메뉴 건너뛰기




Volumn 13, Issue 3, 2011, Pages 421-430

The plant Ca2+-ATPase repertoire: Biochemical features and physiological functions

Author keywords

Ca2+ ATPase; Calcium; Calmodulin; P type ATPases; Phospholipids; Phosphorylation

Indexed keywords

BIOCHEMICAL COMPOSITION; CALCIUM; CELL ORGANELLE; ENZYME ACTIVITY; GENE; HYDROLYSIS; IDENTIFICATION METHOD; INHIBITION; ION; MEMBRANE; MUTATION; PHENOTYPE; YEAST;

EID: 79954529869     PISSN: 14358603     EISSN: 14388677     Source Type: Journal    
DOI: 10.1111/j.1438-8677.2010.00405.x     Document Type: Review
Times cited : (80)

References (89)
  • 2
    • 0031177740 scopus 로고    scopus 로고
    • 2+-ATPases in the vacuolar and plasma membrane in cauliflower
    • 2+-ATPases in the vacuolar and plasma membrane in cauliflower. Plant Physiology, 114, 999-1007.
    • (1997) Plant Physiology , vol.114 , pp. 999-1007
    • Askerlund, P.1
  • 3
    • 0000359866 scopus 로고    scopus 로고
    • Calcium efflux transporters in higher plants
    • In: Smallwood M., Knox J.P., Bowles D.J. (Eds), BIOS Scientific Publishers Ltd, Oxford, UK.
    • Askerlund P., Sommarin M. (1996) Calcium efflux transporters in higher plants. In: Smallwood M., Knox J.P., Bowles D.J. (Eds), Membranes: specialised functions in plants. BIOS Scientific Publishers Ltd, Oxford, UK, pp 281-299.
    • (1996) Membranes: specialised functions in plants , pp. 281-299
    • Askerlund, P.1    Sommarin, M.2
  • 6
    • 0034031809 scopus 로고    scopus 로고
    • 2+-ATPase and for the involvement of its activity in the abscisic acid-induced changes in Egeria densa leaves
    • 2+-ATPase and for the involvement of its activity in the abscisic acid-induced changes in Egeria densa leaves. Plant Biology, 2, 168-175.
    • (2000) Plant Biology , vol.2 , pp. 168-175
    • Beffagna, N.1    Romani, G.2    Sforza, M.C.3
  • 11
    • 1642365552 scopus 로고    scopus 로고
    • 2+-ATPase of Arabidopsis thaliana, and characterization of a hyperactive mutant
    • 2+-ATPase of Arabidopsis thaliana, and characterization of a hyperactive mutant. Planta, 218, 814-823.
    • (2004) Planta , vol.218 , pp. 814-823
    • Bonza, M.C.1    Luoni, L.2    De Michelis, M.I.3
  • 14
    • 4744357955 scopus 로고    scopus 로고
    • 2+ pump by substitution of aspartic 170 by asparagine Activation of plasma membrane calcium ATPase 4 without disruption of the interaction between the catalytic core and the C-terminal regulatory domain
    • 2+ pump by substitution of aspartic 170 by asparagine Activation of plasma membrane calcium ATPase 4 without disruption of the interaction between the catalytic core and the C-terminal regulatory domain. Journal of Biological Chemistry, 279, 41619-41625.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 41619-41625
    • Bredeston, L.M.1    Adamo, H.P.2
  • 15
    • 70349653079 scopus 로고    scopus 로고
    • Calcium pumps in health and disease
    • Brini M., Carafoli E. (2009) Calcium pumps in health and disease. Physiological Reviews, 89, 1341-1378.
    • (2009) Physiological Reviews , vol.89 , pp. 1341-1378
    • Brini, M.1    Carafoli, E.2
  • 16
    • 0026074512 scopus 로고
    • Calcium pump of the plasma membrane
    • Carafoli E. (1991) Calcium pump of the plasma membrane. Physiological Reviews, 71, 129-153.
    • (1991) Physiological Reviews , vol.71 , pp. 129-153
    • Carafoli, E.1
  • 17
    • 0000365738 scopus 로고
    • 2+-ATPase of radish seedlings. I. Biochemical characteristics using ITP as a substrate
    • 2+-ATPase of radish seedlings. I. Biochemical characteristics using ITP as a substrate. Plant Physiology, 98, 1196-1201.
    • (1992) Plant Physiology , vol.98 , pp. 1196-1201
    • Carnelli, A.1    De Michelis, M.I.2    Rasi-Caldogno, F.3
  • 19
    • 0003024799 scopus 로고
    • 2+-ATPase of 120 kilodaltons on the endoplasmic reticulum from carrot (Daucus carota) cells
    • 2+-ATPase of 120 kilodaltons on the endoplasmic reticulum from carrot (Daucus carota) cells. Plant Physiology, 102, 651-661.
    • (1993) Plant Physiology , vol.102 , pp. 651-661
    • Chen, F.H.1    Ratterman, D.M.2    Sze, H.3
  • 20
    • 0031105943 scopus 로고    scopus 로고
    • 2+ in the gibberellin-dependent signaling pathway in aleurone cells
    • 2+ in the gibberellin-dependent signaling pathway in aleurone cells. Plant Journal, 11, 363-371.
    • (1997) Plant Journal , vol.11 , pp. 363-371
    • Chen, X.F.1    Chang, M.C.2    Wang, B.Y.3    Wu, R.4
  • 23
    • 0034730505 scopus 로고    scopus 로고
    • Autoinhibition of a calmodulin dependent calcium pump involves a structure in the stalk that connects the transmembrane domain to the ATPase catalytic domain
    • Curran A.C., Hwang H., Corbin J., Martinez S., Rayle D., Sze H., Harper J.F. (2000) Autoinhibition of a calmodulin dependent calcium pump involves a structure in the stalk that connects the transmembrane domain to the ATPase catalytic domain. Journal of Biological Chemistry, 275, 30301-30308.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 30301-30308
    • Curran, A.C.1    Hwang, H.2    Corbin, J.3    Martinez, S.4    Rayle, D.5    Sze, H.6    Harper, J.F.7
  • 25
    • 84995007841 scopus 로고
    • 2+ pump of the plasma membrane of Arabidopsis thaliana: characteristics and sensitivity to fluorescein derivatives
    • 2+ pump of the plasma membrane of Arabidopsis thaliana: characteristics and sensitivity to fluorescein derivatives. Botanica Acta, 106, 20-25.
    • (1993) Botanica Acta , vol.106 , pp. 20-25
    • De Michelis, M.I.1    Carnelli, A.2    Rasi-Caldogno, F.3
  • 26
    • 0001531069 scopus 로고
    • A calmodulin dependent microsomal ATPase from corn (Zea mays L.)
    • Dieter P., Marmè D. (1981) A calmodulin dependent microsomal ATPase from corn (Zea mays L.). FEBS Letters, 125, 245-248.
    • (1981) FEBS Letters , vol.125 , pp. 245-248
    • Dieter, P.1    Marmè, D.2
  • 28
    • 0032486456 scopus 로고    scopus 로고
    • A calcium pump at the higher plant nuclear envelope?
    • Downie L., Priddle J., Hawes C., Evans E. (1998) A calcium pump at the higher plant nuclear envelope? FEBS Letters, 429, 44-48.
    • (1998) FEBS Letters , vol.429 , pp. 44-48
    • Downie, L.1    Priddle, J.2    Hawes, C.3    Evans, E.4
  • 30
    • 0032578026 scopus 로고    scopus 로고
    • P-type calcium ATPases in higher plants - biochemical, molecular and functional properties
    • Evans D.E., Williams L.E. (1998) P-type calcium ATPases in higher plants - biochemical, molecular and functional properties. Biochimica et Biophysica Acta, 1376, 1-25.
    • (1998) Biochimica et Biophysica Acta , vol.1376 , pp. 1-25
    • Evans, D.E.1    Williams, L.E.2
  • 31
    • 0000021063 scopus 로고
    • 2+ homeostasis in Sinapis alba root hairs
    • 2+ homeostasis in Sinapis alba root hairs. Planta, 188, 306-331.
    • (1992) Planta , vol.188 , pp. 306-331
    • Felle, H.1    Tretyn, A.2    Wagner, G.3
  • 34
    • 0034771863 scopus 로고    scopus 로고
    • Plant cells express several stress calcium ATPase but apparently no sodium ATPase
    • Garciadeblas B., Benito B., Rodriguez-Navarro A. (2001) Plant cells express several stress calcium ATPase but apparently no sodium ATPase. Plant and Soil, 235, 181-192.
    • (2001) Plant and Soil , vol.235 , pp. 181-192
    • Garciadeblas, B.1    Benito, B.2    Rodriguez-Navarro, A.3
  • 36
    • 0034529989 scopus 로고    scopus 로고
    • The ACA4 gene of Arabidopsis encodes a vacuolar membrane calcium pump that improves salt tolerance in yeast
    • Geisler M., Frangne N., Gomès E., Martinoia E., Palmgren M.G. (2000b) The ACA4 gene of Arabidopsis encodes a vacuolar membrane calcium pump that improves salt tolerance in yeast. Plant Physiology, 124, 1814-1827.
    • (2000) Plant Physiology , vol.124 , pp. 1814-1827
    • Geisler, M.1    Frangne, N.2    Gomès, E.3    Martinoia, E.4    Palmgren, M.G.5
  • 37
    • 38949110087 scopus 로고    scopus 로고
    • 2+-ATPase regulates adult vegetative development and inflorescence architecture in Arabidopsis
    • 2+-ATPase regulates adult vegetative development and inflorescence architecture in Arabidopsis. Plant Physiology, 146, 716-728.
    • (2008) Plant Physiology , vol.146 , pp. 716-728
    • George, L.1    Romanowsky, S.M.2    Harper, J.F.3    Sharrock, R.4
  • 43
    • 0033759411 scopus 로고    scopus 로고
    • Calmodulin activation of an endoplasmic reticulum-located calcium pump involves an interaction with the N-terminal autoinhibitory domain
    • Hwang I., Harper J.F., Liang F., Sze H. (2000a) Calmodulin activation of an endoplasmic reticulum-located calcium pump involves an interaction with the N-terminal autoinhibitory domain. Plant Physiology, 122, 157-167.
    • (2000) Plant Physiology , vol.122 , pp. 157-167
    • Hwang, I.1    Harper, J.F.2    Liang, F.3    Sze, H.4
  • 47
    • 0030096580 scopus 로고    scopus 로고
    • Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation
    • Knight H., Trewavas A.J., Knight M.R. (1996) Cold calcium signaling in Arabidopsis involves two cellular pools and a change in calcium signature after acclimation. Plant Cell, 8, 489-503.
    • (1996) Plant Cell , vol.8 , pp. 489-503
    • Knight, H.1    Trewavas, A.J.2    Knight, M.R.3
  • 48
    • 0028252762 scopus 로고
    • 2+-pump at the plasma membrane of cultured carrot cells
    • 2+-pump at the plasma membrane of cultured carrot cells. Plant Science, 104, 23-30.
    • (1994) Plant Science , vol.104 , pp. 23-30
    • Kurosaki, F.1    Kaburaki, H.2
  • 54
    • 0032197522 scopus 로고    scopus 로고
    • 2+ pump (ECA1) from the endoplasmic reticulum is inhibited by cyclopiazonic acid but not by thapsigargin
    • 2+ pump (ECA1) from the endoplasmic reticulum is inhibited by cyclopiazonic acid but not by thapsigargin. Plant Physiology, 118, 817-825.
    • (1998) Plant Physiology , vol.118 , pp. 817-825
    • Liang, F.1    Sze, H.2
  • 56
    • 0034613076 scopus 로고    scopus 로고
    • 2+-ATPase of Arabidopsis thaliana reconstituted in proteoliposomes after calmodulin-affinity purification
    • 2+-ATPase of Arabidopsis thaliana reconstituted in proteoliposomes after calmodulin-affinity purification. FEBS Letters, 482, 225-230.
    • (2000) FEBS Letters , vol.482 , pp. 225-230
    • Luoni, L.1    Bonza, M.C.2    De Michelis, M.I.3
  • 59
    • 0030614802 scopus 로고    scopus 로고
    • 2+-ATPase from plant vacuolar membranes with a putative regulatory domain at its N-terminus
    • 2+-ATPase from plant vacuolar membranes with a putative regulatory domain at its N-terminus. FEBS Letters, 400, 324-328.
    • (1997) FEBS Letters , vol.400 , pp. 324-328
    • Malmström, S.1    Askerlund, P.2    Palmgren, M.G.3
  • 60
    • 0034144402 scopus 로고    scopus 로고
    • Regulatory role of the N-terminus of the vacuolar calcium-ATPase in cauliflower
    • Malmström S., Akerlund H.E., Askerlund P. (2000) Regulatory role of the N-terminus of the vacuolar calcium-ATPase in cauliflower. Plant Physiology, 122, 517-526.
    • (2000) Plant Physiology , vol.122 , pp. 517-526
    • Malmström, S.1    Akerlund, H.E.2    Askerlund, P.3
  • 61
    • 57649171349 scopus 로고    scopus 로고
    • Shaping the calcium signature
    • McAinsh M.R., Pittman J.K. (2009) Shaping the calcium signature. New Phytologist, 181, 275-294.
    • (2009) New Phytologist , vol.181 , pp. 275-294
    • McAinsh, M.R.1    Pittman, J.K.2
  • 62
    • 56849123631 scopus 로고    scopus 로고
    • 2+-ATPase by acidic phospholipids: evidence for a phospholipid binding site which overlaps the calmodulin-binding site
    • 2+-ATPase by acidic phospholipids: evidence for a phospholipid binding site which overlaps the calmodulin-binding site. Molecular Membrane Biology, 25, 539-546.
    • (2008) Molecular Membrane Biology , vol.25 , pp. 539-546
    • Meneghelli, S.1    Fusca, T.2    Luoni, L.3    De Michelis, M.I.4
  • 64
    • 0029940235 scopus 로고    scopus 로고
    • Structural organization, ion transport, and energy transduction of P-type ATPases
    • Møller J.V., Juul B., le Maire M. (1996) Structural organization, ion transport, and energy transduction of P-type ATPases. Biochimica et Biophysica Acta, 1286, 1-51.
    • (1996) Biochimica et Biophysica Acta , vol.1286 , pp. 1-51
    • Møller, J.V.1    Juul, B.2    le Maire, M.3
  • 66
    • 0031847388 scopus 로고    scopus 로고
    • 2+ pump is a 120kDa polypeptide regulated by calmodulin binding to a terminal region
    • 2+ pump is a 120kDa polypeptide regulated by calmodulin binding to a terminal region. Physiologia Plantarum, 103, 35-44.
    • (1998) Physiologia Plantarum , vol.103 , pp. 35-44
    • Olbe, M.1    Sommarin, M.2
  • 67
    • 0030838196 scopus 로고    scopus 로고
    • Active calcium transporters in isolated membranes of wheat root cells
    • Olbe M., Widell S., Sommarin M. (1997) Active calcium transporters in isolated membranes of wheat root cells. Journal of Experimental Botany, 48, 1767-1777.
    • (1997) Journal of Experimental Botany , vol.48 , pp. 1767-1777
    • Olbe, M.1    Widell, S.2    Sommarin, M.3
  • 77
    • 0001226199 scopus 로고    scopus 로고
    • Direct measurement of calcium transport across chloroplast inner-envelope vesicles
    • Roh M.H., Shingles R., Cleveland M.J., McCarty R.E. (1998) Direct measurement of calcium transport across chloroplast inner-envelope vesicles. Plant Physiology, 118, 1447-1454.
    • (1998) Plant Physiology , vol.118 , pp. 1447-1454
    • Roh, M.H.1    Shingles, R.2    Cleveland, M.J.3    McCarty, R.E.4
  • 80
    • 20444404681 scopus 로고    scopus 로고
    • 2+ pumps expressed in stomatal guard cells show opposite expression patterns during cold stress
    • 2+ pumps expressed in stomatal guard cells show opposite expression patterns during cold stress. Physiologia Plantarum, 124, 278-283.
    • (2005) Physiologia Plantarum , vol.124 , pp. 278-283
    • Schiøtt, M.1    Palmgren, M.G.2
  • 83
    • 0031926552 scopus 로고    scopus 로고
    • Calmodulin, calmodulin-related proteins and plant responses to the environment
    • Snedden W.A., Fromm H. (1998) Calmodulin, calmodulin-related proteins and plant responses to the environment. Trends in Plant Science, 3, 299-304.
    • (1998) Trends in Plant Science , vol.3 , pp. 299-304
    • Snedden, W.A.1    Fromm, H.2
  • 84
    • 0034647919 scopus 로고    scopus 로고
    • Maize cap1 encodes a novel SERCA-type calcium ATPase with a calmodulin-binding domain
    • Subbaiah C.C., Sachs M.M. (2000) Maize cap1 encodes a novel SERCA-type calcium ATPase with a calmodulin-binding domain. Journal of Biological Chemistry, 275, 21678-21687.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 21678-21687
    • Subbaiah, C.C.1    Sachs, M.M.2
  • 88
    • 1542350090 scopus 로고    scopus 로고
    • Structurally homologous binding of plant calmodulin isoforms to the calmodulin-binding domain of vacuolar calcium-ATPase
    • Yamniuk A.P., Vogel H.J. (2004) Structurally homologous binding of plant calmodulin isoforms to the calmodulin-binding domain of vacuolar calcium-ATPase. Journal of Biological Chemistry, 279, 7698-7707.
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 7698-7707
    • Yamniuk, A.P.1    Vogel, H.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.