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14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner.

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14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner. / Holtman, W. L.; Roberts, Michael R.; Wang, Mei.
In: Biochemical Society Transactions, Vol. 28, No. 6, 12.2000, p. 834-836.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Holtman, WL, Roberts, MR & Wang, M 2000, '14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner.', Biochemical Society Transactions, vol. 28, no. 6, pp. 834-836. https://doi.org/10.1042/bst0280834

APA

Holtman, W. L., Roberts, M. R., & Wang, M. (2000). 14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner. Biochemical Society Transactions, 28(6), 834-836. https://doi.org/10.1042/bst0280834

Vancouver

Holtman WL, Roberts MR, Wang M. 14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner. Biochemical Society Transactions. 2000 Dec;28(6):834-836. doi: 10.1042/bst0280834

Author

Holtman, W. L. ; Roberts, Michael R. ; Wang, Mei. / 14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner. In: Biochemical Society Transactions. 2000 ; Vol. 28, No. 6. pp. 834-836.

Bibtex

@article{bb60c02801884c868d510819a10403ca,
title = "14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner.",
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 Zeijl 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.",
keywords = "lipid metabolism, protein interactions.",
author = "Holtman, {W. L.} and Roberts, {Michael R.} and Mei Wang",
year = "2000",
month = dec,
doi = "10.1042/bst0280834",
language = "English",
volume = "28",
pages = "834--836",
journal = "Biochemical Society Transactions",
issn = "0300-5127",
publisher = "Portland Press Ltd.",
number = "6",

}

RIS

TY - JOUR

T1 - 14-3-3 proteins and a 13-lipoxygenase form associations in a phosphorylation-dependent manner.

AU - Holtman, W. L.

AU - Roberts, Michael R.

AU - Wang, Mei

PY - 2000/12

Y1 - 2000/12

N2 - 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 Zeijl 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.

AB - 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 Zeijl 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.

KW - lipid metabolism

KW - protein interactions.

U2 - 10.1042/bst0280834

DO - 10.1042/bst0280834

M3 - Journal article

VL - 28

SP - 834

EP - 836

JO - Biochemical Society Transactions

JF - Biochemical Society Transactions

SN - 0300-5127

IS - 6

ER -