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- W2156875265 abstract "ABSTRACT Ral is a ubiquitously expressed Ras-like small GTPase which is abundantly present in human platelets. The biological function of Ral and the signaling pathway in which Ral is involved are largely unknown. Here we describe a novel method to measure Ral activation utilizing the Ral binding domain of the putative Ral effector RLIP76 as an activation-specific probe. With this assay we investigated the signaling pathway that leads to Ral activation in human platelets. We found that Ral is rapidly activated after stimulation with various platelet agonists, including α-thrombin. In contrast, the platelet antagonist prostaglandin I 2 inhibited α-thrombin-induced Ral activation. Activation of Ral by α-thrombin could be inhibited by depletion of intracellular Ca 2+ , whereas the induction of intracellular Ca 2+ resulted in the activation of Ral. Our results show that Ral can be activated by extracellular stimuli. Furthermore, we show that increased levels of intracellular Ca 2+ are sufficient for Ral activation in platelets. This activation mechanism correlates with the activation mechanism of the small GTPase Rap1, a putative upstream regulator of Ral guanine nucleotide exchange factors." @default.
- W2156875265 created "2016-06-24" @default.
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- W2156875265 date "1998-05-01" @default.
- W2156875265 modified "2023-10-14" @default.
- W2156875265 title "Activation of the Small GTPase Ral in Platelets" @default.
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- W2156875265 doi "https://doi.org/10.1128/mcb.18.5.2486" @default.
- W2156875265 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/110628" @default.
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