PRA1 Gene Family in Arabidopsis

• Published in: Plant physiology (Bethesda) 2008-08, Vol.147 (4), p.1735-1749
• Main Authors: Alvim Kamei, Claire Lessa, Boruc, Joanna, Vandepoele, Klaas, Van den Daele, Hilde, Maes, Sara, Russinova, Eugenia, Inzé, Dirk, De Veylder, Lieven
• Format: Article
• Language: English
• Subjects: Amino Acid Motifs; Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis - ultrastructure; Arabidopsis Proteins - analysis; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Arabidopsis thaliana; Biological Transport - genetics; Dimerization; Endoplasmic Reticulum - metabolism; Endosomes - metabolism; Family members; Focus Issue on Membrane Trafficking; Genes; Glucuronidase - analysis; Golgi apparatus; Golgi Apparatus - metabolism; Guard cells; Multigene Family; Phylogeny; Plant cells; Plants; Protein Structure, Tertiary; Proteins; rab GTP-Binding Proteins - metabolism; Recombinant Fusion Proteins - analysis; Seedlings; Sequence Analysis, Protein; Transport Vesicles - metabolism; Trichomes; Vacuoles - metabolism; Vesicular Transport Proteins - analysis; Vesicular Transport Proteins - genetics; Vesicular Transport Proteins - metabolism; Yeasts
• ISSN: 0032-0889; 1532-2548; 1532-2548
• DOI: 10.1104/pp.108.122226

Prenylated Rab acceptor 1 (PRA1) domain proteins are small transmembrane proteins that regulate vesicle trafficking as receptors of Rab GTPases and the vacuolar soluble N-ethylmaleimide-sensitive factor attachment receptor protein VAMP2. However, little is known about PRA1 family members in plants. Sequence analysis revealed that higher plants, compared with animals and primitive plants, possess an expanded family of PRA1 domain-containing proteins. The Arabidopsis (Arabidopsis thaliana) PRA1 (AtPRA1) proteins were found to homodimerize and heterodimerize in a manner corresponding to their phylogenetic distribution. Different AtPRA1 family members displayed distinct expression patterns, with a preference for vascular cells and expanding or developing tissues. AtPRA1 genes were significantly coexpressed with Rab GTPases and genes encoding vesicle transport proteins, suggesting an involvement in the vesicle trafficking process similar to that of their animal counterparts. Correspondingly, AtPRA1 proteins were localized in the endoplasmic reticulum, Golgi apparatus, and endosomes/prevacuolar compartments, hinting at a function in both secretory and endocytic intracellular trafficking pathways. Taken together, our data reveal a high functional diversity of AtPRA1 proteins, probably dealing with the various demands of the complex trafficking system.