PoplarV1, Main, Exploration, bibRecord, 001667

Snapin mediates insulin secretory granule docking, but not trans-SNARE complex formation.

Identifieur interne : 001667 ( Main/Exploration ); précédent : 001666; suivant : 001668

Snapin mediates insulin secretory granule docking, but not trans-SNARE complex formation.

Auteurs : Sangeeta Somanath [Royaume-Uni] ; Christopher J. Partridge [Royaume-Uni] ; Catriona Marshall [Royaume-Uni] ; Tony Rowe [Australie] ; Mark D. Turner [Royaume-Uni]

Source :

Biochemical and biophysical research communications [ 1090-2104 ] ; 2016.

RBID : pubmed:26946359

Descripteurs français

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

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 001880
to stream Main, to step Curation: 001880

Le document en format XML

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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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<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Cellules à insuline (cytologie)</term>
<term>Cellules à insuline (métabolisme)</term>
<term>Exocytose (MeSH)</term>
<term>Insuline (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Lignée cellulaire (MeSH)</term>
<term>Protéine SNAP-25 (analyse)</term>
<term>Protéine SNAP-25 (métabolisme)</term>
<term>Protéines SNARE (métabolisme)</term>
<term>Protéines du transport vésiculaire (analyse)</term>
<term>Protéines du transport vésiculaire (métabolisme)</term>
<term>Rats (MeSH)</term>
<term>Structure tertiaire des protéines (MeSH)</term>
<term>Syntaxine-1 (analyse)</term>
<term>Syntaxine-1 (métabolisme)</term>
<term>Vésicules de sécrétion (métabolisme)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Synaptosomal-Associated Protein 25</term>
<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>
</keywords>
<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Protéine SNAP-25</term>
<term>Protéines du transport vésiculaire</term>
<term>Syntaxine-1</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Cellules à insuline</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Insulin-Secreting Cells</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Insulin-Secreting Cells</term>
<term>Secretory Vesicles</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellules à insuline</term>
<term>Insuline</term>
<term>Protéine SNAP-25</term>
<term>Protéines SNARE</term>
<term>Protéines du transport vésiculaire</term>
<term>Syntaxine-1</term>
<term>Vésicules de sécrétion</term>
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<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Line</term>
<term>Exocytosis</term>
<term>Protein Binding</term>
<term>Protein Structure, Tertiary</term>
<term>Rats</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Exocytose</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
<term>Rats</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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<tree><country name="Royaume-Uni"><region name="Angleterre"><name sortKey="Somanath, Sangeeta" sort="Somanath, Sangeeta" uniqKey="Somanath S" first="Sangeeta" last="Somanath">Sangeeta Somanath</name>
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<name sortKey="Marshall, Catriona" sort="Marshall, Catriona" uniqKey="Marshall C" first="Catriona" last="Marshall">Catriona Marshall</name>
<name sortKey="Partridge, Christopher J" sort="Partridge, Christopher J" uniqKey="Partridge C" first="Christopher J" last="Partridge">Christopher J. Partridge</name>
<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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<country name="Australie"><noRegion><name sortKey="Rowe, Tony" sort="Rowe, Tony" uniqKey="Rowe T" first="Tony" last="Rowe">Tony Rowe</name>
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   |clé=     pubmed:26946359
   |texte=   Snapin mediates insulin secretory granule docking, but not trans-SNARE complex formation.
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Snapin mediates insulin secretory granule docking, but not trans-SNARE complex formation.

Snapin mediates insulin secretory granule docking, but not trans-SNARE complex formation.

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