Binding of abscisic acid to human LANCL2

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• 作者：Laura  ; Sturla^a ;   ; ¹ ;   ; ^{laurasturla@unige.it} ; Chiara  ; Fresia^a ;   ; ^b ;   ; ¹ ; Lucrezia  ; Guida^a ; Alessia  ; Grozio^a ; Tiziana  ; Vigliarolo^a ; Elena  ; Mannino^a ; Enrico  ; Millo^a ; Luca  ; Bagnasco^c ; Santina  ; Bruzzone^a ;   ; ^b ; Antonio  ; De Flora^a ; Elena  ; Zocchi^a ;   ; ^b
• 关键词：Specific binding ; Abscisic acid ; Human LANCL2
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2011
• 出版时间：18 November 2011
• 年：2011
• 卷：415
• 期：2
• 页码：390-395
• 全文大小：552 K

文摘

The phytohormone abscisic acid (ABA) is the central regulator of abiotic stress in plants and plays important roles during plant growth and development. In animal cells, ABA was shown to be an endogenous hormone, acting as a stress signal and stimulating cell functions involved in inflammatory responses and in insulin release. Recently, we demonstrated that Lanthionine synthetase component C-like protein 2 (LANCL2) is required for ABA binding to the plasmamembrane of granulocytes and for the activation of the signaling pathway triggered by ABA in human granulocytes and in rat insulinoma cells. In order to investigate whether ABA activates LANCL2 via direct interaction, we performed specific binding studies on human LANCL2 recombinant protein using different experimental approaches (saturation binding, scintillation proximity assays, dot blot experiments and affinity chromatography). Altogether, results indicate that human recombinant LANCL2 binds ABA directly and provide the first demonstration of ABA binding to a mammalian ABA receptor.