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Ras-related protein Rab-5B (RAB5B) is a member of the Rab family of small GTPases, classified within the Ras superfamily, and functions as a molecular switch regulating endocytic vesicle trafficking in eukaryotic cells[2][3][4]. RAB5B is specifically involved in the formation, transport, binding, and fusion of vesicles with early endosomes, thus playing essential roles in endocytosis, early endosome fusion, and recycling of cell surface molecules[2][3][4]. In lung cells, RAB5B has a specialized, noncanonical role in the processing and trafficking of surfactant proteins SP-B and SP-C, with pathogenic variants causing surfactant dysfunction disorders and interstitial lung disease[1]. In cancer biology, RAB5B regulates cell adhesion, migration, and signaling, with altered expression linked to metastasis, immune evasion, and drug resistance; it holds potential as both a biomarker and therapeutic target, though no direct inhibitors are currently used clinically[3]. RAB5B’s essential functions in membrane trafficking, signal transduction, and autophagy make it a central regulator of cellular homeostasis and disease[3][4].
Modulation/targeting of small GTPase function to alter vesicle trafficking or endocytosis (hypothetical; no approved drugs known targeting RAB5B directly[3])
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