Snapin mediates insulin secretory granule docking, but not trans-SNARE complex formation.
Identifieur interne : 001880 ( Main/Corpus ); précédent : 001879; suivant : 001881Snapin mediates insulin secretory granule docking, but not trans-SNARE complex formation.
Auteurs : Sangeeta Somanath ; Christopher J. Partridge ; Catriona Marshall ; Tony Rowe ; Mark D. TurnerSource :
- Biochemical and biophysical research communications [ 1090-2104 ] ; 2016.
English descriptors
- KwdEn :
- Animals (MeSH), Cell Line (MeSH), Exocytosis (MeSH), Insulin (metabolism), Insulin-Secreting Cells (cytology), Insulin-Secreting Cells (metabolism), Protein Binding (MeSH), Protein Structure, Tertiary (MeSH), Rats (MeSH), SNARE Proteins (metabolism), Secretory Vesicles (metabolism), Synaptosomal-Associated Protein 25 (analysis), Synaptosomal-Associated Protein 25 (metabolism), Syntaxin 1 (analysis), Syntaxin 1 (metabolism), Vesicular Transport Proteins (analysis), Vesicular Transport Proteins (metabolism).
- MESH :
- chemical , analysis : Synaptosomal-Associated Protein 25, Syntaxin 1, Vesicular Transport Proteins.
- chemical , metabolism : Insulin, SNARE Proteins, Synaptosomal-Associated Protein 25, Syntaxin 1, Vesicular Transport Proteins.
- cytology : Insulin-Secreting Cells.
- metabolism : Insulin-Secreting Cells, Secretory Vesicles.
- Animals, Cell Line, Exocytosis, Protein Binding, Protein Structure, Tertiary, Rats.
Abstract
Secretory granule exocytosis is a tightly regulated process requiring granule targeting, tethering, priming, and membrane fusion. At the heart of this process is the SNARE complex, which drives fusion through a coiled-coil zippering effect mediated by the granule v-SNARE protein, VAMP2, and the plasma membrane t-SNAREs, SNAP-25 and syntaxin-1A. Here we demonstrate that in pancreatic β-cells the SNAP-25 accessory protein, snapin, C-terminal H2 domain binds SNAP-25 through its N-terminal Sn-1 domain. Interestingly whilst snapin binds SNAP-25, there is only modest binding of this complex with syntaxin-1A under resting conditions. Instead synataxin-1A appears to be recruited in response to secretory stimulation. These results indicate that snapin plays a role in tethering insulin granules to the plasma membrane through coiled coil interaction of snapin with SNAP-25, with full granule fusion competency only resulting after subsequent syntaxin-1A recruitment triggered by secretory stimulation.
DOI: 10.1016/j.bbrc.2016.02.123
PubMed: 26946359
Links to Exploration step
pubmed:26946359Le document en format XML
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<author><name sortKey="Somanath, Sangeeta" sort="Somanath, Sangeeta" uniqKey="Somanath S" first="Sangeeta" last="Somanath">Sangeeta Somanath</name>
<affiliation><nlm:affiliation>Blizard Institute, Barts and the London School of Medicine and Dentistry, Queen Mary University of London, London, E1 2AT, UK.</nlm:affiliation>
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<author><name sortKey="Partridge, Christopher J" sort="Partridge, Christopher J" uniqKey="Partridge C" first="Christopher J" last="Partridge">Christopher J. Partridge</name>
<affiliation><nlm:affiliation>Diabetes Research Laboratories, Oxford Centre for Diabetes, Endocrinology and Churchill Hospital, University of Oxford, Oxford, OX3 7LJ, UK.</nlm:affiliation>
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<author><name sortKey="Marshall, Catriona" sort="Marshall, Catriona" uniqKey="Marshall C" first="Catriona" last="Marshall">Catriona Marshall</name>
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<author><name sortKey="Rowe, Tony" sort="Rowe, Tony" uniqKey="Rowe T" first="Tony" last="Rowe">Tony Rowe</name>
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<author><name sortKey="Turner, Mark D" sort="Turner, Mark D" uniqKey="Turner M" first="Mark D" last="Turner">Mark D. Turner</name>
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<term>Cell Line (MeSH)</term>
<term>Exocytosis (MeSH)</term>
<term>Insulin (metabolism)</term>
<term>Insulin-Secreting Cells (cytology)</term>
<term>Insulin-Secreting Cells (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
<term>Rats (MeSH)</term>
<term>SNARE Proteins (metabolism)</term>
<term>Secretory Vesicles (metabolism)</term>
<term>Synaptosomal-Associated Protein 25 (analysis)</term>
<term>Synaptosomal-Associated Protein 25 (metabolism)</term>
<term>Syntaxin 1 (analysis)</term>
<term>Syntaxin 1 (metabolism)</term>
<term>Vesicular Transport Proteins (analysis)</term>
<term>Vesicular Transport Proteins (metabolism)</term>
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<term>Syntaxin 1</term>
<term>Vesicular Transport Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Insulin</term>
<term>SNARE Proteins</term>
<term>Synaptosomal-Associated Protein 25</term>
<term>Syntaxin 1</term>
<term>Vesicular Transport Proteins</term>
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<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Insulin-Secreting Cells</term>
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<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Insulin-Secreting Cells</term>
<term>Secretory Vesicles</term>
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<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
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<term>Exocytosis</term>
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<front><div type="abstract" xml:lang="en">Secretory granule exocytosis is a tightly regulated process requiring granule targeting, tethering, priming, and membrane fusion. At the heart of this process is the SNARE complex, which drives fusion through a coiled-coil zippering effect mediated by the granule v-SNARE protein, VAMP2, and the plasma membrane t-SNAREs, SNAP-25 and syntaxin-1A. Here we demonstrate that in pancreatic β-cells the SNAP-25 accessory protein, snapin, C-terminal H2 domain binds SNAP-25 through its N-terminal Sn-1 domain. Interestingly whilst snapin binds SNAP-25, there is only modest binding of this complex with syntaxin-1A under resting conditions. Instead synataxin-1A appears to be recruited in response to secretory stimulation. These results indicate that snapin plays a role in tethering insulin granules to the plasma membrane through coiled coil interaction of snapin with SNAP-25, with full granule fusion competency only resulting after subsequent syntaxin-1A recruitment triggered by secretory stimulation. </div>
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<Abstract><AbstractText>Secretory granule exocytosis is a tightly regulated process requiring granule targeting, tethering, priming, and membrane fusion. At the heart of this process is the SNARE complex, which drives fusion through a coiled-coil zippering effect mediated by the granule v-SNARE protein, VAMP2, and the plasma membrane t-SNAREs, SNAP-25 and syntaxin-1A. Here we demonstrate that in pancreatic β-cells the SNAP-25 accessory protein, snapin, C-terminal H2 domain binds SNAP-25 through its N-terminal Sn-1 domain. Interestingly whilst snapin binds SNAP-25, there is only modest binding of this complex with syntaxin-1A under resting conditions. Instead synataxin-1A appears to be recruited in response to secretory stimulation. These results indicate that snapin plays a role in tethering insulin granules to the plasma membrane through coiled coil interaction of snapin with SNAP-25, with full granule fusion competency only resulting after subsequent syntaxin-1A recruitment triggered by secretory stimulation. </AbstractText>
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