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Syntaxin binding protein 4

Synip, syntaxin 4 interacting protein, Stxbp4
Top mentioned proteins: Insulin, syntaxin 4, VAMP2, Akt, v-SNARE
Papers using Synip antibodies
A map of WW domain family interactions
Supplier
Hamel Frederick G., In PLoS ONE, 2003
... Anti-Synip rabbit monoclonal antibody was from Epitomics, Inc ...
Papers on Synip
Synip phosphorylation is required for insulin-stimulated Glut4 translocation and glucose uptake in podocyte.
Yamada et al., Maebashi, Japan. In Endocr J, 2013
Previously we reported that the phosphorylation of Synip on serine 99 is required for Synip dissociation from Syntaxin4 and insulin-stimulated Glut4 translocation in cultured 3T3-L1 adipocytes.
Synip arrests soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE)-dependent membrane fusion as a selective target membrane SNARE-binding inhibitor.
Shen et al., Boulder, United States. In J Biol Chem, 2013
Using this defined fusion system, we discovered that the regulatory factor synip binds to GLUT4 exocytic SNAREs and inhibits the docking, lipid mixing, and content mixing of the fusion reaction.
[Four-week simulated weightlessness increases the expression of atrial natriuretic peptide in the myocardium].
Yu et al., Xi'an, China. In Sheng Li Xue Bao, 2013
Synip and Munc-18c as regulators of SNAREs did not show significant difference between the CON and SUS.
Syntaxin4 interacting protein (Synip) binds phosphatidylinositol (3,4,5) triphosphate.
Mori et al., Maebashi, Japan. In Plos One, 2011
The syntaxin 4 interacting protein (Synip) binds to syntaxin 4 in the basal state and dissociates in the insulin-stimulated state allowing for the subsequent binding of Vamp2 containing Glut4 vesicles and fusion with the plasma membrane.
VAMP3 regulates podosome organisation in macrophages and together with Stx4/SNAP23 mediates adhesion, cell spreading and persistent migration.
GeneRIF
Murray et al., Sydney, Australia. In Exp Cell Res, 2011
By altering the levels of individual components of the VAMP3/Stx4/SNAP23 complex we show here that this SNARE complex regulates efficient macrophage adhesion, spreading and migration on fibronectin.
Stxbp4 regulates DeltaNp63 stability by suppression of RACK1-dependent degradation.
GeneRIF
Prives et al., New York City, United States. In Mol Cell Biol, 2009
Stxbp4 and RACK1, two scaffold proteins, play central roles in balancing DeltaNp63 protein levels. While Stxbp4 functions to stabilize DeltaNp63 proteins, RACK1 targets DeltaNp63 for degradation.
An efficient co-expression and purification system for the complex of Stx4 and C-terminal domain of Synip.
Xu et al., Wuhan, China. In Biochem Biophys Res Commun, 2008
Synip and Stx4 complex plays a key role in GLUT4 vesicle trafficking and fusion with plasma membrane.
Synip phosphorylation is required for insulin-stimulated Glut4 translocation.
Mori et al., Maebashi, Japan. In Biochem Biophys Res Commun, 2007
Previously we identified an unusual potential dual Akt/protein kinase B consensus phosphorylation motif in the protein Synip (RxKxRS(97)xS(99)) with serine 99 as a unique Akt2, but not Akt1 or for Akt3, substrate phosphorylation site.
Syntaxin 4 facilitates biphasic glucose-stimulated insulin secretion from pancreatic beta-cells.
GeneRIF
Thurmond et al., Indianapolis, United States. In Mol Endocrinol, 2006
Syntaxin 4-based SNARE complexes are essential for biphasic insulin granule fusion in pancreatic beta-cells.
Minireview: recent developments in the regulation of glucose transporter-4 traffic: new signals, locations, and partners.
Review
Klip et al., Toronto, Canada. In Endocrinology, 2005
At the cell periphery, GLUT4-containing vesicles tether, dock, and fuse with the PM assisted by the exocyst complex followed by engagement of a soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex [with vesicle-associated membrane protein (VAMP)2 as the vesicular (v)-SNARE and soluble NSF-attachment protein (SNAP)23 and syntaxin4 as target (t)-SNAREs] regulated by the accessory proteins Munc18c, Synip and Tomosyn.
Synip phosphorylation does not regulate insulin-stimulated GLUT4 translocation.
Lienhard et al., United States. In Biochem Biophys Res Commun, 2005
Another potential connecting substrate is the protein Synip, which associates with the SNARE syntaxin4.
Akt2 phosphorylates Synip to regulate docking and fusion of GLUT4-containing vesicles.
Mori et al., Maebashi, Japan. In J Cell Biol, 2005
We have identified an unusual potential dual Akt/protein kinase B consensus phosphorylation motif in the protein Synip (RxKxRS(97)xS(99)).
Syntaxin 4 and Synip (syntaxin 4 interacting protein) regulate insulin secretion in the pancreatic beta HC-9 cell.
GeneRIF
Mori et al., Maebashi, Japan. In J Biol Chem, 2003
Syntaxin 4 and Synip (syntaxin 4 interacting protein) regulate insulin secretion in the pancreatic beta HC-9 cells
Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes.
Pessin et al., Ann Arbor, United States. In Mol Cell, 1999
Insulin-stimulated glucose transport and GLUT4 translocation require regulated interactions between the v-SNARE, VAMP2, and the t-SNARE, syntaxin 4. We have isolated a novel syntaxin 4-binding protein, Synip, which specifically interacts with syntaxin 4. Insulin induces a dissociation of the Synip:syntaxin 4 complex due to an apparent decrease in the binding affinity of Synip for syntaxin 4. In contrast, the carboxyterminal domain of Synip does not dissociate from syntaxin 4 in response to insulin stimulation but inhibits glucose transport and GLUT4 translocation.
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