PH and SEC7 domain-containing protein 4 (PSD4)

PH and SEC7 domain-containing protein 4 (PSD4) is a member of the guanine nucleotide exchange factor (GEF) family that specifically activates small GTPases in the ARF family, notably ARF6 and ARL14/ARF7[1]. The protein contains pleckstrin homology (PH) and Sec7 domains; the PH domain enables phospholipid binding, and the Sec7 domain confers GEF activity. Through activation of ARF6 and ARL14, PSD4 regulates signal transduction related to actin cytoskeleton remodeling and membrane recycling, especially in immune cells such as dendritic cells, by controlling movement of MHC class II vesicles. PSD4 is located primarily at ruffle membranes in cells, consistent with roles in dynamic membrane processes[1][3]. No approved drugs target this molecule, and no direct disease associations are high-confidence, although its molecular function suggests possible involvement in processes critical to immunity and cell trafficking.

Other names

PSD4Pleckstrin and Sec7 domain containing 4EFA6BExchange factor for ARF6 BTICADP-ribosylation factor guanine nucleotide-exchange factor 6BTelomeric of interleukin-1 cluster proteinSEC7 homolog

Not applicable (no drugs established yet). Putative mechanism for a hypothetical drug would be inhibition or modulation of GEF activity for ARF6/ARF7, affecting signal transduction and membrane trafficking