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Ral guanine nucleotide dissociation stimulator (RALGDS) is a ubiquitously expressed enzyme that functions as a guanine nucleotide exchange factor (GEF) for the small GTPases RalA and RalB, mediating the exchange of GDP for GTP to activate these proteins. RALGDS also serves as an effector for members of the Ras superfamily (including HRAS, KRAS, RRAS, and RAP1A), thus bridging Ras signaling to downstream cellular processes, notably in exocyst complex assembly and intracellular transport. It is critical in signal transduction pathways regulating cell growth, differentiation, and vesicle trafficking. Mutational studies have highlighted that specific residues within its Ras-interacting domain are essential for binding. Dysregulation of RALGDS or its signaling partners is implicated in cancer, underscoring its role as a therapeutic target. However, there are no known drugs directly targeting RALGDS as of the latest data.
Not applicable; there are currently no drugs directly targeting RALGDS described in the results.
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