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Calcium‐Induced Membrane Microdomains Trigger Plant Phospholipase D Activity
Author(s) -
Kuppe Konstantin,
Kerth Andreas,
Blume Alfred,
UlbrichHofmann Renate
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200800431
Subject(s) - popc , phospholipase d , phospholipid , chemistry , vesicle , biophysics , calcium , lipid microdomain , biochemistry , membrane , enzyme , biology , organic chemistry
Plant α‐type phospholipase D proteins are calcium‐dependent, lipolytic enzymes. The morphology of the aggregates of their phospholipid substrate fundamentally defines the interaction between the enzyme and the surface. Here we demonstrate that the Ca 2+ ‐induced generation of membrane microdomains dramatically activates α‐type phospholipase D from white cabbage. 500‐fold stimulation was observed upon incorporation of 10 mol % 1‐palmitoyl‐2‐oleoyl‐ sn ‐glycero‐3‐phosphate (POPA) into 1‐palmitoyl‐2‐oleoyl‐ sn ‐glycero‐3‐phosphocholine (POPC) vesicles in the presence of Ca 2+ ions. Enhanced association of PLD α 2 with phospholipid surfaces containing anionic components was indicated by lag phase analysis and film balance measurements. Differential scanning calorimetry showed that the POPA‐specific activation correlates with the phase behavior of the POPC/POPA vesicles in the presence of Ca 2+ ions. We conclude from the results that the Ca 2+ ‐induced formation of POPA microdomains is the crucial parameter that facilitates the binding of PLD to the phospholipid surface and suggest that this effect serves as a cellular switch for controlling PLD activity.