Pumping with plant P-type ATPases

被引:120
作者
Palmgren, MG
Harper, JF
机构
[1] Royal Vet & Agr Univ, Dept Plant Biol, DK-1871 Copenhagen, Denmark
[2] Scripps Res Inst, Dept Cell Biol, La Jolla, CA 92037 USA
关键词
P-type ATPases; plasma membrane; ER; tonoplast; proton pump; transport;
D O I
10.1093/jexbot/50.suppl_1.883
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
In the past 10 years, research on P-type ATPases in plants has advanced from its roots in biochemistry to molecular biology, genetics, structure, and back to biochemistry. Since the first cloning of a plant proton pump, plant genes have been identified from all five groups of P-type ATPases. These pumps have been implicated in the transport of multiple ions, including protons, calcium, manganese, molybdenum, copper, and phospholipids. To mediate similar cellular functions, plants and animals in some cases utilize entirely different ion pumps. For example, plants utilize an H+- ATPase instead of an Na+/K+-ATPase to energize the plasma membrane with an electrochemical gradient. Another distinction between plants and animals is that in some cases similar pumps are used in different subcellular locations. For example, while in animals the 'plasma membrane'-type calmodulin-regulated Ca2+-ATPases are exclusively found in plasma membrane, several plant homologues have been found in endomembrane locations, such as the ER and tonoplast. Through multidisciplinary approaches the next decade should reveal insights into important questions, including: What are the ion specificities of various divergent pumps? What are the structural changes mediating ion translocation? What are the cellular and organismal functions of different pumps? How are pumps regulated? and, ultimately, How can we use our knowledge of P-type ATPases for applications in agriculture?
引用
收藏
页码:883 / 893
页数:11
相关论文
共 78 条
  • [1] 14-3-3 and its possible role in co-ordinating multiple signalling pathways
    Aitken, A
    [J]. TRENDS IN CELL BIOLOGY, 1996, 6 (09) : 341 - 347
  • [2] The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold
    Aravind, L
    Galperin, MY
    Koonin, EV
    [J]. TRENDS IN BIOCHEMICAL SCIENCES, 1998, 23 (04) : 127 - 129
  • [3] Three-dimensional map of the plasma membrane H+-ATPase in the open conformation
    Auer, M
    Scarborough, GA
    Kühlbrandt, W
    [J]. NATURE, 1998, 392 (6678) : 840 - 843
  • [4] Evolution of substrate specificities in the P-type ATPase superfamily
    Axelsen, KB
    Palmgren, MG
    [J]. JOURNAL OF MOLECULAR EVOLUTION, 1998, 46 (01) : 84 - 101
  • [5] Modified plant plasma membrane H+-ATPase with improved transport coupling efficiency identified by mutant selection in yeast
    Baunsgaard, L
    Venema, K
    Axelsen, KB
    Villalba, JM
    Welling, A
    Wollenweber, B
    Palmgren, MG
    [J]. PLANT JOURNAL, 1996, 10 (03) : 451 - 458
  • [6] The 14-3-3 proteins associate with the plant plasma membrane H+-ATPase to generate a fusicoccin binding complex and a fusicoccin responsive system
    Baunsgaard, L
    Fuglsang, AT
    Jahn, T
    Korthout, HAAJ
    de Boer, AH
    Palmgren, MG
    [J]. PLANT JOURNAL, 1998, 13 (05) : 661 - 671
  • [7] MOLECULAR-CLONING OF A FAMILY OF PLANT GENES ENCODING A PROTEIN HOMOLOGOUS TO PLASMA-MEMBRANE H+-TRANSLOCATING ATPASES
    BOUTRY, M
    MICHELET, B
    GOFFEAU, A
    [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1989, 162 (02) : 567 - 574
  • [8] ATP synthase - past and future
    Boyer, PD
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 1998, 1365 (1-2): : 3 - 9
  • [9] A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis
    Bull, LN
    van Eijk, MJT
    Pawlikowska, L
    DeYoung, JA
    Juijn, JA
    Liao, M
    Klomp, LWJ
    Lomri, N
    Berger, R
    Scharschmidt, BF
    Knisely, AS
    Houwen, RHJ
    Freimer, NB
    [J]. NATURE GENETICS, 1998, 18 (03) : 219 - 224
  • [10] Characterization of a protease-resistant domain of the cytosolic portion of sarcoplasmic reticulum Ca2+-ATPase -: Nucleotide- and metal-binding sites
    Champeil, P
    Menguy, T
    Soulié, S
    Juul, B
    de Gracia, AG
    Rusconi, F
    Falson, P
    Denoroy, L
    Henao, F
    le Maire, M
    Moller, JV
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (12) : 6619 - 6631