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Published online
doi:10.1083/jcb.200612068
The Journal of Cell Biology, Vol. 177, No. 6, 1133-1143
The Rockefeller University Press, 0021-9525 $30.00
© Fuchs et al.
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Article

Specific Rab GTPase-activating proteins define the Shiga toxin and epidermal growth factor uptake pathways



Evelyn Fuchs1, Alexander K. Haas1, Robert A. Spooner2, Shin-ichiro Yoshimura1,3, J. Michael Lord2, and Francis A. Barr1,3

1 Department of Cell Biology, Max Planck Institute of Biochemistry, Martinsried 82152, Germany
2 Department of Biological Sciences, Molecular Cell Biology Group, University of Warwick, Coventry CV4 7AL, England, UK
3 University of Liverpool Cancer Studies Centre, Liverpool L3 9TA, England, UK

Correspondence to Francis A. Barr: f.a.barr{at}liverpool.ac.uk

Rab family guanosine triphosphatases (GTPases) together with their regulators define specific pathways of membrane traffic within eukaryotic cells. In this study, we have investigated which Rab GTPase-activating proteins (GAPs) can interfere with the trafficking of Shiga toxin from the cell surface to the Golgi apparatus and studied transport of the epidermal growth factor (EGF) from the cell surface to endosomes. This screen identifies 6 (EVI5, RN-tre/USP6NL, TBC1D10A–C, and TBC1D17) of 39 predicted human Rab GAPs as specific regulators of Shiga toxin but not EGF uptake. We show that Rab43 is the target of RN-tre and is required for Shiga toxin uptake. In contrast, RabGAP-5, a Rab5 GAP, was unique among the GAPs tested and reduced the uptake of EGF but not Shiga toxin. These results suggest that Shiga toxin trafficking to the Golgi is a multistep process controlled by several Rab GAPs and their target Rabs and that this process is discrete from ligand-induced EGF receptor trafficking.

Abbreviations used in this paper: GAP, GTPase-activating protein; STxB, Shiga toxin B subunit.


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