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A more recent version of this article appeared on January 1, 2005
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Submitted on March 29, 2004
Accepted on October 5, 2004
Cell Biology and Biophysics Programme, European Molecular Biology Laboratory, D-69117 Heidelberg, Germany
Monitoring Editor: Benjamin Glick
The small GTPase, rab6A but not the isoform, rab6A', has previously been identified as a regulator of the COPI-independent recycling route that carries Golgi-resident proteins and certain toxins from the Golgi to the ER. The isoform, rab6A', has been implicated in Golgi to endosomal recycling. Since rab6A but not A', binds rabkinesin6, this motor protein is proposed to mediate COPI-independent recycling. We show here that both rab6A and rab6A' GTP restricted mutants promote, with similar efficiency, a microtubule-dependent recycling of Golgi resident glycosylation enzymes upon overexpression. Moreover, we used siRNA mediated down-regulation of rab6A and A' expression and found that reduced levels of rab6 perturbs organization of the Golgi apparatus and delays Golgi to ER recycling. Rab6 directed Golgi to ER recycling appears to require functional dynactin, as overexpression of p50/dynamitin or a C-terminal fragment of BicD, both known to interact with dynactin inhibit recycling. We further present evidence that rab6 mediated recycling appears to be initiated from the TGN. Together, this suggests that a recycling pathway operates at the level of the trans Golgi linking directly to the ER. This pathway would be the preferred route for both toxins and resident Golgi proteins.
Present address: Department of Medical Biochemistry, Göteborg University, 413 90 Göteborg, Sweden.
Corresponding authors.
E-mail: pepperko{at}embl.de E-mail: tommy.nilsson{at}medkem.gu.se
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