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SH3 domain-binding protein 5-like (SH3BP5L) is a cytoplasmic guanine nucleotide exchange factor (GEF) that selectively activates Rab11 family GTPases, stimulating GDP release to permit GTP binding and thus activation of signaling pathways involved in membrane recycling, exocytosis, and cell division. SH3BP5L localizes mainly to recycling endosomes in mammalian cells, and its activity is critical for Rab11-mediated endosomal sorting and vesicular transport. The protein is predicted to play a role in intracellular signal transduction and shares structural and functional similarities with SH3BP5, forming part of a unique Rab11 GEF family. Disease association is currently limited to a genetic link with Bardet-Biedl syndrome 2, with no established roles in cancer, neurodegeneration, or inflammation. No approved drugs, biomarkers, or therapeutic safety concerns have been identified for SH3BP5L at present[1][2][5][6].
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