Loss of receptor regulation by a phospholipase D1 mutant unresponsive to protein kinase C |
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| Authors: | Zhang Y Altshuller Y M Hammond S M Hayes F Morris A J Frohman M A |
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| Affiliation: | Molecular and Cellular Biology Program, SUNY at Stony Brook, Stony Brook, NY 11794-8651, USA. |
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| Abstract: | Activation of phosphatidylcholine-specific phospholipase D (PLD) constitutes an important part of the cellular response to agonist signaling. PLD1 is stimulated in vitro in a direct and synergistic manner by protein kinase C (PKC), ADP-ribosylation factor (ARF) and Rho family members. However, the direct and specific role of each of these effectors in agonist-stimulated PLD activation is poorly understood. We have used transposon mutagenesis to generate a library of PLD1 alleles containing random pentapeptide insertions. Forty-five alleles were characterized to identify functionally important regions. Use of an allele unresponsive to PKC, but otherwise seemingly normal, to examine coupling of PLD1 to a subset of G-protein-coupled receptors demonstrates for the first time direct stimulation of PLD1 in vivo by PKC and reveals that this direct stimulation is unexpectedly critical for PLD1 activation. |
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