Cytohesin-3 (CYTH3)

Cytohesin-3 (CYTH3) is a guanine-nucleotide exchange factor (GEF) belonging to the cytohesin/PSCD protein family, characterized by an N-terminal coiled-coil motif, a central Sec7 GEF domain, and a C-terminal pleckstrin homology (PH) domain. It promotes guanine-nucleotide exchange on ARF GTPases (particularly ARF1 and ARF6), facilitating their activation by exchanging GDP for GTP. Cytohesin-3 plays a role in regulating Golgi structure and function, mediating protein sorting, membrane trafficking, and epithelial cell polarity. It localizes to multiple subcellular compartments, including the cytosol, plasma membrane, Golgi membrane, nucleoplasm, and cell junctions. Genetic and functional associations link CYTH3 to several biologically and clinically relevant processes, although no specific pharmacological modulators or approved interacting drugs are documented to date.

Other names

Cytohesin 3ARNO3PSCD3GRP1Protein ARNO3General receptor of phosphoinositides 1ARF nucleotide-binding site opener 3PH, SEC7 and coiled-coil domain-containing protein 3Pleckstrin homology Sec7 and coiled-coil domains 3Cytohesin-3CYTH3

If targeted, drugs would be expected to inhibit guanine-nucleotide exchange activity on ARF1/ARF6, affecting vesicle trafficking and ARF signaling. This is an inference based on the established biological activity of the protein.