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Ras-related protein Rab-37 (RAB37) is a small GTPase belonging to the Rab family within the RAS oncogene superfamily. It regulates intracellular vesicle trafficking and exocytosis, playing a critical role in processes such as autophagy, secretion of anti-tumor factors (like TIMP1 and thrombospondin-1), and insulin granule release. In various cancers, RAB37 functions predominantly as a metastasis suppressor by mediating the exocytosis of cargo proteins that inhibit migration, invasion, and neovasculature formation, thus modulating the tumor microenvironment. Its expression is often reduced via hypermethylation in tumors, leading to increased metastasis and poorer prognosis. In specific contexts, such as tumor-associated macrophages, RAB37 may exert protumorigenic effects by mediating secretion of immunomodulatory cytokines. RAB37 is not currently a direct drug target, but its pathway is subject to regulation by posttranslational modifications, including phosphorylation by protein kinase C alpha, which abrogates its tumor suppressive exocytic functions[1][2][3][4][5][7].
Not directly drug-modulated; protein activity regulated by post-translational modifications such as phosphorylation (notably by PKCα), methylation, and epigenetic mechanisms[1][2][3][4]
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