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  • Title: Involvement of Ral GTPase in v-Src-induced phospholipase D activation.
    Author: Jiang H, Luo JQ, Urano T, Frankel P, Lu Z, Foster DA, Feig LA.
    Journal: Nature; 1995 Nov 23; 378(6555):409-12. PubMed ID: 7477381.
    Abstract:
    An early response to the tyrosine kinase activity of v-Src is an increase in phospholipase D (PLD) activity, which leads to the generation of biologically active lipid second messengers, including phosphatidic acid, lysophosphatidic acid and diacylglycerol. We have recently demonstrated that v-Src-induced PLD activity is mediated by Ras, although Ras involvement was indirect, requiring a cytosolic factor for PLD activation. Ras interacts with and activates Ral-GDS, the exchange factor responsible for the activation of Ral GTPases. Here we report that this newly identified Ras/Ral signalling pathway mediates PLD activation by v-Src. PLD activity could be precipitated from v-Src-transformed cell lysates with immobilized RalA protein and with an anti-Ral antibody. A mutation to the region of RalA analogous to the 'effector domain' of Ras did not reduce the ability of RalA to complex with PLD, although deletion of a Ral-specific amino-terminal region did. Overexpression of RalA potentiated PLD activation by v-Src, and expression of dominant negative RalA mutants inhibited both v-Src- and v-Ras-induced PLD activity. Thus RalA is involved in the tyrosine kinase activation of PLD through its unique N terminus, and that PLD is a downstream target of a Ras/Ral GTPase cascade.
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