Characterization of the Palmitoylation Domain of SNAP‐25

@article{Lane1997CharacterizationOT,
  title={Characterization of the Palmitoylation Domain of SNAP‐25},
  author={Simon Lane and Yun Liu},
  journal={Journal of Neurochemistry},
  year={1997},
  volume={69}
}
  • S. Lane, Y. Liu
  • Published 1997
  • Biology, Medicine
  • Journal of Neurochemistry
Abstract: SNAP‐25 (synaptosomal associated protein of 25 kDa) is a neural specific protein that has been implicated in the synaptic vesicle docking and fusion process. It is tightly associated with membranes, and it is one of the major palmitoylated proteins found in neurons. The functional role of palmitoylation for SNAP‐25 is unclear. In this report, we show that the palmitate of SNAP‐25 is rapidly turned over in PC12 cells, with a half‐life of ∼3 h, and the half‐life for the protein is 8 h… Expand
Membrane localization and biological activity of SNAP-25 cysteine mutants in insulin-secreting cells.
TLDR
It is concluded that both palmitoylation and binding to syntaxin are implicated in membrane association of SNAP-25 and suggests a complex, multi-component process for association of Snapchat with the membrane and its recruitment to a biologically productive state. Expand
Palmitoylation of the SNAP25 Protein Family
TLDR
It is shown that overexpression of specific Golgi-localized DHHC proteins active against SNAP25/23 proteins perturbs the normal secretion of human growth hormone from PC12 cells and DHHC2 is, thus, a candidate enzyme to regulate SNAP 25/23 palmitoylation dynamics at the plasma membrane. Expand
Identification of PSD-95 Palmitoylating Enzymes
TLDR
Inhibition of P-PAT activity in neurons reduced palmitoylation and synaptic clustering of PSD-95 and diminished AMPA receptor-mediated neurotransmission and this study suggests that P- PATs regulate synaptic function through PSd-95 palmitoyslation. Expand
Differential palmitoylation regulates intracellular patterning of SNAP25
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It is proposed that the cysteine-rich domain of SNAP25 is designed to facilitate the dual function of this SNARE protein at the plasma membrane and endosomes, and that dynamic palmitoylation acts as a mechanism to regulate the precise intracellular patterning ofSNAP25. Expand
SNAP-25 Is Targeted to the Plasma Membrane through a Novel Membrane-binding Domain*
TLDR
It is shown that the minimal plasma membrane-targeting domain of SNAP-25 maps to residues 85–120, which represents a protein module that is physically and functionally separable from the SNARE complex-forming domains. Expand
SNAP-23 and SNAP-25 are palmitoylated in vivo.
  • K. Vogel, P. Roche
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
  • 1999
TLDR
It is reported that like SNAP-25, SNAP-23 is palmitoylated in vivo on one or more cysteine residues present in a central "palmitoylation domain" of the t-SNARE complex. Expand
The SNAP-25 linker as an adaptation toward fast exocytosis.
TLDR
The SNAP-25 linker might have evolved as an adaptation toward calcium triggering and a high rate of execution of the fusion process, those features that distinguish exocytosis from other membrane fusion pathways. Expand
Regulation of SNAP-25 trafficking and function by palmitoylation.
TLDR
The mechanisms of SNAP-25 palmitoylation are discussed and how this modification regulates the intracellular trafficking and exocytotic function of this essential protein is discussed. Expand
SNAP‐25 and Gene‐targeted Mouse Mutants
  • C. Bark
  • Biology, Medicine
  • Annals of the New York Academy of Sciences
  • 2009
TLDR
The evolutionary conserved soluble N‐ethylmaleimide‐sensitive factor attachment protein receptor (SNARE) fusion machinery is the operational unit in the release of neurotransmitters and hormones from excitable cells and recent findings in gene‐targeted mouse mutants have started to unravel the importance that physiological levels of total SNAP‐25 protein are present and, importantly, that this is accompanied by a balanced expression of SNAP­25a and SNAP‐ 25b. Expand
Palmitoylated Peptides from the Cysteine-rich Domain of SNAP-23 Cause Membrane Fusion Depending on Peptide Length, Position of Cysteines, and Extent of Palmitoylation*
TLDR
The results suggest an important role for the cysteine-rich palmitoylated domain of SNAP-23 in promoting membrane fusion in cells and generate synthetic peptides corresponding to this domain and covalently modified thecysteines with palmitic acid. Expand
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References

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Determination of the Structural Requirements for Palmitoylation of p63 (*)
TLDR
The six-amino acid distance between the end of the predicted transmembrane domain and the palmitoylation site was found to be essential for proper acylation of p63, and analysis of a chimeric construct between p63 and the plasma membrane protein di peptidylpeptidase IV revealed that p63 palMIToylation is not dependent on its transmemBRane domain. Expand
Multiple palmitoylation of synaptotagmin and the t‐SNARE SNAP‐25
TLDR
It is reported that both synaptotagmin and SNAP‐25 are palmitoylated with their fatty acids attached in a labile thioester‐type bond, establishing that SNAP‐ 25 is membrane‐anchored via covalently linked palmitate. Expand
SNAP-25, a t-SNARE which binds to both syntaxin and synaptobrevin via domains that may form coiled coils.
TLDR
It is concluded that SNAP-25 can interact with both syntaxin and synaptobrevin and that binding may be mediated by alpha-helical domains that form intermolecular coiled-coil structures. Expand
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TLDR
Data suggest that the complex of the vesicular protein synaptobrevin with the plasma membrane protein syntaxin is required for physiological α-SNAP binding, which probably functions in a late step of the membrane fusion reaction after the formation of the synaptOBrevin-syntaxin- SNAP25 core complex. Expand
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TLDR
Using the yeast two-hybrid system, a 23-kDa protein from human B lymphocytes is identified that binds tightly to multiple syntaxins and synaptobrevins/VAMPs in vitro and suggests that SNAP-23 is an essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion in all mammalian cells. Expand
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TLDR
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TLDR
Light and electron microscopic immunocytochemistry indicated that SNAP-25 is located within the presynaptic terminals of hippocampal mossy fibers and the inner molecular layer of the dentate gyrus, suggesting that Snapchat may play an important role in the synaptic function of specific neuronal systems. Expand
The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS
TLDR
It is shown here that SuP is identical to SNAP-25, a highly conserved synaptic protein of known primary structure, by immunoprecipitation with anti-SNAP-25 antiserum of SuP labeled with 35S-methionine and transported by retinal ganglion cells of rat and cat. Expand
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TLDR
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TLDR
Findings indicate that alternative isoforms of SNAP-25 may play distinct roles in vesicular fusion events required for membrane addition during axonal outgrowth and for release of neuromodulatory peptides and neurotransmitters. Expand
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