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Imaging the post-fusion release and capture of a vesicle membrane protein.
- Source :
-
Nature communications [Nat Commun] 2012; Vol. 3, pp. 1154. - Publication Year :
- 2012
-
Abstract
- The molecular mechanism responsible for capturing, sorting and retrieving vesicle membrane proteins following triggered exocytosis is not understood. Here we image the post-fusion release and then capture of a vesicle membrane protein, the vesicular acetylcholine transporter, from single vesicles in living neuroendocrine cells. We combine these measurements with super-resolution interferometric photo-activation localization microscopy and electron microscopy, and modelling to map the nanometer-scale topography and architecture of the structures responsible for the transporter's capture following exocytosis. We show that after exocytosis, the transporter rapidly diffuses into the plasma membrane, but most travels only a short distance before it is locally captured over a dense network of membrane-resident clathrin-coated structures. We propose that the extreme density of these structures acts as a short-range diffusion trap. They quickly sequester diffusing vesicle material and limit its spread across the membrane. This system could provide a means for clathrin-mediated endocytosis to quickly recycle vesicle proteins in highly excitable cells.
- Subjects :
- Animals
Cell Membrane physiology
Cell Membrane ultrastructure
Clathrin physiology
Clathrin ultrastructure
Endocytosis physiology
Exocytosis physiology
Membrane Proteins ultrastructure
Microscopy, Electron
Microscopy, Interference methods
PC12 Cells physiology
Rats
Synaptic Vesicles physiology
Synaptic Vesicles ultrastructure
Vesicular Acetylcholine Transport Proteins ultrastructure
Membrane Fusion physiology
Membrane Proteins physiology
Vesicular Acetylcholine Transport Proteins physiology
Subjects
Details
- Language :
- English
- ISSN :
- 2041-1723
- Volume :
- 3
- Database :
- MEDLINE
- Journal :
- Nature communications
- Publication Type :
- Academic Journal
- Accession number :
- 23093191
- Full Text :
- https://doi.org/10.1038/ncomms2158