JCVI: ADP-ribosylation Factor (ARF)-like 3, a New Member of the ARF Family of GTP-binding Proteins Cloned from Human and Rat Tissues
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Cavenagh, M. M., Breiner, M., Schurmann, A., Rosenwald, A. G., Terui, T., Zhang, C., Randazzo, P. A., Adams, M., Joost, H. G., Kahn, R. A.

ADP-ribosylation Factor (ARF)-like 3, a New Member of the ARF Family of GTP-binding Proteins Cloned from Human and Rat Tissues

J Biol Chem. 1994 Jul 22; 269(29): 18937-42.

PubMed Citation


The human and rat homologues of a new member of the ADP-ribosylation factor (ARF) family of 21-kDa GTP-binding proteins, termed Arl3, were identified as an expressed sequence tag (human) and as a product of polymerase chain reaction amplification using degenerate probes derived from conserved sequences in members of the ARF family (rat). Alignments of the full-length open reading frames of the human and rat homologues revealed the encoded proteins to be over 97% identical to each other and 43% identical to human ARF1. Northern blots of mRNA from seven human tissues and four rat tissues revealed the presence of a ubiquitous band of about 1 kilobase in length that hybridized with the corresponding Arl3 probes. A number of human tumor cell lines expressed Arl3, as determined by immunoblotting with an Arl-specific antibody, raised against a peptide derived from the human Arl3 sequence. The level of Arl3 expressed in these cell lines was on the order of 0.01% of total cell protein. Purified recombinant human Arl3 was shown to bind guanine nucleotides but lacks ARF activity and intrinsic or ARF GTPase-activating protein-stimulated GTPase activity. In contrast to ARF proteins, the Arl3 protein has reduced dependence on phospholipids and magnesium for guanine nucleotide exchange. Thus, Arl3 is a ubiquitously expressed GTP-binding protein in the ARF family with distinctive biochemical properties consistent with its having unique, but unknown, role(s) in cell physiology.