Affiliation:
1. Institute of Molecular Cell Biology, Medical Faculty, Friedrich-Schiller-University, Drackendorfer Strasse 1, 07747 Jena, Germany
Abstract
The topology of the signalling pathway linking the G-protein-coupled receptor agonist lysophosphatidic acid (LPA) to extracellular-signal-regulated kinase activation remains undeciphered. In the present study, we report that analysis of LPA signals at the level of Ras-GTP formation and Ras nucleotide exchange discriminates true mediatory signals from permissive activities that do not participate in signal relay. Hence, whereas pertussis toxin (PTX) treatment impairs stimulation of nucleotide exchange, epidermal growth factor receptor (EGFR) inhibition does not compromise LPA-induced acceleration of nucleotide exchange, but instead attenuates basal nucleotide turnover on Ras. Our data indicate that LPA activation of Ras proceeds via PTX-sensitive Gi/o-proteins and requires a permissive input from basal EGFR activity.
Subject
Cell Biology,Molecular Biology,Biochemistry
Cited by
26 articles.
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