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Vacuolar protein sorting-associated protein 37C (VPS37C) is a subunit of the ESCRT-I complex, essential for sorting ubiquitinated transmembrane proteins into the internal vesicles of multivesicular bodies[1][2][3][4][5]. VPS37C forms a ternary complex in mammalian cells with Tsg101 and VPS28 and interacts with Hrs and calcium-dependent adaptor proteins such as ALG-2, coordinating protein–protein interactions in response to calcium signaling[2][3][4]. VPS37C is recruited to aberrant endosomes and to the plasma membrane during the budding of enveloped viruses like HIV-1, where its fusion with HIV-1 Gag can bypass the canonical PTAP motif requirement for virion release[1][2][3]. Beyond its role in endosomal sorting and viral budding, VPS37C also regulates erythroid differentiation by stabilizing the EKLF transcription factor, promoting erythroid-specific gene expression[2]. While VPS37C is implicated in pathways exploited by certain viral infections, no established drug interactions, mechanisms of action, biomarkers, or safety concerns have been reported in current reference databases.
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