Disease relevance of ARF3

• We describe a reverse two-hybrid method that generates loss-of-interaction mutations of the catalytic subunit of the Escherichia coli heat-labile toxin (LTA1) with decreased binding to the active (GTP-bound) form of human ARF3, its protein cofactor [1].

High impact information on ARF3

• A 200-kDa guanine nucleotide-exchange protein (p200 or GEP) for ADP-ribosylation factors 1 and 3 (ARF1 and ARF3) that was inhibited by brefeldin A (BFA) was purified earlier from cytosol of bovine brain cortex [2].
• Role for Arf3p in development of polarity, but not endocytosis, in Saccharomyces cerevisiae [3].
• The nucleotide-binding, N-terminal region, and N-terminal myristate of Arf3p are important for its proper localization [3].
• Yeast Arf3p, which is most similar to mammalian ARF6, is not essential for cell viability and not required for endoplasmic reticulum-to-Golgi protein transport [3].
• Both haploid and homologous diploid arf3 mutants exhibit a random budding defect, and the overexpression of the GTP-bound form Arf3p(Q71L) or GDP-binding defective Arf3p(T31N) mutant interfered with budding-site selection [3].

Biological context of ARF3

• A family of three structurally related proteins were cloned from human cDNA libraries by their ability to interact preferentially with the activated form of human ADP-ribosylation factor 3 (ARF3) in two-hybrid assays [4].

Anatomical context of ARF3

• Taken together, our data provide further evidence for the role of Lsb5p in membrane-trafficking events at the plasma membrane and also demonstrate for the first time an interaction of Arf3 with the endocytic machinery in yeast [5].

Other interactions of ARF3

• Our findings demonstrate that Afi1p functions as an Arf3p polarization-specific adapter and participates in development of polarity [6].

References