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A more recent version of this article appeared on January 1, 2004
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Submitted on July 1, 2003
Revised on October 2, 2003
Accepted on October 3, 2003
1 Cell and Molecular Biology, Division of Biomedical Sciences, Faculty of Medicine, Imperial College London, London SW7 2AZ, UK
2 Sir William Dunn School of Pathology, University of Oxford, OX1 3RE, UK
* Corresponding author. E-mail address: m.seabra{at}imperial.ac.uk.
Vesicular transport is a complex multi-step process regulated by distinct Rab GTPases. Here we show for the first time that an EGFP-Rab fusion protein is fully functional in a mammalian organism. We constructed a PAC-based transgenic mouse, which expresses EGFP-Rab27a under the control of endogenous Rab27a promoter. The EGFP-Rab27a transgene was fully functional and rescued the two major defects of the ashen Rab27a knock-out mouse. We achieved cell-specific expression of EGFP-Rab27a, which faithfully followed the pattern of expression of endogenous Rab27a. We found that Rab27a is expressed in an exceptionally broad range of specialized secretory cells, including exocrine (particularly in mucin- and zymogen-secreting cells), endocrine, ovarian and hematopoietic cells, most of which undergo regulated exocytosis. We suggest that Rab27a acts in concert with Rab3 proteins in most regulated-secretory events. The present strategy represents one way in which the complex pattern of expression and function of proteins involved in specialized cell types may be unraveled.
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