Originally published as Genetics Published Articles Ahead of Print on April 3, 2007.

Genetics, Vol. 176, 1307-1322, June 2007, Copyright © 2007
doi:10.1534/genetics.106.066761

Thirty-One Flavors of Drosophila Rab Proteins

* Departments of Developmental Biology, Genetics, and Bioengineering, Howard Hughes Medical Institute, Stanford University School of Medicine, Stanford, California 94305, {dagger} Howard Hughes Medical Institute, Department of Molecular and Human Genetics, Stanford University School of Medicine, Stanford, California 94305, § Program in Developmental Biology, Baylor College of Medicine, Houston, Texas 77030, ** Department of Genome Biology, Lawrence Berkeley National Laboratory, Berkeley, California 94720-3200 and {ddagger} Department of Physiology Green Center Division for Systems Biology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9040

1 Corresponding author: Departments of Developmental Biology, Genetics, and Bioengineering, Howard Hughes Medical Institute, Clark Center, West Wing W252, 318 Campus Dr., Stanford University School of Medicine, Stanford, CA 94305-5439.
E-mail: mscott{at}stanford.edu

Rab proteins are small GTPases that play important roles in transport of vesicle cargo and recruitment, association of motor and other proteins with vesicles, and docking and fusion of vesicles at defined locations. In vertebrates, >75 Rab genes have been identified, some of which have been intensively studied for their roles in endosome and synaptic vesicle trafficking. Recent studies of the functions of certain Rab proteins have revealed specific roles in mediating developmental signal transduction. We have begun a systematic genetic study of the 33 Rab genes in Drosophila. Most of the fly proteins are clearly related to specific vertebrate proteins. We report here the creation of a set of transgenic fly lines that allow spatially and temporally regulated expression of Drosophila Rab proteins. We generated fluorescent protein-tagged wild-type, dominant-negative, and constitutively active forms of 31 Drosophila Rab proteins. We describe Drosophila Rab expression patterns during embryogenesis, the subcellular localization of some Rab proteins, and comparisons of the localization of wild-type, dominant-negative, and constitutively active forms of selected Rab proteins. The high evolutionary conservation and low redundancy of Drosophila Rab proteins make these transgenic lines a useful tool kit for investigating Rab functions in vivo.


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