로고    scopus 로고
    • Cytosolic pH regulates root water transport during anoxic stress through gating of aquaporins
    • Tournaire-Roux C., Sutka M., Javot H., Gout E., Gerbeau P., Luu D.T., Bligny R., and Maurel C. Cytosolic pH regulates root water transport during anoxic stress through gating of aquaporins. Nature 425 (2003) 393-397
    • (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.T.6    Bligny, R.7    Maurel, C.8
  • 45
    • 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., and Chrispeels M.J. Plasma membrane intrinsic proteins from maize cluster in two sequence subgroups with differential aquaporin activity. Plant Physiol. 122 (2000) 1025-1034
    • (2000) Plant Physiol. , vol.122 , pp. 1025-1034
    • Chaumont, F.1    Barrieu, F.2    Jung, R.3    Chrispeels, M.J.4
  • 46
    • 0742270773 scopus 로고    scopus 로고
    • Diurnal regulation of water transport and aquaporin gene expression in maize roots: contribution of PIP2 proteins
    • Lopez F., Bousser A., Sissoeff I., Gaspar M., Lachaise B., Hoarau J., and Mahe A. Diurnal regulation of water transport and aquaporin gene expression in maize roots: contribution of PIP2 proteins. Plant Cell Physiol. 44 (2003) 1384-1395
    • (2003) Plant Cell Physiol. , vol.44 , pp. 1384-1395
    • Lopez, F.1    Bousser, A.2    Sissoeff, I.3    Gaspar, M.4    Lachaise, B.5    Hoarau, J.6    Mahe, A.7
  • 47
    • 0842291747 scopus 로고    scopus 로고
    • Interactions between plasma membrane aquaporins modulate their water channel activity
    • Fetter K., Van Wilder V., Moshelion M., and Chaumont F. Interactions between plasma membrane aquaporins modulate their water channel activity. Plant Cell 16 (2004) 215-228
    • (2004) Plant Cell , vol.16 , pp. 215-228
    • Fetter, K.1    Van Wilder, V.2    Moshelion, M.3    Chaumont, F.4
  • 50
    • 2942700260 scopus 로고    scopus 로고
    • Overexpression of the barley aquaporin HvPIP2;1 increases internal CO(2) conductance and CO(2) assimilation in the leaves of transgenic rice plants
    • Hanba Y.T., Shibasaka M., Hayashi Y., Hayakawa T., Kasamo K., Terashima I., and Katsuhara M. Overexpression of the barley aquaporin HvPIP2;1 increases internal CO(2) conductance and CO(2) assimilation in the leaves of transgenic rice plants. Plant Cell Physiol. 45 (2004) 521-529
    • (2004) Plant Cell Physiol. , vol.45 , pp. 521-529
    • Hanba, Y.T.1    Shibasaka, M.2    Hayashi, Y.3    Hayakawa, T.4    Kasamo, K.5    Terashima, I.6    Katsuhara, M.7
  • 52
    • 0032029335 scopus 로고    scopus 로고
    • Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation
    • Johansson I., Karlsson M., Shukla V.K., Chrispeels M.J., Larsson C., and Kjellbom P. Water transport activity of the plasma membrane aquaporin PM28A is regulated by phosphorylation. Plant Cell 10 (1998) 451-459
    • (1998) 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
  • 53
    • 0030199138 scopus 로고    scopus 로고
    • The major integral proteins of spinach leaf plasma membranes are putative aquaporins and are phosphorylated in response to Ca2+ and apoplastic water potential
    • Johansson I., Larsson C., Ek B., and Kjellbom P. The major integral proteins of spinach leaf plasma membranes are putative aquaporins and are phosphorylated in response to Ca2+ and apoplastic water potential. Plant Cell 8 (1996) 1181-1191
    • (1996) Plant Cell , vol.8 , pp. 1181-1191
    • Johansson, I.1    Larsson, C.2    Ek, B.3    Kjellbom, P.4
  • 56
    • 0033791634 scopus 로고    scopus 로고
    • Regulators and regulation of legume root nodule development
    • Stougaard J. Regulators and regulation of legume root nodule development. Plant Physiol. 124 (2000) 531-540
    • (2000) Plant Physiol. , vol.124 , pp. 531-540
    • Stougaard, J.1
  • 57
    • 85047684128 scopus 로고    scopus 로고
    • What makes the rhizobia-legume symbiosis so special?
    • Hirsch A.M., Lum M.R., and Downie J.A. What makes the rhizobia-legume symbiosis so special?. Plant Physiol. 127 (2001) 1484-1492
    • (2001) Plant Physiol. , vol.127 , pp. 1484-1492
    • Hirsch, A.M.1    Lum, M.R.2    Downie, J.A.3
  • 58
    • 0001318886 scopus 로고
    • Specific targeting of membrane nodulins to the bacteroid-enclosing compartment in soybean nodules
    • Fortin M.G., Zelechowska M., and Verma D.P. Specific targeting of membrane nodulins to the bacteroid-enclosing compartment in soybean nodules. EMBO J. 4 (1985) 3041-3046
    • (1985) EMBO J. , vol.4 , pp. 3041-3046
    • Fortin, M.G.1    Zelechowska, M.2    Verma, D.P.3
  • 59
    • 0000308417 scopus 로고
    • Calcium-dependent phosphorylation of symbiosome membrane-proteins from nitrogen-fixing soybean nodules - evidence for phosphorylation of nodulin-26
    • Weaver C.D., Crombie B., Stacey G., and Roberts D.M. Calcium-dependent phosphorylation of symbiosome membrane-proteins from nitrogen-fixing soybean nodules - evidence for phosphorylation of nodulin-26. Plant Physiol. 95 (1991) 222-227
    • (1991) Plant Physiol. , vol.95 , pp. 222-227
    • Weaver, C.D.1    Crombie, B.2    Stacey, G.3    Roberts, D.M.4
  • 60
    • 0033524436 scopus 로고    scopus 로고
    • Purification and functional reconstitution of soybean nodulin 26, An aquaporin with water and glycerol transport properties
    • Dean R.M., Rivers R.L., Zeidel M.L., and Roberts D.M. Purification and functional reconstitution of soybean nodulin 26, An aquaporin with water and glycerol transport properties. Biochemistry 38 (1999) 347-353
    • (1999) Biochemistry , vol.38 , pp. 347-353
    • Dean, R.M.1    Rivers, R.L.2    Zeidel, M.L.3    Roberts, D.M.4
  • 61
    • 33748630579 scopus 로고
    • Structural and functional-characterization of soybean nodulin-26 phosphorylation by the calcium-dependent protein-kinase
    • Weaver C.D., Ouyang L.J., Day D.A., and Roberts D.M. Structural and functional-characterization of soybean nodulin-26 phosphorylation by the calcium-dependent protein-kinase. Mol. Biol. Cell 3 (1992) A124
    • (1992) Mol. Biol. Cell , vol.3
    • Weaver, C.D.1    Ouyang, L.J.2    Day, D.A.3    Roberts, D.M.4
  • 62
    • 0026646048 scopus 로고
    • Determination of the site of phosphorylation of nodulin-26 by the calcium-dependent protein-kinase from soybean nodules
    • Weaver C.D., and Roberts D.M. Determination of the site of phosphorylation of nodulin-26 by the calcium-dependent protein-kinase from soybean nodules. Biochemistry 31 (1992) 8954-8959
    • (1992) Biochemistry , vol.31 , pp. 8954-8959
    • Weaver, C.D.1    Roberts, D.M.2
  • 63
    • 0037394367 scopus 로고    scopus 로고
    • Phosphorylation of soybean nodulin 26 on serine 262 enhances water permeability and is regulated developmentally and by osmotic signals
    • Guenther J.F., Chanmanivone N., Galetovic M.P., Wallace I.S., Cobb J.A., and Roberts D.M. Phosphorylation of soybean nodulin 26 on serine 262 enhances water permeability and is regulated developmentally and by osmotic signals. Plant Cell 15 (2003) 981-991
    • (2003) 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
  • 64
    • 0031200862 scopus 로고    scopus 로고
    • The major intrinsic protein family of Arabidopsis has 23 members that form three distinct groups with functional aquaporins in each group
    • Weig A., Deswarte C., and Chrispeels M.J. The major intrinsic protein family of Arabidopsis has 23 members that form three distinct groups with functional aquaporins in each group. Plant Physiol. 114 (1997) 1347-1357
    • (1997) Plant Physiol. , vol.114 , pp. 1347-1357
    • Weig, A.1    Deswarte, C.2    Chrispeels, M.J.3
  • 65
    • 0031777369 scopus 로고    scopus 로고
    • Prediction of functional residues in water channels and related proteins
    • Froger A., Tallur B., Thomas D., and Delamarche C. Prediction of functional residues in water channels and related proteins. Protein Sci. 7 (1998) 1458-1468
    • (1998) Protein Sci. , vol.7 , pp. 1458-1468
    • Froger, A.1    Tallur, B.2    Thomas, D.3    Delamarche, C.4
  • 66
    • 0028675651 scopus 로고
    • Isolation and expression analysis of two rice genes encoding the major intrinsic protein
    • Liu Q., Umeda M., and Uchimiya H. Isolation and expression analysis of two rice genes encoding the major intrinsic protein. Plant Mol. Biol. 26 (1994) 2003-2007
    • (1994) Plant Mol. Biol. , vol.26 , pp. 2003-2007
    • Liu, Q.1    Umeda, M.2    Uchimiya, H.3
  • 67
    • 0344316017 scopus 로고    scopus 로고
    • Aquaporin function, structure, and expression: are there more surprises to surface in water relations?
    • Schaffner A.R. Aquaporin function, structure, and expression: are there more surprises to surface in water relations?. Planta 204 (1998) 131-139
    • (1998) Planta , vol.204 , pp. 131-139
    • Schaffner, A.R.1
  • 68
  • 69
    • 0033151856 scopus 로고    scopus 로고
    • The Nicotiana tabacum plasma membrane aquaporin NtAQP1 is mercury-insensitive and permeable for glycerol
    • Biela A., Grote K., Otto B., Hoth S., Hedrich R., and Kaldenhoff R. The Nicotiana tabacum plasma membrane aquaporin NtAQP1 is mercury-insensitive and permeable for glycerol. Plant J. 18 (1999) 565-570
    • (1999) Plant J. , vol.18 , pp. 565-570
    • Biela, A.1    Grote, K.2    Otto, B.3    Hoth, S.4    Hedrich, R.5    Kaldenhoff, R.6
  • 70
    • 23644442412 scopus 로고    scopus 로고
    • Water channel activities of Mimosa pudica plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation
    • Temmei Y., Uchida S., Hoshino D., Kanzawa N., Kuwahara M., Sasaki S., and Tsuchiya T. Water channel activities of Mimosa pudica plasma membrane intrinsic proteins are regulated by direct interaction and phosphorylation. FEBS Lett. 579 (2005) 4417-4422
    • (2005) FEBS Lett. , 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
  • 71
    • 0031888726 scopus 로고    scopus 로고
    • Effect of expressing the water channel aquaporin-1 on the CO2 permeability of Xenopus oocytes
    • Nakhoul N.L., Davis B.A., Romero M.F., and Boron W.F. Effect of expressing the water channel aquaporin-1 on the CO2 permeability of Xenopus oocytes. Am. J. Physiol. 274 (1998) C543-C548
    • (1998) Am. J. Physiol. , vol.274
    • Nakhoul, N.L.1    Davis, B.A.2    Romero, M.F.3    Boron, W.F.4
  • 73
    • 0032245776 scopus 로고    scopus 로고
    • Effect of PCMBS on CO2 permeability of Xenopus oocytes expressing aquaporin 1 or its C189S mutant
    • Cooper G.J., and Boron W.F. Effect of PCMBS on CO2 permeability of Xenopus oocytes expressing aquaporin 1 or its C189S mutant. Am. J. Physiol. 275 (1998) C1481-C1486
    • (1998) Am. J. Physiol. , vol.275
    • Cooper, G.J.1    Boron, W.F.2
  • 74
    • 0036008346 scopus 로고    scopus 로고
    • Effects of HgCl(2) on CO(2) dependence of leaf photosynthesis: evidence indicating involvement of aquaporins in CO(2) diffusion across the plasma membrane
    • Terashima I., and Ono K. Effects of HgCl(2) on CO(2) dependence of leaf photosynthesis: evidence indicating involvement of aquaporins in CO(2) diffusion across the plasma membrane. Plant Cell Physiol. 43 (2002) 70-78
    • (2002) Plant Cell Physiol. , vol.43 , pp. 70-78
    • Terashima, I.1    Ono, K.2
  • 75
    • 0028675704 scopus 로고
    • The plasma membrane of Arabidopsis thaliana contains a mercury-insensitive aquaporin that is a homolog of the tonoplast water channel protein TIP
    • Daniels M.J., Mirkov T.E., and Chrispeels M.J. The plasma membrane of Arabidopsis thaliana contains a mercury-insensitive aquaporin that is a homolog of the tonoplast water channel protein TIP. Plant Physiol. 106 (1994) 1325-1333
    • (1994) Plant Physiol. , vol.106 , pp. 1325-1333
    • Daniels, M.J.1    Mirkov, T.E.2    Chrispeels, M.J.3
  • 76
    • 11444260781 scopus 로고    scopus 로고
    • PIP1 and PIP2 aquaporins are differentially expressed during tobacco anther and stigma development
    • Bots M., Feron R., Uehlein N., Weterings K., Kaldenhoff R., and Mariani T. PIP1 and PIP2 aquaporins are differentially expressed during tobacco anther and stigma development. J. Exp. Bot. 56 (2005) 113-121
    • (2005) J. Exp. Bot. , vol.56 , pp. 113-121
    • Bots, M.1    Feron, R.2    Uehlein, N.3    Weterings, K.4    Kaldenhoff, R.5    Mariani, T.6
  • 77
    • 20444445196 scopus 로고    scopus 로고
    • Aquaporins of the PIP2 class are required for efficient anther dehiscence in tobacco
    • Bots M., Vergeldt F., Wolters-Arts M., Weterings K., van As H., and Mariani C. Aquaporins of the PIP2 class are required for efficient anther dehiscence in tobacco. Plant Physiol. 137 (2005) 1049-1056
    • (2005) Plant Physiol. , vol.137 , pp. 1049-1056
    • Bots, M.1    Vergeldt, F.2    Wolters-Arts, M.3    Weterings, K.4    van As, H.5    Mariani, C.6
  • 78
    • 0033737020 scopus 로고    scopus 로고
    • Permeability and channel-mediated transport of boric acid across membrane vesicles isolated from squash roots
    • Dordas C., Chrispeels M.J., and Brown P.H. Permeability and channel-mediated transport of boric acid across membrane vesicles isolated from squash roots. Plant Physiol. 124 (2000) 1349-1362
    • (2000) Plant Physiol. , vol.124 , pp. 1349-1362
    • Dordas, C.1    Chrispeels, M.J.2    Brown, P.H.3
  • 80
    • 0036011030 scopus 로고    scopus 로고
    • The water permeability of Arabidopsis plasma membrane is regulated by divalent cations and pH
    • Gerbeau P., Amodeo G., Henzler T., Santoni V., Ripoche P., and Maurel C. The water permeability of Arabidopsis plasma membrane is regulated by divalent cations and pH. Plant J. 30 (2002) 71-81
    • (2002) Plant J. , vol.30 , pp. 71-81
    • Gerbeau, P.1    Amodeo, G.2    Henzler, T.3    Santoni, V.4    Ripoche, P.5    Maurel, C.6
  • 81
    • 26944462019 scopus 로고    scopus 로고
    • Regulation of plant aquaporin activity
    • Chaumont F., Moshelion M., and Daniels M.J. Regulation of plant aquaporin activity. Biol. Cell 97 (2005) 749-764
    • (2005) Biol. Cell , vol.97 , pp. 749-764
    • Chaumont, F.1    Moshelion, M.2    Daniels, M.J.3
  • 82


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.