메뉴 건너뛰기




Volumn 63, Issue , 2013, Pages 151-158

Aquaporin OsPIP1;1 promotes rice salt resistance and seed germination

Author keywords

Aquaporin; Cellular localization; Salt resistance; Seed germination; Seed yield; Water permeability

Indexed keywords

AQUAPORIN; SODIUM CHLORIDE; VEGETABLE PROTEIN; WATER;

EID: 84871461981     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2012.11.018     Document Type: Article
Times cited : (141)

References (44)
  • 1
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • Preston G.M., Carroll T.P., Guggino W.B., Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 1992, 256:385-387.
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carroll, T.P.2    Guggino, W.B.3    Agre, P.4
  • 2
    • 33644536712 scopus 로고    scopus 로고
    • The aquaporin water channels
    • Agre P. The aquaporin water channels. Proc. Am. Thor. Soc. 2006, 3:5-13.
    • (2006) Proc. Am. Thor. Soc. , vol.3 , pp. 5-13
    • Agre, P.1
  • 3
    • 0033913601 scopus 로고    scopus 로고
    • The Escherichia coli aquaporin-Z water channel
    • Calamita G. The Escherichia coli aquaporin-Z water channel. Mol. Microbiol. 2000, 37:254-262.
    • (2000) Mol. Microbiol. , vol.37 , pp. 254-262
    • Calamita, G.1
  • 4
    • 0036713490 scopus 로고    scopus 로고
    • The role of aquaporins in root water uptake
    • Javot H., Maurel C. The role of aquaporins in root water uptake. Ann. Bot. 2002, 90:301-313.
    • (2002) Ann. Bot. , vol.90 , pp. 301-313
    • Javot, H.1    Maurel, C.2
  • 5
    • 26444617525 scopus 로고    scopus 로고
    • Identification of 33 rice aquaporin genes and analysis of their expression and function
    • Sakurai J., Ishikawa F., Yamaguchi T., Uemura M., Maeshima M. Identification of 33 rice aquaporin genes and analysis of their expression and function. Plant Cell. Physiol. 2005, 46:1568-1577.
    • (2005) Plant Cell. Physiol. , vol.46 , pp. 1568-1577
    • Sakurai, J.1    Ishikawa, F.2    Yamaguchi, T.3    Uemura, M.4    Maeshima, M.5
  • 6
    • 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., Jung R. Aquaporins constitute a large and highly divergent protein family in maize. Plant Physiol. 2001, 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
  • 8
    • 0028426887 scopus 로고
    • Aquaporins: the molecular basis of facilitated water movement through living plant cells?
    • Chrispeels M.J., Maurel C. Aquaporins: the molecular basis of facilitated water movement through living plant cells?. Plant Physiol. 1994, 105:9-13.
    • (1994) Plant Physiol. , vol.105 , pp. 9-13
    • Chrispeels, M.J.1    Maurel, C.2
  • 10
    • 33748625436 scopus 로고    scopus 로고
    • Functional aquaporin diversity in plants
    • Kaldenhoff R., Fischer M. Functional aquaporin diversity in plants. Biochim. Biophys. Acta 2006, 1758:1134-1141.
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1134-1141
    • Kaldenhoff, R.1    Fischer, M.2
  • 12
    • 0842291747 scopus 로고    scopus 로고
    • Interactions between plasma membrane aquaporins modulate their water channel activity
    • Fetter K., Van Wilder V., Moshelion M., Chaumont F. Interactions between plasma membrane aquaporins modulate their water channel activity. Plant Cell 2004, 16:215-228.
    • (2004) Plant Cell , vol.16 , pp. 215-228
    • Fetter, K.1    Van Wilder, V.2    Moshelion, M.3    Chaumont, F.4
  • 13
    • 70349488887 scopus 로고    scopus 로고
    • A look inside: localization patterns and functions of intracellular plant aquaporins
    • Wudick M.M., Luu D.T., Maurel C. A look inside: localization patterns and functions of intracellular plant aquaporins. New Phytol. 2009, 184:289-302.
    • (2009) New Phytol. , vol.184 , pp. 289-302
    • Wudick, M.M.1    Luu, D.T.2    Maurel, C.3
  • 16
    • 0000179989 scopus 로고    scopus 로고
    • PIP1 aquaporins are concentrated in plasmalemmasomes of Arabidopsis thaliana mesophyll
    • Robinson D.R., Sieber H., Kammerloher W., Schaffner A.R. PIP1 aquaporins are concentrated in plasmalemmasomes of Arabidopsis thaliana mesophyll. Plant Physiol. 1996, 111:645-649.
    • (1996) Plant Physiol. , vol.111 , pp. 645-649
    • Robinson, D.R.1    Sieber, H.2    Kammerloher, W.3    Schaffner, A.R.4
  • 17
    • 34547625251 scopus 로고    scopus 로고
    • FRET imaging in living maize cells reveals that plasma membrane aquaporins interact to regulate their subcellular localization
    • Zelazny E., Borst J.W., Muylaert M., Batoko H., Hemminga M.A., Chaumont F. FRET imaging in living maize cells reveals that plasma membrane aquaporins interact to regulate their subcellular localization. Proc. Natl. Acad. Sci. 2007, 104:12359-12364.
    • (2007) Proc. Natl. Acad. Sci. , vol.104 , pp. 12359-12364
    • Zelazny, E.1    Borst, J.W.2    Muylaert, M.3    Batoko, H.4    Hemminga, M.A.5    Chaumont, F.6
  • 20
    • 33645055384 scopus 로고    scopus 로고
    • Expression and functional analysis of the rice plasma-membrane intrinsic protein gene family
    • Guo L., Wang Z.Y., Lin H., Cui W.E., Chen J., Liu M., Chen Z.L., Qu L.J., Gu H. Expression and functional analysis of the rice plasma-membrane intrinsic protein gene family. Cell. Res. 2006, 16:277-286.
    • (2006) Cell. Res. , vol.16 , pp. 277-286
    • Guo, L.1    Wang, Z.Y.2    Lin, H.3    Cui, W.E.4    Chen, J.5    Liu, M.6    Chen, Z.L.7    Qu, L.J.8    Gu, H.9
  • 21
    • 0034657264 scopus 로고    scopus 로고
    • Molecular cloning of a novel water channel from rice: its products expression in Xenopus oocytes and involvement in chilling tolerance
    • Li L., Li S., Tao Y., Kitagawa Y. Molecular cloning of a novel water channel from rice: its products expression in Xenopus oocytes and involvement in chilling tolerance. Plant Sci. 2000, 154:43-51.
    • (2000) Plant Sci. , vol.154 , pp. 43-51
    • Li, L.1    Li, S.2    Tao, Y.3    Kitagawa, Y.4
  • 22
    • 34547146467 scopus 로고    scopus 로고
    • The role of water channel proteins and nitric oxide signaling in rice seed germination
    • Liu H.Y., Yu X., Cui D.Y., Sun M.H., Sun W.N., Tang Z.C., Kwak S.S., Su W.A. The role of water channel proteins and nitric oxide signaling in rice seed germination. Cell. Res. 2007, 17:638-649.
    • (2007) Cell. Res. , vol.17 , pp. 638-649
    • Liu, H.Y.1    Yu, X.2    Cui, D.Y.3    Sun, M.H.4    Sun, W.N.5    Tang, Z.C.6    Kwak, S.S.7    Su, W.A.8
  • 23
    • 40549101581 scopus 로고    scopus 로고
    • A fruit-specific plasma membrane aquaporin subtype PIP1;1 is regulated during strawberry (Fragaria x ananassa) fruit ripening
    • Mut P., Bustamante C., Martínez G., Alleva K., Sutka M., Civello M., Amodeo G. A fruit-specific plasma membrane aquaporin subtype PIP1;1 is regulated during strawberry (Fragaria x ananassa) fruit ripening. Physiol. Plant 2008, 132:538-551.
    • (2008) Physiol. Plant , vol.132 , pp. 538-551
    • Mut, P.1    Bustamante, C.2    Martínez, G.3    Alleva, K.4    Sutka, M.5    Civello, M.6    Amodeo, G.7
  • 24
    • 33745241356 scopus 로고    scopus 로고
    • Water relations and an expression analysis of plasma membrane intrinsic proteins in sensitive and tolerant rice during chilling and recovery
    • Yu X., Peng Y.H., Zhang M.H., Shao Y.J., Su W.A., Tang Z.C. Water relations and an expression analysis of plasma membrane intrinsic proteins in sensitive and tolerant rice during chilling and recovery. Cell. Res. 2006, 16:599-608.
    • (2006) Cell. Res. , vol.16 , pp. 599-608
    • Yu, X.1    Peng, Y.H.2    Zhang, M.H.3    Shao, Y.J.4    Su, W.A.5    Tang, Z.C.6
  • 26
    • 0033520342 scopus 로고    scopus 로고
    • Functional reconstitution and characterization of AqpZ, the E. coli water channel protein
    • Borgnia M.J., Kozono D., Calamita G., Maloney P.C., Agre P. Functional reconstitution and characterization of AqpZ, the E. coli water channel protein. J. Mol. Biol. 1999, 291:1169-1179.
    • (1999) J. Mol. Biol. , vol.291 , pp. 1169-1179
    • Borgnia, M.J.1    Kozono, D.2    Calamita, G.3    Maloney, P.C.4    Agre, P.5
  • 27
    • 0037855844 scopus 로고    scopus 로고
    • Functional expression and characterization of an archaeal aquaporin. AqpM from methanothermobacter marburgensis
    • Kozono D., Ding X., Iwasaki I., Meng X., Kamagata Y., Agre P., Kitagawa Y. Functional expression and characterization of an archaeal aquaporin. AqpM from methanothermobacter marburgensis. J. Biol. Chem. 2003, 278:10649-10656.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10649-10656
    • Kozono, D.1    Ding, X.2    Iwasaki, I.3    Meng, X.4    Kamagata, Y.5    Agre, P.6    Kitagawa, Y.7
  • 28
    • 70349488887 scopus 로고    scopus 로고
    • A look inside: localization patterns and functions of intracellular plant aquaporins
    • Michael M.W., Doan-Trung L., Maurel C. A look inside: localization patterns and functions of intracellular plant aquaporins. New Phytol. 2009, 184:289-302.
    • (2009) New Phytol. , vol.184 , pp. 289-302
    • Michael, M.W.1    Doan-Trung, L.2    Maurel, C.3
  • 29
    • 84857657357 scopus 로고    scopus 로고
    • Fluorescence recovery after photobleaching reveals high cycling dynamics of plasma membrane aquaporins in Arabidopsis roots under salt stress
    • Luu D.T., Martinière A., Sorieul M., Runions J., Maurel C. Fluorescence recovery after photobleaching reveals high cycling dynamics of plasma membrane aquaporins in Arabidopsis roots under salt stress. Plant J. 2012, 69:894-905.
    • (2012) Plant J. , vol.69 , pp. 894-905
    • Luu, D.T.1    Martinière, A.2    Sorieul, M.3    Runions, J.4    Maurel, C.5
  • 30
    • 34548754063 scopus 로고    scopus 로고
    • Ectopic expression of a foreign aquaporin disrupts the natural expression patterns of endogenous aquaporin genes and alters plant responses to different stress conditions
    • Jang J.Y., Rhee J.Y., Kim D.G., Chung G.C., Lee J.H., Kang H. Ectopic expression of a foreign aquaporin disrupts the natural expression patterns of endogenous aquaporin genes and alters plant responses to different stress conditions. Plant Cell. Physiol. 2007, 48:1331-1339.
    • (2007) Plant Cell. Physiol. , vol.48 , pp. 1331-1339
    • Jang, J.Y.1    Rhee, J.Y.2    Kim, D.G.3    Chung, G.C.4    Lee, J.H.5    Kang, H.6
  • 31
    • 60549098614 scopus 로고    scopus 로고
    • Improving aquaporin Z expression in Escherichia coli by fusion partners and subsequent condition optimization
    • Lian J., Ding S., Cai J., Zhang D., Xu Z., Wang X. Improving aquaporin Z expression in Escherichia coli by fusion partners and subsequent condition optimization. Appl. Microbiol. Biotechnol. 2009, 82:463-470.
    • (2009) Appl. Microbiol. Biotechnol. , vol.82 , pp. 463-470
    • Lian, J.1    Ding, S.2    Cai, J.3    Zhang, D.4    Xu, Z.5    Wang, X.6
  • 32
    • 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., Mariani T. PIP1 and PIP2 aquaporins are differentially expressed during tobacco anther and stigma development. J. Exp. Bot. 2005, 56:113-121.
    • (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
  • 34
    • 73249141415 scopus 로고    scopus 로고
    • The role of tobacco Aquaporin1 in improving water use efficiency, hydraulic conductivity, and yield production under salt stress
    • Sade N., Gebretsadik M., Seligmann R., Schwartz A., Wallach R., Moshelion M. The role of tobacco Aquaporin1 in improving water use efficiency, hydraulic conductivity, and yield production under salt stress. Plant Physiol. 2010, 152:2452-2454.
    • (2010) Plant Physiol. , vol.152 , pp. 2452-2454
    • Sade, N.1    Gebretsadik, M.2    Seligmann, R.3    Schwartz, A.4    Wallach, R.5    Moshelion, M.6
  • 35
    • 84555186746 scopus 로고    scopus 로고
    • Regulation of root water uptake under abiotic stress conditions
    • Aroca R., Porcel R., Ruiz-Lozano J.M. Regulation of root water uptake under abiotic stress conditions. J. Exp. Bot. 2012, 63:43-57.
    • (2012) J. Exp. Bot. , vol.63 , pp. 43-57
    • Aroca, R.1    Porcel, R.2    Ruiz-Lozano, J.M.3
  • 36
    • 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. 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 2003, 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
  • 37
    • 79956196495 scopus 로고    scopus 로고
    • The influence of natural mineral water on aquaporin water permeability and human natural killer cell activity
    • Kitagawa Y., Liu C., Ding X. The influence of natural mineral water on aquaporin water permeability and human natural killer cell activity. Biochem. Biophys. Res. Commun. 2011, 409:40-45.
    • (2011) Biochem. Biophys. Res. Commun. , vol.409 , pp. 40-45
    • Kitagawa, Y.1    Liu, C.2    Ding, X.3
  • 38
    • 0028787084 scopus 로고
    • Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli
    • Calamita G., Bishai W.R., Preston G.M., Guggino W.B., Agre P. Molecular cloning and characterization of AqpZ, a water channel from Escherichia coli. J. Biol. Chem. 1995, 270:29063-29066.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29063-29066
    • Calamita, G.1    Bishai, W.R.2    Preston, G.M.3    Guggino, W.B.4    Agre, P.5
  • 40
    • 0022461542 scopus 로고
    • Osmotic water permeabilities of brush border and basolateral membrane vesicles from rat renal cortex and small intestine
    • van Heeswijk M.P.E., van Os C.H. Osmotic water permeabilities of brush border and basolateral membrane vesicles from rat renal cortex and small intestine. J. Membr. Biol. 1986, 92:183-193.
    • (1986) J. Membr. Biol. , vol.92 , pp. 183-193
    • van Heeswijk, M.P.E.1    van Os, C.H.2
  • 42
    • 16444371574 scopus 로고    scopus 로고
    • A synthetic green fluorescent protein gene for plant biotechnology
    • Niwa Y. A synthetic green fluorescent protein gene for plant biotechnology. Plant Biotechnol. 2003, 20:1-11.
    • (2003) Plant Biotechnol. , vol.20 , pp. 1-11
    • Niwa, Y.1
  • 43
    • 33748347060 scopus 로고    scopus 로고
    • A highly efficient transient protoplast system for analyzing defence gene expression and protein-protein interactions in rice
    • Chen S., Tao L., Zeng L., Vega-Sanchez M.E., Umemura K., Wang G.L. A highly efficient transient protoplast system for analyzing defence gene expression and protein-protein interactions in rice. Mol. Plant Pathol. 2006, 7:417-427.
    • (2006) Mol. Plant Pathol. , vol.7 , pp. 417-427
    • Chen, S.1    Tao, L.2    Zeng, L.3    Vega-Sanchez, M.E.4    Umemura, K.5    Wang, G.L.6
  • 44
    • 53549121971 scopus 로고    scopus 로고
    • Cysteine proteases XCP1 and XCP2 aid micro-autolysis within the intact central vacuole during xylogenesis in Arabidopsis root
    • Avci U., Petzold H.E., Ismail I.O., Beers E.P., Haigler C.H. Cysteine proteases XCP1 and XCP2 aid micro-autolysis within the intact central vacuole during xylogenesis in Arabidopsis root. Plant J. 2008, 56:303-315.
    • (2008) Plant J. , vol.56 , pp. 303-315
    • Avci, U.1    Petzold, H.E.2    Ismail, I.O.3    Beers, E.P.4    Haigler, C.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.