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  Imaging direct, dynamin-dependent recapture of fusing secretory granules on plasma membrane lawns from PC12 cells

Holroyd, P., Lang, T., Wenzel, D., De Camilli, P., & Jahn, R. (2002). Imaging direct, dynamin-dependent recapture of fusing secretory granules on plasma membrane lawns from PC12 cells. Proceedings of the National Academy of Sciences of the United States of America, 99(26), 16806-16811. Retrieved from http://www.pnas.org/content/99/26/16806.full.pdf+html.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F254-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-8175-F
Genre: Journal Article

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Holroyd, P.1, Author              
Lang, T.1, Author              
Wenzel, D.2, Author              
De Camilli, P., Author
Jahn, R.1, Author              
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1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              
2Facility for Electron Microscopy, MPI for biophysical chemistry, Max Planck Society, ou_578615              

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 Abstract: During exocytosis, secretory granules fuse with the plasma membrane and discharge their content into the extracellular space. The excicytosed membrane is then reinternalized in a coordinated fashion. A role of clathrin-coated vesicles in this process is well established, whereas the involvement of a direct retrieval mechanism (often called kiss and run) is still debated. Here we report that a significant population of docked secretory granules in the neuroendocrine cell line PC12 fuses with the plasma membrane, takes up fluid-phase markers, and is retrieved at the same position. Fusion allows for complete discharge of small molecules, whereas GFP-labeled neuropeptide Y (molecular mass approximate to35 kDa) is only partially released. Retrieved granules were preferentially associated with dynamin. Furthermore, recapture is inhibited by guanosine 5'-[gamma-thio]triphosphate and peptides known to block dynamin function. We conclude that secretory granules can be recaptured immediately after formation of an exocytotic opening by an endocytic reaction that is spatially and temporally coupled to soluble N-ethylmaleimide-sensitive factor attachment protein receptor(SNARE)-dependent fusion, but is not a reversal of the fusion reaction.

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Language(s): eng - English
 Dates: 2002-12-24
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 99 (26) Sequence Number: - Start / End Page: 16806 - 16811 Identifier: -