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Secretory carrier-associated membrane protein 3 (SCAMP3) is an integral membrane protein belonging to the SCAMP family, which is highly conserved and expressed in various secretory and endocytic carriers involved in membrane trafficking events. SCAMP3 is implicated in post-Golgi recycling pathways, where it regulates the trafficking and degradation of cell surface receptors, particularly the epidermal growth factor receptor (EGFR). It participates in the modulation of cellular signaling pathways such as AKT, ERK, and STAT3, and its overexpression has been associated with tumor proliferation, migration, and invasion, especially in triple-negative breast cancer. SCAMP3 is characterized structurally by conserved NPF repeats, proline-rich motifs, and four transmembrane domains, and it is often found to be tyrosine-phosphorylated. It is considered a promising molecular target in cancer due to its role in tumor progression and receptor signaling regulation[1][2][3][5][7].
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