ARF1 is a small GTPase that alternates between an inactive GDP-bound form and an active GTP-bound form. This cycling between forms is essential for its function in cellular processes. In its GTP-bound form, ARF1 triggers the recruitment of coatomer proteins to the Golgi membrane, facilitating vesicle budding and uncoating within the Golgi complex . The hydrolysis of ARF1-bound GTP, mediated by ARFGAPs proteins, is required for the dissociation of coat proteins from Golgi membranes and vesicles .
ARF1 is involved in several key cellular processes:
Recombinant human ARF1 is typically produced in Escherichia coli (E. coli) and consists of amino acids 2-181. The calculated molecular weight for this recombinant protein is approximately 55.7 kDa . Recombinant ARF1 is used in various research applications to study its function and role in cellular processes.
Structural studies of ARF1 have revealed unique conformational changes that distinguish it from other small GTP-binding proteins. These changes involve the switch 1 and switch 2 regions, which bind tightly to the gamma-phosphate of GTP but poorly or not at all to the GDP nucleotide . In the GTP-bound form, the interswitch undergoes a two-residue register shift that pulls switch 1 and switch 2 up, restoring an active conformation that can bind GTP .