A protein kinase target of a PDK1 signalling pathway is involved in root hair growth in Arabidopsis

被引:218
作者
Anthony, RG
Henriques, R
Helfer, A
Mészáros, T
Rios, G
Testerink, C
Munnik, T
Deák, M
Koncz, C
Bögre, L
机构
[1] Univ London Royal Holloway & Bedford New Coll, Sch Biol Sci, Egham TW20 0EX, Surrey, England
[2] Max Planck Inst Zuchtungsforsch, D-5000 Cologne, Germany
[3] Univ Amsterdam, Dept Plant Physiol, Swammerdam Inst Life Sci, NL-1012 WX Amsterdam, Netherlands
[4] Univ Dundee, MRC, Prot Phosphorylat Unit, Dundee, Scotland
基金
英国生物技术与生命科学研究理事会;
关键词
AGC kinase; growth signalling; lipid signalling; PDK1; phosphatidic acid; root hair elongation;
D O I
10.1038/sj.emboj.7600068
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
Here we report on a lipid-signalling pathway in plants that is downstream of phosphatidic acid and involves the Arabidopsis protein kinase, AGC2-1, regulated by the 3'-phosphoinositide-dependent kinase-1 (AtPDK1). AGC2-1 specifically interacts with AtPDK1 through a conserved C-terminal hydrophobic motif that leads to its phosphorylation and activation, whereas inhibition of AtPDK1 expression by RNA interference abolishes AGC2-1 activity. Phosphatidic acid specifically binds to AtPDK1 and stimulates AGC2-1 in an AtPDK1-dependent manner. AtPDK1 is ubiquitously expressed in all plant tissues, whereas expression of AGC2-1 is abundant in fast-growing organs and dividing cells, and activated during re-entry of cells into the cell cycle after sugar starvation-induced G1-phase arrest. Plant hormones, auxin and cytokinin, synergistically activate the AtPDK1-regulated AGC2-1 kinase, indicative of a role in growth and cell division. Cellular localisation of GFP-AGC2-1 fusion protein is highly dynamic in root hairs and at some stages confined to root hair tips and to nuclei. The agc2-1 knockout mutation results in a reduction of root hair length, suggesting a role for AGC2-1 in root hair growth and development.
引用
收藏
页码:572 / 581
页数:10
相关论文
共 46 条
  • [1] Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase B alpha
    Alessi, DR
    James, SR
    Downes, CP
    Holmes, AB
    Gaffney, PRJ
    Reese, CB
    Cohen, P
    [J]. CURRENT BIOLOGY, 1997, 7 (04) : 261 - 269
  • [2] Discovery of PDKI, one of the missing links in insulin signal transduction
    Alessi, DR
    [J]. BIOCHEMICAL SOCIETY TRANSACTIONS, 2001, 29 : 1 - 14
  • [3] Regulation of the pollen-specific actin-depolymerizing factor LIADF1
    Allwood, EG
    Anthony, RG
    Smertenko, AP
    Reichelt, S
    Drobak, BK
    Doonan, JH
    Weeds, AG
    Hussey, PJ
    [J]. PLANT CELL, 2002, 14 (11) : 2915 - 2927
  • [4] Snapping of the carboxyl terminal tail of the catalytic subunit of PKA onto its core: Characterization of the sites by mutagenesis
    Batkin, M
    Schvartz, I
    Shaltiel, S
    [J]. BIOCHEMISTRY, 2000, 39 (18) : 5366 - 5373
  • [5] BAUDE EJ, 1994, J BIOL CHEM, V269, P2316
  • [6] Benjamins R, 2001, DEVELOPMENT, V128, P4057
  • [7] Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA
    Biondi, RM
    Cheung, PCF
    Casamayor, A
    Deak, M
    Currie, RA
    Alessi, DR
    [J]. EMBO JOURNAL, 2000, 19 (05) : 979 - 988
  • [8] BIONDI RM, 2003, BIOCHEM J, V15, P1
  • [9] The cdc2Ms kinase is differently regulated in the cytoplasm and in the nucleus
    Bogre, L
    Zwerger, K
    Meskiene, I
    Binarova, P
    Csizmadia, V
    Planck, C
    Wagner, E
    Hirt, H
    HeberleBors, E
    [J]. PLANT PHYSIOLOGY, 1997, 113 (03) : 841 - 852
  • [10] Growth signalling pathways in Arabidopsis and the AGC protein kinases
    Bögre, L
    Ökrész, L
    Henriques, R
    Anthony, RG
    [J]. TRENDS IN PLANT SCIENCE, 2003, 8 (09) : 424 - 431