Title : Role of phospholipase D1 in the regulation of mTOR activity by lysophosphatidic acid.

Pub. Date : 2004 Feb

PMID : 14769825






3 Functional Relationships(s)
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Compound Name
Protein Name
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1 LPA caused much less phosphorylation of Akt and this was dependent on PLD activity. lysophosphatidic acid AKT serine/threonine kinase 1 Homo sapiens
2 Toxin B, which inactivates Rho GTPases, markedly impaired PLD1 activation and phosphorylation of Akt, p70(S6K), and 4E-BP1 induced by LPA but had a minimal or no effect on the actions of PDGF. lysophosphatidic acid AKT serine/threonine kinase 1 Homo sapiens
3 These results support the hypothesis that LPA activates protein translation through the action of PLD1-generated PA on mTOR and the PI3K/Akt pathway whereas PDGF acts through P13K/Akt independent of PLD1. lysophosphatidic acid AKT serine/threonine kinase 1 Homo sapiens