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Ras-related protein Rab-40C (RAB40C) is a small GTPase enzyme, member of the Rab subfamily of the Ras superfamily of monomeric G proteins, which are key regulators of vesicular trafficking in eukaryotic cells. RAB40C acts as a substrate-recognition component of the ECS(RAB40C) E3 ubiquitin ligase complex, directing ubiquitination and degradation of specific target proteins. It modulates cell migration by inhibiting protein phosphatase 6 complex activity and affecting focal adhesion assembly, and negatively regulates the accumulation of lipid droplets. RAB40C is expressed in diverse tissues and is upregulated in multiple human cancers, with a significant role in tumor progression, immune regulation, and as a prognostic biomarker. Elevated expression is associated with altered immune cell infiltration, including CD4 T cells, macrophages, and regulatory T cells, and correlates with poor prognosis in several cancer types, highlighting its potential as a therapeutic target and biomarker in oncology.
No drugs directly targeting RAB40C are reported; mechanisms for targeting would likely include inhibition of its GTPase activity or interference with its function in ubiquitin ligase complexes
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