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Rab-interacting lysosomal protein (RILP) is a cytosolic adaptor protein of approximately 45 kDa that specifically interacts with the GTP-bound forms of the small GTPases Rab7 and Rab34[2][3][4][1]. RILP contains two coiled-coil regions typical of myosin-like proteins and is critical for late endosomal and lysosomal organization and trafficking. Overexpression of RILP causes perinuclear aggregation and changes in lysosomal morphology, while loss or truncation of RILP can disperse lysosomes and inhibit endocytic degradation. These activities result from RILP’s function as a downstream Rab7 effector, acting to coordinate vesicular movement and positioning through Rab-dependent recruitment to late endosomal/lysosomal membranes[2][3][1]. The molecular region required for Rab7 binding and functional activity is mapped to a unique C-terminal stretch; dimerization of RILP is essential for its Rab7 interaction and cellular localization[4]. While RILP is essential for vesicle dynamics, it is not recognized as a direct drug target, and no approved drugs or clinical biomarkers are associated with it[2][3][1][4].
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