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  Analysis of protein phosphorylation in nerve terminal reveals extensive changes in active zone proteins upon exocytosis.

Kohansalnodehi, M., Chua, J. J., Urlaub, H., Jahn, R., & Czernik, D. (2016). Analysis of protein phosphorylation in nerve terminal reveals extensive changes in active zone proteins upon exocytosis. eLife, 5: e14530. doi:10.7554/eLife.14530.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-E46A-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-D05D-0
Genre: Journal Article

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 Creators:
Kohansalnodehi, M.1, Author              
Chua, J. J.2, Author              
Urlaub, H.3, Author              
Jahn, R.1, Author              
Czernik, D.1, Author              
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              
2Research Group of Protein Trafficking in Synaptic Development and Function, MPI for Biophysical Chemistry, Max Planck Society, ou_1933287              
3Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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Free keywords: active zone; exocytosis; phosphoproteomics; phosphorylation; protein kinase; rat; synaptosome
 Abstract: Neurotransmitter release is mediated by the fast, calcium-triggered fusion of synaptic vesicles with the presynaptic plasma membrane, followed by endocytosis and recycling of the membrane of synaptic vesicles. While many of the proteins governing these processes are known, their regulation is only beginning to be understood. Here we have applied quantitative phosphoproteomics to identify changes in phosphorylation status of presynaptic proteins in resting and stimulated nerve terminals isolated from the brains of Wistar rats. Using rigorous quantification, we identified 252 phosphosites that are either up- or downregulated upon triggering calcium-dependent exocytosis. Particularly pronounced were regulated changes of phosphosites within protein constituents of the presynaptic active zone, including bassoon, piccolo, and RIM1. Additionally, we have mapped kinases and phosphatases that are activated upon stimulation. Overall, our study provides a snapshot of phosphorylation changes associated with presynaptic activity and provides a foundation for further functional analysis of key phosphosites involved in presynaptic plasticity.

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Language(s): eng - English
 Dates: 2016-04-26
 Publication Status: Published online
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.7554/eLife.14530
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Title: eLife
Source Genre: Journal
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Pages: 25 Volume / Issue: 5 Sequence Number: e14530 Start / End Page: - Identifier: -