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A more recent version of this article appeared on October 1, 2004
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Submitted on December 5, 2003
Revised on June 20, 2004
Accepted on July 8, 2004
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 138673, Singapore
Monitoring Editor: Vivek Malhotra
The precise cellular function of Arl1 and its effectors, the GRIP domain Golgins, is not resolved, despite our recent understanding that Arl1 regulates the membrane recruitment of these Golgins. In this report, we describe our functional study of Golgin-97. Using a STxB based in vitro transport assay, we demonstrated that Golgin-97 plays a role in transport from the endosome to the TGN. The recombinant GRIP domain of Golgin-97 as well as antibodies against Golgin-97 inhibited the transport of STxB in vitro. Membrane-associated Golgin-97, but not its cytosolic pool, was required in the in vitro transport assay. The kinetic characterization of inhibition by anti-Golgin-97 antibody in comparison to antisyntaxin 16 antibody established that Golgin-97 acts prior to syntaxin 16 in endosome to TGN transport. Knock-down of Golgin-97 or Arl1 by their respective siRNAs also significantly inhibited the transport of STxB to the Golgi in vivo. In siRNA treated cells with reduced levels of Arl1, internalized STxB was instead distributed peripherally. Microinjection of Golgin-97 antibody led to the fragmentation of Golgi apparatus and the arrested transport to the Golgi of internalized CTxB. We suggest that Golgin-97 may function as a tethering molecule in endosome to TGN retrograde traffic.
Corresponding author.
E-mail: mcbhwj{at}imcb.a-star.edu.sg
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