This entry represents a group of Arf-like small GTP-binding proteins, including ARL2/3 from animals, Cin4 from budding yeasts, Alp41 from fission yeasts and ARL2 from Arabidopsis. They are involved in microtubule-dependent processes []. Despite the structural similarity of ARL2 and ARL3, they have different biochemical properties and biological functions []. ARL2 plays roles in both the regulation of tubulin folding and microtubule destruction. It is also essential to a number of mitochondrial functions, including mitochondrial morphology, motility, and maintenance of ATP levels []. ARL3 is required for normal cytokinesis and cilia signaling []. Alp41 is essential for the cofactor-dependent biogenesis of microtubules [].
This domain superfamily is found in ADP-ribosylation factor-like 2 (ARF2) binding protein, also known as BART. BART binds specifically to ARF2.GTP with a high affinity. However, it does not bind to ARF2.GDP. It is thought that this specific interaction is due to BART being the first identified ARF2-specific effector. The function is not completely characterised []. BART is predominantly cytosolic but can also be found to be associated with mitochondria. BART is also involved in binding to the adenine nucleotide transporter ANT1 [].The interactions between ARL2 and BART involve a conserved N-terminal LLxIL motif of ARL2 []. This domain is also found in CFAP36/CCDC104, a protein renamed as BARTL1. The BART-like domain of CCDC104/BARTL1 recognizes an LLxILxxL motif at the N-terminal amphipathic helix of ARL3 [].
This domain is found in ADP-ribosylation factor-like 2 (ARF2) binding protein, also known as BART. BART binds specifically to ARF2.GTP with a high affinity. However, it does not bind to ARF2.GDP. It is thought that this specific interaction is due to BART being the first identified ARF2-specific effector. The function is not completely characterised []. BART is predominantly cytosolic but can also be found to be associated with mitochondria. BART is also involved in binding to the adenine nucleotide transporter ANT1 [].The interactions between ARL2 and BART involve a conserved N-terminal LLxIL motif of ARL2 []. This domain is also found in CFAP36/CCDC104, a protein renamed as BARTL1. The BART-like domain of CCDC104/BARTL1 recognizes an LLxILxxL motif at the N-terminal amphipathic helix of ARL3 [].
