Do CrlA and Gα5 Function in the Same Pathway?

Hannah Villines, Jeffrey Hadwiger

Abstract


G proteins have been an important factor amongst signal transduction pathways in Dictyostelium and most other eukaryotes. These proteins are known to connect receptors to other signaling components such as MAP kinases, cAMP, and phosphodiesterases. Even though we have identified many G proteins, we still need to determine what receptors are connected to these proteins, especially to the highly conserved Gα5 protein. As for the greater than 60 receptors in Dictyostelium, several have been characterized such as crlA, fAR1 and the 4 cARs. Among those receptors, there is little to no information on what external stimuli turn on the crlA receptors and whether or not this receptor has a connection with the Gα5 protein. To answer whether these two signaling proteins interact with each other, we tested to see if they both function in the same pathway. We tested this theory by determining whether phenotypes associated with the overexpression of one protein require the function of the other protein. Our results indicate that the overexpression phenotypes do not require the function of the other protein suggesting that these proteins most likely function in separate signaling pathways.

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References


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