Journal of Plant Research

, Volume 125, Issue 3, pp 439–449

Degradation of long-chain base 1-phosphate (LCBP) in Arabidopsis: functional characterization of LCBP phosphatase involved in the dehydration stress response

Authors

  • Noriko Nakagawa
    • Department of Biology, Graduate School of Natural ScienceKonan University
  • Mai Kato
    • Department of Biology, Graduate School of Natural ScienceKonan University
  • Yohei Takahashi
    • Department of Biology, Faculty of ScienceKyushu University
  • Ken-ichiro Shimazaki
    • Department of Biology, Faculty of ScienceKyushu University
  • Kentarao Tamura
    • Department of Botany, Graduate School of ScienceKyoto University
  • Yoshihiko Tokuji
    • Department of Food ScienceObihiro University of Agriculture and Veterinary Medicine
  • Akio Kihara
    • Laboratory of Biochemistry, Faculty of Pharmaceutical SciencesHokkaido University
    • Department of Biology, Graduate School of Natural ScienceKonan University
Regular Paper

DOI: 10.1007/s10265-011-0451-9

Cite this article as:
Nakagawa, N., Kato, M., Takahashi, Y. et al. J Plant Res (2012) 125: 439. doi:10.1007/s10265-011-0451-9

Abstract

Sphingolipid metabolites, long-chain base 1-phosphates (LCBPs), are involved in ABA signaling pathways. The LCBPs synthesized by long-chain base kinase are dephosphorylated by LCBP phosphatase or degraded by LCBP lyase. Here we show that the At3g58490 gene encodes AtSPP1, a functional LCBP phosphatase. Transient expression of green fluorescent protein fusion in suspension-cultured Arabidopsis cells showed that AtSPP1 is localized in the endoplasmic reticulum. The level of dihydrosphingosine 1-phosphate was increased in loss-of-function mutants (spp1) compared with wild-type (WT) plants, suggesting a role of AtSPP1 in regulating LCBP levels. The rate of decrease in fresh weight of detached aerial parts was significantly slower in spp1 mutants than in WT plants. A stomatal closure bioassay showed that the stomata of spp1 mutants were more sensitive than the WT to ABA, suggesting that AtSPP1 is involved in guard cell signaling. However, spp1 mutants showed decreased sensitivity to ABA with respect to primary root growth but not to seed germination. The response to fumonisin B1 did not differ between the WT and spp1 mutant. A significant decrease in AtDPL1 (LCBP lyase) transcripts in spp1 mutants was observed. We conclude that AtSPP1 is a functional LCBP phosphatase that may play a role in stomatal responses through LCBP-mediated ABA signaling.

Keywords

ABA Arabidopsis thaliana Dehydration stress Long-chain base 1-phosphate phosphatase Stomatal closure Sphingolipids

Abbreviations

Dhs

Dihydrosphingosine

Dhs-P

Dihydrosphingosine 1-phosphate

FB1

Fumonisin B1

LCB

Long-chain base

LCBP

Long-chain base 1-phosphate

Phs

Phytosphingosine

Phs-P

Phytosphingosine 1-phosphate

Sph

Sphingosine

Sph-P

Sphingosine 1-phosphate

Supplementary material

10265_2011_451_MOESM1_ESM.pdf (123 kb)
Supplementary Fig. S1 (PDF 122 kb)
10265_2011_451_MOESM2_ESM.pdf (132 kb)
Supplementary Fig. S2 (PDF 131 kb)
10265_2011_451_MOESM3_ESM.pdf (98 kb)
Supplementary Fig. S3 (PDF 98 kb)
10265_2011_451_MOESM4_ESM.pdf (60 kb)
Supplementary Table S1 (PDF 60 kb)
10265_2011_451_MOESM5_ESM.pdf (89 kb)
Supplementary Table S2 (PDF 88 kb)

Copyright information

© The Botanical Society of Japan and Springer 2011