Arabidonsis sphingosine kinase and the effects of phytosphingosine-1-phosphate on stomatal aperture

被引:118
作者
Coursol, S [1 ]
Le Stunff, H
Lynch, DV
Gilroy, S
Assmann, SM
Spiegel, S
机构
[1] Penn State Univ, Dept Biol, University Pk, PA 16802 USA
[2] Univ Paris 11, Stn Genet Vegetale,Natl Agron Paris Grignon, Unite Mixte Rech 320, Inst Natl Rech Agron,Ctr Natl Rech Sci 8120, F-91190 Gif Sur Yvette, France
[3] Virginia Commonwealth Univ, Med Ctr, Dept Biochem, Richmond, VA 23892 USA
[4] Univ Paris 11, Lab Activat Cellulaire & Transduct Signaux, Inst Biochim & Biophys Mol & Cellulaire, Unite Mixte Rech 8619,Ctr Natl Rech Sci, F-91405 Orsay, France
[5] Williams Coll, Dept Biol, Williamstown, MA 01267 USA
关键词
D O I
10.1104/pp.104.055806
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Sphingolipids are a major component of membrane lipids and their metabolite sphingosine-1-phosphate (S1P) is a potent lipid mediator in animal cells. Recently, we have shown that the enzyme responsible for S1P production, sphingosine kinase (SphK), is stimulated by the phytohormone abscisic acid in guard cells of Arabidopsis (Arabidopsis thaliana) and that S1P is effective in regulating guard cell turgor. We have now characterized SphK from Arabidopsis leaves. SphK activity was mainly associated with the membrane fraction and phosphorylated predominantly the Delta4-unsaturated long-chain sphingoid bases sphingosine (Sph) and 4,8-sphingadienine, and to a lesser extent, the saturated long-chain sphingoid bases dihydrosphingosine and phytosphingosine (Phyto-Sph). 4-Hydroxy-8-sphingenine, which is a major sphingoid base in complex glycosphingolipids from Arabidopsis leaves, was a relatively poor substrate compared with the corresponding saturated Phyto-Sph. In contrast, mammalian SphK1 efficiently phosphorylated Sph, dihydrosphingosine, and 4,8-sphingadienine, but not the 4-hydroxylated long-chain bases Phyto-Sph and 4-hydroxy-8-sphingenine. Surface dilution kinetic analysis of Arabidopsis SphK with Sph presented in mixed Triton X-100 micelles indicated that SphK associates with the micellar surface and then with the substrate presented on the surface. In addition, measurements of SphK activity under different assay conditions combined with phylogenetic analysis suggest that multiple isoforms of SphK may be expressed in Arabidopsis. Importantly, we found that phytosphingosine-l-phosphate, similar to S1P, regulates stomatal apertures and that its action is impaired in guard cells of Arabidopsis plants harboring T-DNA null mutations in the sole prototypical G-protein a-subunit gene, GPA1.
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收藏
页码:724 / 737
页数:14
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