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Volumn 45, Issue 5, 2004, Pages 608-617

Phosphorylation of plasma membrane aquaporin regulates temperature- dependent opening of tulip petals

Author keywords

Ca2+; CDPK; Dephosphorylation; Petal oscillation; Phosphorylation; Water transport

Indexed keywords

AQUAPORIN; CALCIUM; CALCIUM CHANNEL BLOCKING AGENT; CHELATING AGENT; WATER;

EID: 2942711718     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/pcp/pch069     Document Type: Article
Times cited : (119)

References (50)
  • 2
    • 0028989065 scopus 로고
    • 2+ from individual plant vacuoles by both InsP3 and cyclic ADP-ribose
    • 2+ from individual plant vacuoles by both InsP3 and cyclic ADP-ribose. Science 268: 735-737.
    • (1995) Science , vol.268 , pp. 735-737
    • Allen, G.J.1    Muir, S.R.2    Sanders, D.3
  • 3
    • 0030029529 scopus 로고    scopus 로고
    • 2+ transport in membrane vesicles)
    • 2+ transport in membrane vesicles). Plant Physiol. 110: 913-922.
    • (1996) Plant Physiol. , vol.110 , pp. 913-922
    • Askerlund, P.1
  • 4
    • 0033198468 scopus 로고    scopus 로고
    • Rapid stalk elongation in tulip (Tulipa gesneriana L. cv. Apeldoorn) and the combined action of cold-induced invertase and the water-channel protein γTIP
    • Balk, P.A. and Boer, A.D. de (1999) Rapid stalk elongation in tulip (Tulipa gesneriana L. cv. Apeldoorn) and the combined action of cold-induced invertase and the water-channel protein γTIP. Planta 209: 346-354.
    • (1999) Planta , vol.209 , pp. 346-354
    • Balk, P.A.1    De Boer, A.D.2
  • 7
    • 0033980876 scopus 로고    scopus 로고
    • Nitric oxide donors, nitrosothiols and mitochondrial respiration inhibitors induce caspase activation by different mechanisms
    • Borutaite, V., Morkuniene, R. and Brown, G.C. (2000) Nitric oxide donors, nitrosothiols and mitochondrial respiration inhibitors induce caspase activation by different mechanisms. FEBS Lett. 467: 155-159.
    • (2000) FEBS Lett. , vol.467 , pp. 155-159
    • Borutaite, V.1    Morkuniene, R.2    Brown, G.C.3
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein using the principle for protein-dye binding
    • Bradford, M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein using the principle for protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 9
    • 77957077486 scopus 로고
    • Isolation of plasma membrane: Membrane markers and general principles
    • Briskin, D.P., Leonard, R.T. and Hodges, T.K. (1987) Isolation of plasma membrane: Membrane markers and general principles. Methods Enzymol. 148: 542-559.
    • (1987) Methods Enzymol. , vol.148 , pp. 542-559
    • Briskin, D.P.1    Leonard, R.T.2    Hodges, T.K.3
  • 10
    • 0032867192 scopus 로고    scopus 로고
    • Autophosphorylation-dependent activation of a calcium-dependent protein kinase from groundnut
    • Chaudhury, S., Seal, A. and DasGupta, M. (1999) Autophosphorylation- dependent activation of a calcium-dependent protein kinase from groundnut. Plant Physiol. 120: 859-866.
    • (1999) Plant Physiol. , vol.120 , pp. 859-866
    • Chaudhury, S.1    Seal, A.2    DasGupta, M.3
  • 12
    • 0037164119 scopus 로고    scopus 로고
    • Ultralow calcium requirements of fungi facilitate use of calcium regulation agents to suppress host calcium dependent defenses, synergizing infection by a mycoherbicide
    • Gressel, J., Michaeli, D., Kampel, V., Amsellem, Z. and Warshawsky, A. (2002) Ultralow calcium requirements of fungi facilitate use of calcium regulation agents to suppress host calcium dependent defenses, synergizing infection by a mycoherbicide. J. Agric. Food Chem. 50: 6353-6360.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 6353-6360
    • Gressel, J.1    Michaeli, D.2    Kampel, V.3    Amsellem, Z.4    Warshawsky, A.5
  • 15
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signaling
    • Janssens, V. and Goris, J. (2001) Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signaling. Biochem. J. 353: 417-439.
    • (2001) Biochem. J. , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 17
    • 0031953311 scopus 로고    scopus 로고
    • Stomatal control of photosynthesis and transpiration
    • Jones, H.G. (1998) Stomatal control of photosynthesis and transpiration. J. Exp. Bot. 49: 387-398.
    • (1998) J. Exp. Bot. , vol.49 , pp. 387-398
    • Jones, H.G.1
  • 18
    • 0037468462 scopus 로고    scopus 로고
    • Reconstitution of water channel function of an aquaporin over expressed and purified from Pichia pastoris
    • Karlsson, M., Fotiadis, D., Sjovall, S., Johansson, I., Hedfalk, K., Engel, A. and Kjellbom, P. (2003) Reconstitution of water channel function of an aquaporin over expressed and purified from Pichia pastoris. FEBS Lett. 537: 68-72.
    • (2003) FEBS Lett. , vol.537 , pp. 68-72
    • Karlsson, M.1    Fotiadis, D.2    Sjovall, S.3    Johansson, I.4    Hedfalk, K.5    Engel, A.6    Kjellbom, P.7
  • 19
    • 0035983678 scopus 로고    scopus 로고
    • The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis
    • Kerk, D., Bulgrien, J., Smith, D.W., Barsam, B., Veretnik, S. and Gribskov, M. (2002) The complement of protein phosphatase catalytic subunits encoded in the genome of Arabidopsis. Plant Physiol. 129: 908-925.
    • (2002) Plant Physiol. , vol.129 , pp. 908-925
    • Kerk, D.1    Bulgrien, J.2    Smith, D.W.3    Barsam, B.4    Veretnik, S.5    Gribskov, M.6
  • 20
    • 84989711475 scopus 로고
    • Preparation and polypeptide composition of chlorophyll-free plasma membranes from leaves of light-grown spinach and barley
    • Kjellbom, P. and Larsson, C. (1984) Preparation and polypeptide composition of chlorophyll-free plasma membranes from leaves of light-grown spinach and barley. Physiol. Plant. 62: 501-509.
    • (1984) Physiol. Plant. , vol.62 , pp. 501-509
    • Kjellbom, P.1    Larsson, C.2
  • 22
    • 0037008196 scopus 로고    scopus 로고
    • In vivo and vitro phosphorylation of membrane and soluble forms of soybean nodule sucrose synthase
    • Komina, O., Zhou, Y., Sarath, G. and Chollet, R. (2002) In vivo and vitro phosphorylation of membrane and soluble forms of soybean nodule sucrose synthase. Plant Physiol. 129: 1664-1673.
    • (2002) Plant Physiol. , vol.129 , pp. 1664-1673
    • Komina, O.1    Zhou, Y.2    Sarath, G.3    Chollet, R.4
  • 24
    • 0028903887 scopus 로고
    • AMP-dependent phosphorylation stimulates water permeability of aquaporin collecting duct water channel protein expressed in Xenopus oocytes
    • Kuwahara, M., Fushimi, K., Terada, Y., Bai, L., Marumo, F. and Sasaki, S. (1995) cAMP-dependent phosphorylation stimulates water permeability of aquaporin collecting duct water channel protein expressed in Xenopus oocytes. J. Biol. Chem. 270: 10384-10387.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10384-10387
    • Kuwahara, M.1    Fushimi, K.2    Terada, Y.3    Bai, L.4    Marumo, F.5    Sasaki, S.6
  • 25
    • 0032297190 scopus 로고    scopus 로고
    • Involvement of plasma membrane redox activity and calcium homeostasis in the UV-B and UV-A/blue light induction of gene expression in Arabidopsis
    • Long, J.C. and Jenkins, G.I. (1998) Involvement of plasma membrane redox activity and calcium homeostasis in the UV-B and UV-A/blue light induction of gene expression in Arabidopsis. Plant Cell 10: 2077-2086.
    • (1998) Plant Cell , vol.10 , pp. 2077-2086
    • Long, J.C.1    Jenkins, G.I.2
  • 26
  • 27
    • 0348199154 scopus 로고    scopus 로고
    • Aquaporins and water permeability of plant membranes
    • Maurel, C. (1997) Aquaporins and water permeability of plant membranes. Annu. Rev. Plant Physiol. Plant Mol. Biol. 48: 399-429.
    • (1997) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.48 , pp. 399-429
    • Maurel, C.1
  • 28
    • 0028997596 scopus 로고
    • Phophorylation regulates the water channel activity of the seed-specific aquaporin α-TIP
    • Maurel, C., Kado, R.T., Guern, J. and Chrispeels, M.J. (1995) Phophorylation regulates the water channel activity of the seed-specific aquaporin α-TIP. EMBO J. 14: 3028-3035.
    • (1995) EMBO J. , vol.14 , pp. 3028-3035
    • Maurel, C.1    Kado, R.T.2    Guern, J.3    Chrispeels, M.J.4
  • 30
    • 0035193614 scopus 로고    scopus 로고
    • Rapid movements of plant organs require solute-water co-transporters or contractile proteins
    • Morillon, R., David, L., Crispeels, M.J. and Lassalles, J.P. (2001) Rapid movements of plant organs require solute-water co-transporters or contractile proteins. Plant Physiol. 127: 720-723.
    • (2001) Plant Physiol. , vol.127 , pp. 720-723
    • Morillon, R.1    David, L.2    Crispeels, M.J.3    Lassalles, J.P.4
  • 33
    • 0034754544 scopus 로고    scopus 로고
    • Low aquaporin content and low osmotic water permeability of the plasma and vacuolar membranes of a CAM plant Graptopetallum paraguayense: Comparison with radish
    • Ohshima, Y., Iwasaki, I., Suga, S., Murakami, M., Inoue, K. and Maeshima, M. (2001) Low aquaporin content and low osmotic water permeability of the plasma and vacuolar membranes of a CAM plant Graptopetallum paraguayense: Comparison with radish. Plant Cell Physiol. 42: 1119-1129.
    • (2001) Plant Cell Physiol. , vol.42 , pp. 1119-1129
    • Ohshima, Y.1    Iwasaki, I.2    Suga, S.3    Murakami, M.4    Inoue, K.5    Maeshima, M.6
  • 34
    • 0034978310 scopus 로고    scopus 로고
    • Possible involvement of protein phosphorylation in aluminium-responsive malate influx from wheat root apex
    • Osawa, H. and Matsumoto, H. (2001) Possible involvement of protein phosphorylation in aluminium-responsive malate influx from wheat root apex. Plant Physiol. 126: 411-420.
    • (2001) Plant Physiol. , vol.126 , pp. 411-420
    • Osawa, H.1    Matsumoto, H.2
  • 35
    • 0026503030 scopus 로고
    • Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein
    • Preston, G.M., Carrol, T.P., Guggino, W.B. and Arge, P. (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256: 385-387.
    • (1992) Science , vol.256 , pp. 385-387
    • Preston, G.M.1    Carrol, T.P.2    Guggino, W.B.3    Arge, P.4
  • 36
    • 0023641558 scopus 로고
    • Calcium- regulated in vivo protein phosphorylation in Zea mays L. root lips
    • Raghothama, K.G., Reddy, A.S.N., Friedmann, M. and Poovaiah, B.W. (1987) Calcium- regulated in vivo protein phosphorylation in Zea mays L. root lips. Plant Physiol. 83: 1008-1013.
    • (1987) Plant Physiol. , vol.83 , pp. 1008-1013
    • Raghothama, K.G.1    Reddy, A.S.N.2    Friedmann, M.3    Poovaiah, B.W.4
  • 37
    • 0001176645 scopus 로고    scopus 로고
    • Calcium-dependent protein phosphorylation may mediate the gibberellic acid response in barley aleurone
    • Ritchie, S. and Gilroy, S. (1998) Calcium-dependent protein phosphorylation may mediate the gibberellic acid response in barley aleurone. Plant Physiol. 116: 765-776.
    • (1998) Plant Physiol. , vol.116 , pp. 765-776
    • Ritchie, S.1    Gilroy, S.2
  • 40
    • 85024564919 scopus 로고
    • Light and clock-controlled leaflet movements in Samanea saman: A physiological, biophysical and biochemical analysis
    • Satter, R.L., Morse, M.J., Lee, Y., Crain, R.C., Cote, G. and Moran, N. (1988) Light and clock-controlled leaflet movements in Samanea saman: a physiological, biophysical and biochemical analysis. Bot. Acta 101: 205-213.
    • (1988) Bot. Acta , vol.101 , pp. 205-213
    • Satter, R.L.1    Morse, M.J.2    Lee, Y.3    Crain, R.C.4    Cote, G.5    Moran, N.6
  • 41
    • 0344316017 scopus 로고    scopus 로고
    • Aquaporin function, structure and expression: Are there more surprises to surface in water relations?
    • Schaffner, A.R. (1998) Aquaporin function, structure and expression: are there more surprises to surface in water relations? Planta 204: 131-139.
    • (1998) Planta , vol.204 , pp. 131-139
    • Schaffner, A.R.1
  • 42
    • 0036808135 scopus 로고    scopus 로고
    • Aquaporin isoforms responsive to salt and water stresses and phytohormones in radish seedlings
    • Suga, S., Komatsu, S. and Maeshima, M. (2002) Aquaporin isoforms responsive to salt and water stresses and phytohormones in radish seedlings. Plant Cell Physiol. 43: 1229-1237.
    • (2002) Plant Cell Physiol. , vol.43 , pp. 1229-1237
    • Suga, S.1    Komatsu, S.2    Maeshima, M.3
  • 43
    • 0033942378 scopus 로고    scopus 로고
    • Blue light activates potassium-efflux channels in flexor cells from Samanea saman motor organs via two mechanisms
    • Suh, S., Moran, N. and Lee, Y. (2000) Blue light activates potassium-efflux channels in flexor cells from Samanea saman motor organs via two mechanisms. Plant Physiol. 123: 833-843.
    • (2000) Plant Physiol. , vol.123 , pp. 833-843
    • Suh, S.1    Moran, N.2    Lee, Y.3
  • 45
    • 0004178982 scopus 로고    scopus 로고
    • Sinauer Associates, Inc., Publishers, Sunderland, MA
    • Taiz, L. and Zeiger, E. (1998) Plant Physiology, Second edition. p. 99. Sinauer Associates, Inc., Publishers, Sunderland, MA.
    • (1998) Plant Physiology, Second Edition , pp. 99
    • Taiz, L.1    Zeiger, E.2
  • 46
    • 0028318721 scopus 로고
    • Voltage-dependent calcium-permeable channels in the plasma membrane of a higher plant cell
    • Thuleau, P., Ward, J.M., Ranjeva, R. and Schroeder, J.I. (1994) Voltage-dependent calcium-permeable channels in the plasma membrane of a higher plant cell. EMBO J. 13: 2970-2975.
    • (1994) EMBO J. , vol.13 , pp. 2970-2975
    • Thuleau, P.1    Ward, J.M.2    Ranjeva, R.3    Schroeder, J.I.4
  • 47
    • 0034646828 scopus 로고    scopus 로고
    • Transcript levels of the nuclear-encoded respiratory genes in rice decrease by oxygen deprivation: Evidence for involvement of calcium in expression of the alternative oxidase 1a gene
    • Tsuji, H., Nakazono, M., Saisho, D., Tsutsumi, N. and Hirai, A. (2000) Transcript levels of the nuclear-encoded respiratory genes in rice decrease by oxygen deprivation: evidence for involvement of calcium in expression of the alternative oxidase 1a gene. FEBS Lett. 471: 201-204.
    • (2000) FEBS Lett. , vol.471 , pp. 201-204
    • Tsuji, H.1    Nakazono, M.2    Saisho, D.3    Tsutsumi, N.4    Hirai, A.5
  • 48
    • 0036187202 scopus 로고    scopus 로고
    • Plant aquaporins: Multifunctional water and solute channels with expending roles
    • Tyerman, S.D., Niemietz, C.M. and Bramley, H. (2002) Plant aquaporins: multifunctional water and solute channels with expending roles. Plant Cell Environ. 25: 173-194.
    • (2002) Plant Cell Environ. , vol.25 , pp. 173-194
    • Tyerman, S.D.1    Niemietz, C.M.2    Bramley, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.