Involvement of Ral GTPase in v-Src-induced phospholipase D activation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-11-01

AUTHORS

Hong Jiang, Jing-Qing Luo, Takeshi Urano, Paul Frankel, Zhimin Lu, David A. Foster, Larry A. Feig

ABSTRACT

AN early response to the tyrosine kinase activity of v-Src is an increase in phospholipase D (PLD) activity1, which leads to the generation of biologically active lipid second messengers, including phosphatidic acid, lysophosphatidic acid and diacylglycerol2. We have recently demonstrated that v-Src-induced PLD activity is mediated by Ras3, although Ras involvement was indirect, requiring a cytosolic factor for PLD activation3. Ras interacts with4–6 and activates Ral–GDS13, 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. More... »

PAGES

409-412

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/378409a0

DOI

http://dx.doi.org/10.1038/378409a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1026207451

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7477381


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