Cytohesin-2 (CYTH2)

Cytohesin-2 is an enzyme encoded by the *CYTH2* gene in humans. It acts as a guanine-nucleotide exchange factor (GEF) that activates ARF small GTPases—specifically ARF1, ARF3, and ARF6—by promoting exchange of GDP for GTP, regulating key processes in membrane trafficking and protein sorting[1][2][5]. Cytohesin-2 contains an N-terminal coiled-coil motif (for homodimerization), a central Sec7 domain (responsible for GEF activity), and a C-terminal pleckstrin homology (PH) domain (membrane association via lipid binding)[1][2]. CYTH2 is highly homologous to CYTH1, and member of the cytohesin family. It is implicated in the regulation of cell shape changes, actin cytoskeletal dynamics, and neurite outgrowth[3]. In disease, CYTH2 has been linked to neuroblastoma, Peutz-Jeghers syndrome, and is involved in processes relevant to cancer cell migration and inflammation[2][3]. It has protein-protein interactions with ARF1, ARF6, GRASP, CCDC120, and arrestin beta isoforms[1][3]. No approved drugs directly target CYTH2 at present.

Other names

ARNOCTS18CTS18.1PSCD2PSCD2LSEC7LSec7p-LSec7p-likeARF exchange factorARF nucleotide-binding site openerProtein ARNO

Drugs targeting this molecule (if developed) would likely inhibit its guanine-nucleotide exchange factor activity for ARF proteins, blocking activation of ARF GTPases and disrupting intracellular trafficking and signal transduction[5][2].