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A more recent version of this article appeared on January 1, 2003
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Submitted on June 13, 2002
Revised on September 4, 2002
Accepted on September 4, 2002
1 Institut de Biologie, EP CNRS 525, Institut Pasteur de Lille, 1 rue Professeur Calmette, BP447, 59021 Lille Cedex, France (present address: Department of Cell Biology and Neuroscience (A1), Osaka University Graduate School of Medicine, Osaka, Japan)
2 Institut de Biologie, EP CNRS 525, Institut Pasteur de Lille, 1 rue Professeur Calmette, BP447, 59021 Lille Cedex, France
3 Department of Cell Biology and Neuroscience (A1), Osaka University Graduate School of Medicine, Osaka, Japan
4 Institut de Biologie, EP CNRS 525, Institut Pasteur de Lille, 1 rue Professeur Calmette, BP447, 59021 Lille Cedex, France (present address: Technische Universitat Dresden, c/o Max Planck-Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany)
* Corresponding author. E-mail address: hoflack{at}mpi-cbg.de.
We have stably expressed in HeLa cells a chimeric protein made of the Green
Fluorescent Protein (GFP) fused to the transmembrane and cytoplasmic domains of the mannose 6-phosphate/insulin like growth factor II receptor in order to stud its dynamics in living cells. At steady state, the bulk of this chimeric protein (GFP-CI-MPR) localized to the trans-Golgi network (TGN) but significant amounts are also detected in peripheral, tubulo-vesicular structures and early endosomes as well as at the plasma membrane. Time-lapse video-microscopy shows that the GFP-CI-MPR is ubiquitously detected in tubular elements that detach from the TGN, move towards the cell periphery, sometimes breaking into smaller tubular fragments. The formation of the TGN-derived tubules is temperature-dependent, requires the presence of intact microtubule and actin networks, and is regulated by the ARF-1 GTPase. The TGN-derived tubules fuse with peripheral, tubulo-vesicular structures also containing the GFP-CI-MPR. These structures are highly dynamic, fusing with each other as well as with early endosomes. Time-lapse video-microscopy performed on HeLa cells co-expressing the CFP-CI-MPR and the AP-1 complex whose 
-subunit was fused to YFP shows that AP-1 is present not only on the TGN and peripheral CFP-CI-MPR containing structures but also on TGN-derived tubules containing the CFP-CI-MPR. The data support the notion that tubular elements can mediate MPR transport from the TGN to a peripheral, tubulo-vesicular network dynamically connected with the endocytic pathway and that the AP-1 coat may facilitate MPR sorting in the TGN and endosomes.
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