High impact information on PLDBETA1

• PLDbetacat exhibited Ca(2+)-dependent activity, was much less active, and required a higher level of Ca(2+) than the full-length PLDbeta [1].
• Scatchard plot analysis of Ca(2+) binding data yielded an estimate of 3.6 high affinity (K(d) = 29 mum) binding sites on PLDbeta [1].
• These conformational changes, not shown by any of the previously characterized C2 domains of animal origin, occurred at micromolar Ca(2+) concentrations for PLDbeta C2 but at millimolar levels of the cation for PLDalpha C2 [2].
• Multiple amino acid sequence alignments suggest that PLDalpha and PLDbeta both contain a Ca(2+)-dependent phospholipid-binding C2 domain near their N termini [2].
• The PLDbeta cDNA contains an open reading frame of 2904 nucleotides coding for a 968-amino acid protein of 108,575 daltons [3].

Biological context of PLDBETA1

• 9. PLDgamma shares a 66% amino acid sequence identity with PLDbeta, but only a 41% identity with PLDalpha [4].
• Phospholipase D (PLD; EC 3.1.4.4) plays an important role in membrane lipid hydrolysis and in mediation of plant responses to a wide range of stresses [5].

Anatomical context of PLDBETA1

• In contrast, PLDbeta was not detectable in any of the subcellular fractions [6].

Associations of PLDBETA1 with chemical compounds

• Binding studies showed that the PLDs bound PIP2 in the order of PLDbeta > PLDgamma > PLDalpha [4].
• Sequence analysis reveals that PLDbeta is evolutionarily divergent from PLDalpha and that its N terminus contains a regulatory Ca2+-dependent phospholipid-binding (C2) domain that is found in a number of signal transducing and membrane trafficking proteins [3].
• The activity of the expressed PLDbeta is dependent on PIP2 and submicromolar amounts of Ca2+, inhibited by neomycin, and stimulated by a soluble factor from plant extracts [3].
• We were thus able to identify 58 genes that were regulated by temperature downshift via PLC activity and 87 genes regulated by temperature downshift via PLD-produced phosphatidic acid [7].
• PLD zeta 1 requires PIP(2) for activity, but unlike the PIP(2)-requiring PLD beta or gamma, phosphatidylethanolamine is not needed in substrate vesicles [8].

Analytical, diagnostic and therapeutic context of PLDBETA1

• Molecular cloning and functional analysis of polyphosphoinositide-dependent phospholipase D, PLDbeta, from Arabidopsis [3].

References