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  Protein kinase C-dependent phosphorylation of synaptosome- associated protein of 25 kDa at Ser(187) potentiates vesicle recruitment

Nagy, G., Matti, U., Nehring, R., Binz, T., Rettig, J., Neher, E., et al. (2002). Protein kinase C-dependent phosphorylation of synaptosome- associated protein of 25 kDa at Ser(187) potentiates vesicle recruitment. Journal of Neuroscience, 22(21), 9278-9286. Retrieved from http://www.jneurosci.org/cgi/reprint/22/21/9278.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F299-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E47A-7
Genre: Journal Article

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 Creators:
Nagy, G.1, Author              
Matti, U., Author
Nehring, R.1, Author              
Binz, T., Author
Rettig, J.1, Author              
Neher, E.1, Author              
Soerensen, J. B.2, Author              
Affiliations:
1Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society, ou_578579              
2Research Group of Molecular Mechanisms of the Exocytosis, MPI for biophysical chemistry, Max Planck Society, ou_578584              

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Free keywords: chromaffin cell; exocytosis; membrane capacitance; protein kinase C; SNARE proteins; SNAP-25
 Abstract: Activation of protein kinase C (PKC) constitutes a key event in the upregulation of secretory strength in neurons and neurosecretory cells during extensive stimulation, presumably by speeding up vesicle supply. However, the molecular targets and their mode of action remain elusive. We studied the only PKC-dependent phosphorylation site in the neuronal soluble N- ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex, Ser(187),in synaptosome-associated protein of 25 kDa (SNAP-25). This phosphorylation site is located within the negatively charged C-terminal end of SNAP-25, which has been shown to be of critical importance in calcium-triggered exocytosis. We combined mutational studies that used overexpression in chromaffin cells with capacitance measurements and flash photolysis of caged calcium, allowing for high time resolution during both the stimulation and measurement of exocytosis. Overexpression of mutants simulating the phosphorylated form of Ser(187) accelerated vesicle recruitment after the emptying of the releasable vesicle pools. Overexpression of mutants simulating the nonphosphorylated form, or block of PKC, impaired the refilling of the vesicle pools to similar extents. Biochemical studies verified the phosphorylation of a subpopulation of SNAP-25 after elevation of intracellular calcium concentrations. Some of the mutations led to a moderately decreased fast exocytotic burst component, which did not seem to be associated with the phosphorylation state of SNAP-25. Thus the C terminus of SNAP-25 plays a role for both fast exocytosis triggering and vesicle recruitment, and the latter process is regulated by PKC-dependent phosphorylation.

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Language(s): eng - English
 Dates: 2002-11-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: Journal of Neuroscience
Source Genre: Journal
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Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 22 (21) Sequence Number: - Start / End Page: 9278 - 9286 Identifier: -