Binding of 14-3-3 protein to the plasma membrane H+-ATPase AHA2 involves the three C-terminal residues Tyr946-Thr-Val and requires phosphorylation of Thr947

被引:286
作者
Fuglsang, AT
Visconti, S
Drumm, K
Jahn, T
Stensballe, A
Mattei, B
Jensen, ON
Aducci, P
Palmgren, MG
机构
[1] Royal Vet & Agr Univ, Dept Plant Biol, DK-1871 Frederiksberg, Copenhagen, Denmark
[2] Univ Roma Tor Vergata, Dept Biol, I-00133 Rome, Italy
[3] Odense Univ, Univ So Denmark, Dept Biol Mol, Prot Res Grp, DK-5230 Odense, Denmark
[4] Univ Rome La Sapienza, Dept Plant Biol, I-00185 Rome, Italy
关键词
D O I
10.1074/jbc.274.51.36774
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
14-3-3 proteins play a regulatory role in a diverse array of cellular functions such as apoptosis, regulation of the cell cycle, and regulation of gene transcription. The phytotoxin fusicoccin specifically induces association of virtually any 14-3-3 protein to plant plasma membrane Hf-ATPase. The 14-3-3 binding site in the Arabidopsis plasma membrane H+-ATPase AHA2 was localized to the three C-terminal residues of the enzyme (Tyr(946)-Thr-Val). finding of 14-3-3 protein to this target was induced by phosphorylation of Thr(947) (K-D = 88 nM) and was in practice irreversible in the presence of fusicoccin (K-D = 7 nM). Mass spectrometry analysis demonstrated that AHA2 expressed in yeast was phosphorylated at Thr(947). We conclude that the extreme end of AHA2 contains an unusual high-affinity binding site for 14-3-3 protein.
引用
收藏
页码:36774 / 36780
页数:7
相关论文
共 45 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] ISOLATION OF PHOSPHOPROTEINS BY IMMOBILIZED METAL (FE-3+) AFFINITY-CHROMATOGRAPHY
    ANDERSSON, L
    PORATH, J
    [J]. ANALYTICAL BIOCHEMISTRY, 1986, 154 (01) : 250 - 254
  • [3] Binding of purified 14-3-3 ζ signaling protein to discrete amino acid sequences within the cytoplasmic domain of the platelet membrane glycoprotein Ib-IX-V complex
    Andrews, RK
    Harris, SJ
    McNally, T
    Berndt, MC
    [J]. BIOCHEMISTRY, 1998, 37 (02) : 638 - 647
  • [4] Molecular dissection of the C-terminal regulatory domain of the plant plasma membrane H+-ATPase AHA2:: Mapping of residues that when altered give rise to an activated enzyme
    Axelsen, KB
    Venema, K
    Jahn, T
    Baunsgaard, L
    Palmgren, MG
    [J]. BIOCHEMISTRY, 1999, 38 (22) : 7227 - 7234
  • [5] The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14-3-3 protein
    Bachmann, M
    Huber, JL
    Liao, PC
    Gage, DA
    Huber, SC
    [J]. FEBS LETTERS, 1996, 387 (2-3) : 127 - 131
  • [6] FUSICOCCIN BINDING-SITES IN SUBCELLULAR PREPARATIONS OF SPINACH LEAVES
    BALLIO, A
    FEDERICO, R
    PESSI, A
    SCALORBI, D
    [J]. PLANT SCIENCE LETTERS, 1980, 18 (01): : 39 - 44
  • [7] BALLIO A, 1968, Annali dell'Istituto Superiore di Sanita, V4, P317
  • [8] 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
  • [9] MATURATION OF THE YEAST PLASMA-MEMBRANE [H+]ATPASE INVOLVES PHOSPHORYLATION DURING INTRACELLULAR-TRANSPORT
    CHANG, A
    SLAYMAN, CW
    [J]. JOURNAL OF CELL BIOLOGY, 1991, 115 (02) : 289 - 295
  • [10] THE RETINOBLASTOMA PROTEIN ASSOCIATES WITH THE PROTEIN PHOSPHATASE TYPE-1 CATALYTIC SUBUNIT
    DURFEE, T
    BECHERER, K
    CHEN, PL
    YEH, SH
    YANG, YZ
    KILBURN, AE
    LEE, WH
    ELLEDGE, SJ
    [J]. GENES & DEVELOPMENT, 1993, 7 (04) : 555 - 569