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  Reconstitution of calcium-mediated exocytosis of dense-core vesicles.

Kreutzberger, A. B., Kiessling, V., Liang, B., Seelheim, P., Jakhanwal, S., Jahn, R., et al. (2017). Reconstitution of calcium-mediated exocytosis of dense-core vesicles. Science Advances, 3(7): e1603208. doi:10.1126/sciadv.1603208.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-D147-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-D14A-4
Genre: Journal Article

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 Creators:
Kreutzberger, A.J. B., Author
Kiessling, V., Author
Liang, B., Author
Seelheim, P., Author
Jakhanwal, S.1, Author              
Jahn, R.1, Author              
Castle, J. D., Author
Tamm, L. K., Author
Affiliations:
1Department of Neurobiology, MPI for Biophysical Chemistry, Max Planck Society, ou_578595              

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 Abstract: Regulated exocytosis is a process by which neurotransmitters, hormones, and secretory proteins are released from the cell in response to elevated levels of calcium. In cells, secretory vesicles are targeted to the plasma membrane, where they dock, undergo priming, and then fuse with the plasma membrane in response to calcium. The specific roles of essential proteins and how calcium regulates progression through these sequential steps are currently incompletely resolved. We have used purified neuroendocrine dense-core vesicles and artificial membranes to reconstruct in vitro the serial events that mimic SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor)-dependent membrane docking and fusion during exocytosis. Calcium recruits these vesicles to the target membrane aided by the protein CAPS (calcium-dependent activator protein for secretion), whereas synaptotagmin catalyzes calcium-dependent fusion; both processes are dependent on phosphatidylinositol 4,5-bisphosphate. The soluble proteins Munc18 and complexin-1 are necessary to arrest vesicles in a docked state in the absence of calcium, whereas CAPS and/or Munc13 are involved in priming the system for an efficient fusion reaction.

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Language(s): eng - English
 Dates: 2017-07-19
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1126/sciadv.1603208
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Title: Science Advances
Source Genre: Journal
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Pages: 11 Volume / Issue: 3 (7) Sequence Number: e1603208 Start / End Page: - Identifier: -