Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Published on June 26, 2008; 10.1104/pp.108.122226

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Received April 29, 2008
Accepted June 25, 2008

The PRA1 gene family in Arabidopsis

Claire Lessa Alvim Kamei , Joanna Boruc , Klaas Vandepoele , Hilde Van den Daele , Sara Maes , Eugenia Russinova , Dirk Inze , and Lieven De Veylder *

Instituto de Bioquimica Medica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil; Department of Plant Systems Biology, Flanders Institute for Biotechnology; Department of Molecular Genetics, Ghent University, B-9052 Gent, Belgium
Instituto de Bioquimica Medica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, RJ, Brazil; and Department of Plant Systems Biology, Flanders Institute for Biotechnology and Department of Molecular Genetics, Ghent University, B-9052 Gent, Belgium

* Corresponding author; email: lieven.deveylder{at}psb.ugent.be.

Prenylated Rab acceptor 1 (PRA1) domain proteins are small transmembrane proteins that regulate vesicle trafficking as receptors of Rab GTPases and the v-SNARE protein VAMP2. In plants, however, little is known about the PRA1 family members in plants. Sequence analysis revealed that higher plants, compared to animals and primitive plants, possess an expanded family of PRA1 domain-containing proteins. The Arabidopsis thaliana PRA1 (AtPRA1) proteins were found to homo- and heterodimerize in a manner corresponding to their phylogenetical distribution. Different AtPRA1 family members displayed distinct expression patterns, with a preference for vascular cells and expanding or developing tissues. AtPRA1 genes were significantly co-expressed 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.




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