14-3-3 Proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner. (December 2000)

• Record Type: Journal Article
• Authors: Holtman, W. L.; Roberts, M. R.; Wang, M.
• Is Part Of: Biochemical Society transactions. Volume 28:Number 6(2000)
• Page Start: 834
• Page End: 836
• Publication Date: 2000-12
• Subjects: lipid metabolism -- protein interactions; LOX, lipoxygenase -- PP2A, protein phosphatase 2A -- HMM, high-molecular-mass -- FC, fusicoccin -- 13-HPOD, 13-hydroxy-9Z, 11 E-octadecadieonic acid -- 9-HPOD, 9-hydroperoxy-10E, 12Z-octadecadieonic acid; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0280834
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : Recently, we have demonstrated by two different methods that lipoxgenases (LOXs) and 14-3-3 proteins form interactions in barley embryos [Holtman, Roberts, Oppedijk, Testerink, van Zeij] and Wang (2000) FEBS Lett. 474, 48–52]. It was shown by both co-immunoprecipitations and surface-plasmon resonance experiments that 13-LOX, but not 9-LOX, forms interactions with 14-3-3 proteins. In the present report we show that the presence of 13-LOX and 14-3-3 proteins was established in high-molecular-mass complexes. Amounts of 13-LOX and 14-3-3 proteins in high-molecular-mass fractions increased during germination, but were reduced after dephosphorylation of protein extracts or competition with the 14-3-3-binding peptide P-Raf-259, indicating that 13-LOX and 14-3-3 proteins interact in a phosphorylation-dependent manner.