Insulin-like growth factor-I inhibits transcriptional responses of transforming growth factor-beta by phosphatidylinositol 3-kinase/Akt-dependent suppression of the activation of Smad3 but not Smad2.
In PLoS ONE, 2002
... 03, 1005), Glucose-6-P dehydrogenase (Abcam, ab34436), Protein Kinase C-zeta (Cell signaling, ab51157), P-PKC-zeta (Abcam, ab76129), Syntaxin 4 (Abcam, ab57841), Vamp2 (Abcam, ab3347), ...
Tctex1d2 Is a Negative Regulator of GLUT4 Translocation and Glucose Uptake.
Japan. In Endocrinology, Oct 2015
Although overexpression of Tctex1d2 had no significant effect on GLUT4 internalization, Tctex1d2 was found to associate with syntaxin 4 in an insulin-dependent manner and inhibit Doc2b binding to syntaxin 4. In addition, glucose-dependent insulinotropic polypeptide rescued the Tctex1d2 inhibition of insulin-stimulated GLUT4 translocation by suppressing the Tctex1d2-syntaxin 4 interaction and increasing Doc2b-Synatxin4 interactions.
Tomosyn is a novel Akt substrate mediating insulin-dependent GLUT4 exocytosis.
Fukuoka, Japan. In Int J Biochem Cell Biol, May 2015
In vitro pull-down assay showed that phosphorylation of tomosyn at Ser-783 by Akt inhibited the interaction with syntaxin 4. Insulin stimulation increased GLUT4 in the cell surface of CHO-K1 cells to promote glucose uptake, however exogenous expression of the mutant tomosyn attenuated the increase by insulin.
Gelsolin associates with the N terminus of syntaxin 4 to regulate insulin granule exocytosis.
Indianapolis, United States. In Mol Endocrinol, 2012
data support a mechanistic model for gelsolin's role in insulin exocytosis: gelsolin clamps unsolicited soluble N-ethylmaleimide-sensitive factor attachment receptor-regulated exocytosis through association with Syn4 which is relieved upon stimulus-induced calcium influx to activate gelsolin to facilitate insulin exocytosis
Minireview: recent developments in the regulation of glucose transporter-4 traffic: new signals, locations, and partners.
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.
The epithelium in inflammatory bowel disease: potential role of endocytosis of junctional proteins in barrier disruption.
Atlanta, United States. In Novartis Found Symp, 2003
Interestingly, internalized AJ and TJ proteins enter early endosomes followed by movement to organelles that do not label with markers of late and recycling endosomes, lysosomes or Golgi but appear to represent a unique storage compartment that colocalizes with t-SNARE protein, syntaxin 4. A better understanding of the mechanisms of junctional internalization and recycling will likely provide new insights into the mechanisms of altered barrier function in IBD.