Abstract 2574 A pseudoGTPase mediates chaperone-substrate interaction in membrane trafficking complex assembly

GTPases are known to regulate various cellular processes, from cell signaling to membrane trafficking, through conformational changes triggered by GTP or GDP binding. Recently, pseudoGTPases, the catalytically inactive counterparts of GTPases, have been identified across species from bacteria to human, although their functions and mechanisms remain largely unexplored. In this study, we demonstrate that the N-terminal region of the assembly chaperone AAGAB, previously annotated as a GTPase domain, is actually a pseudoGTPase domain (psGD).