The 4-aminobutyrate type A receptor-associated protein (GABARAP) is a versatile
adaptor protein that plays an important role in intracellular vesicle
trafficking, particularly in neuronal cells. We have investigated the structural
determinants underlying the interaction of GABARAP with calreticulin using
spectroscopic and crystallographic techniques. Specifically, we present the
crystal structure of GABARAP in complex with its major binding epitope on the
chaperone. Molecular modeling of a complex containing full-length calreticulin
suggests a novel mode of substrate interaction, which may have functional
implications for the calreticulin/calnexin family in general.