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Ras-related protein Rab-1B (RAB1B) is a small GTPase of the Rab family, acting as a master regulator of vesicular transport between the endoplasmic reticulum (ER) and Golgi apparatus[1][4]. It alternates between an active GTP-bound state and inactive GDP-bound state, coordinating the recruitment of various effectors responsible for the formation, movement, tethering, and fusion of transport vesicles. RAB1B is essential for early secretory pathway function, normal Golgi structure, and participates in the initial events of autophagic vacuole formation[1][3]. Deficiencies or dysregulation are linked to disruptions in vesicle trafficking and rare Mendelian diseases, as well as pathogen exploitation during infection[1][5]. No approved drugs specifically target RAB1B, but it remains a potential, though challenging, target in pathways of interest for conditions that rely on secretory or trafficking processes.
Not established for drug targeting; mechanistically, Rab1b cycles between inactive GDP-bound and active GTP-bound forms to regulate vesicle targeting and fusion[1][3]
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