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Cross talk between tetanus neurotoxin-insensitive vesicle-associated membrane protein-mediated transport and L1-mediated adhesion

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Item Type:Article
Title:Cross talk between tetanus neurotoxin-insensitive vesicle-associated membrane protein-mediated transport and L1-mediated adhesion
Creators Name:Alberts, P. and Rudge, R. and Hinners, I. and Muzerelle, A. and Martinez-Arca, S. and Irinopoulou, T. and Marthiens, V. and Tooze, S. and Rathjen, F. and Gaspar, P. and Galli, T.
Abstract:The membrane-trafficking pathway mediated by tetanus neurotoxin-insensitive vesicle-associated membrane protein (TI-VAMP) in neurons is still unknown. We show herein 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 soluble N-ethylmaleimide-sensitive factor attachment protein receptors, 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. Furthermore, 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 L1 and that L1-mediated adhesion controls this membrane trafficking, thereby suggesting an important cross talk between membrane trafficking and cell-cell adhesion.
Keywords:Biological Transport, Brain, Cadherins, Cell Compartmentation, Cell Membrane, Cultured Cells, Cytoplasmic Granules, Mammalian Embryo, Membrane Proteins, Video Microscopy, Neural Cell Adhesion Molecule L1, Neurites, Neurons, PC12 Cells, Protein Binding, Tertiary Protein Structure, R-SNARE Proteins, Small Interfering RNA, SNARE Proteins, Signal Transduction, Subcellular Fractions, Vesicular Transport Proteins, Animals, Mice, Rats
Source:Molecular Biology of the Cell
Publisher:American Society for Cell Biology
Page Range:4207-4220
Date:October 2003
Additional Information:Copyright (c) 2003 by The American Society for Cell Biology
Official Publication:https://doi.org/10.1091/mbc.E03-03-0147
PubMed:View item in PubMed

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