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MBC in Press, published online ahead of print June 27, 2003
Mol. Biol. Cell 10.1091/mbc.E03-03-0147

A more recent version of this article appeared on October 1, 2003
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Submitted on March 14, 2003
Revised on June 2, 2003
Accepted on June 4, 2003

Cross-talk between Tetanus neurotoxin-Insensitive Vesicle-Associated Membrane Protein-mediated transport and L1-mediated adhesion

Philipp Alberts1, Rachel Rudge1, Ina Hinners2, Aude Muzerelle3, Sonia Martinez-Arca1, Theano Irinopoulou1, Véronique Marthiens4, Sharon Tooze2, Fritz Rathjen5, Patricia Gaspar3, and Thierry Galli1*

1 Membrane Traffic and Neuronal Plasticity, INSERM U536, F-75005 Paris, France
2 Secretory Pathways Laboratory, Cancer Research UK, London Research Institute, London, UK
3 INSERM U106, Hôpital Salpêtrière, F-75651, Paris cedex 13, France
4 INSERM U440, F-75005 Paris, France
5 Max-Delbrueck-Centrum fuer Molekulare Medizin, D-13092 Berlin, Germany

* Corresponding author. E-mail address: mailto:galli{at}ifm.inserm.fr.

The membrane trafficking pathway mediated by Tetanus neurotoxin-Insensitive Vesicle Associated Membrane Protein (TI-VAMP) in neurons is still unknown. We show here that TI-VAMP expression is necessary for neurite outgrowth in PC12 cells and hippocampal neurons in culture. TI-VAMP interacts with plasma membrane and endosomal target SNAREs suggesting that TI-VAMP mediates a recycling pathway. L1, a cell-cell adhesion molecule involved in axonal outgrowth, colocalized with TI-VAMP in the developing brain, neurons in culture, and PC12 cells. Plasma membrane L1 was internalized into the TI-VAMP-containing compartment. Silencing of TI-VAMP resulted in reduced expression of L1 at the plasma membrane. Finally, using the extracellular domain of L1 and N-Cadherin immobilized on beads, we found that the silencing of TI-VAMP led to impaired L1- but not N-Cadherin-mediated adhesion. Futhermore, TI-VAMP- but not Synaptobrevin 2-containing vesicles accumulated at the site of the L1 bead-cell junction. We conclude that TI-VAMP mediates the intracellular transport of L1and that L1-mediated adhesion controls this membrane trafficking, thereby suggesting an important cross-talk between membrane trafficking and cell-cell adhesion.




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