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Ras-related protein Rab-9A (RAB9A) is a member of the Rab family of small GTPases, molecular switches that regulate intracellular vesicle trafficking. RAB9A is primarily involved in the transport of proteins between late endosomes and the trans-Golgi network, particularly recycling mannose 6-phosphate receptors required for lysosomal enzyme delivery[4][1]. It binds GTP and GDP and cycles between active and inactive states to control the budding, motility, docking, and fusion of transport vesicles[3]. In oligodendroglial cells, RAB9A has been shown to negatively regulate cellular morphological changes related to differentiation and myelination, and its knockdown ameliorates cellular stress relevant to disorders such as hypomyelinating leukodystrophy[2]. RAB9A is broadly expressed and acts as a key coordinator of protein sorting, endosome dynamics, and autophagic processes in various cell types[4][2]. Dysfunctional or dysregulated RAB9A activity can contribute to neurodevelopmental and neurodegenerative diseases, and it is being studied as a potential therapeutic target for modulation of vesicular trafficking and cellular stress responses[2].
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