Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
PubMed
14596913
DOI
10.1016/s0014-5793(03)01093-7
PII: S0014579303010937
Knihovny.cz E-resources
- MeSH
- Brassica enzymology MeSH
- Phosphatidylinositol 4,5-Diphosphate metabolism MeSH
- Phospholipase D metabolism MeSH
- Phosphorylation MeSH
- Acid Phosphatase metabolism MeSH
- Membrane Proteins metabolism MeSH
- Peptide Fragments MeSH
- Plant Proteins metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Alignment MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization MeSH
- Binding Sites MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
- Names of Substances
- Phosphatidylinositol 4,5-Diphosphate MeSH
- Phospholipase D MeSH
- Acid Phosphatase MeSH
- Membrane Proteins MeSH
- Peptide Fragments MeSH
- Plant Proteins MeSH
Phospholipase D (PLD) forms the major family of phospholipases that was first discovered and cloned in plants. In this report we have shown, for the first time, that C2 phosphatidylinositol-4,5-bisphosphate (PIP2)-dependent PLD(s) from 5 day hypocotyls of Brassica oleracea associated with plasma membrane is covalently modified-phosphorylated. Pre-incubation of the plasma membrane fraction with acid phosphatase resulted in concentration-dependent inhibition of PIP2-dependent PLD activity. Using matrix-assisted laser desorption/ionization time of flight mass spectrometry of tryptic in-gel digests, the BoPLDgamma(1,2) isoform was identified. Comparing the spectra of the proteins obtained from the plasma membrane fractions treated and non-treated with acid phosphatase, three peptides differing in the mass of the phosphate group (80 Da) were revealed: TMQMMYQTIYK, EVADGTVSVYNSPR and KASKSRGLGK which possess five potential Ser/Thr phosphorylation sites. Our findings suggest that a phosphorylation/dephosphorylation mechanism may be involved in the regulation of plant PIP2-dependent PLDgamma activity.
References provided by Crossref.org
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