Abstract
The molecular mechanisms by which dense core vesicles (DCVs) translocate, tether, dock and prime are poorly understood. In this study, Caenorhabditis elegans was used as a model organism to study the function of Rab proteins and their effectors in DCV exocytosis. RAB-27/AEX-6, but not RAB-3, was found to be required for peptide release from neurons. By analyzing the movement of DCVs approaching the plasma membrane using total internal reflection fluorescence microscopy, we demonstrated that RAB-27/AEX-6 is involved in the tethering of DCVs and that its effector rabphilin/RBF-1 is required for the initial tethering and subsequent stabilization by docking.
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Feng, W., Liang, T., Yu, J. et al. RAB-27 and its effector RBF-1 regulate the tethering and docking steps of DCV exocytosis in C. elegans. Sci. China Life Sci. 55, 228–235 (2012). https://doi.org/10.1007/s11427-012-4296-9
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DOI: https://doi.org/10.1007/s11427-012-4296-9