Plant PIP2-dependent phospholipase D activity is regulated by phosphorylation
Jazyk angličtina Země Anglie, Velká Británie Médium print
Typ dokumentu časopisecké články, práce podpořená grantem, 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-zdroje
- MeSH
- Brassica enzymologie MeSH
- fosfatidylinositol-4,5-difosfát metabolismus MeSH
- fosfolipasa D metabolismus MeSH
- fosforylace MeSH
- kyselá fosfatasa metabolismus MeSH
- membránové proteiny metabolismus MeSH
- peptidové fragmenty MeSH
- rostlinné proteiny metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvenční seřazení MeSH
- spektrometrie hmotnostní - ionizace laserem za účasti matrice MeSH
- vazebná místa MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
- Názvy látek
- fosfatidylinositol-4,5-difosfát MeSH
- fosfolipasa D MeSH
- kyselá fosfatasa MeSH
- membránové proteiny MeSH
- peptidové fragmenty MeSH
- rostlinné proteiny 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.
Citace poskytuje Crossref.org
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