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
... dehydrogenase (Abcam, ab34436), Protein Kinase C-zeta (Cell signaling, ab51157), P-PKC-zeta (Abcam, ab76129), Syntaxin 4 (Abcam, ab57841), Vamp2 (Abcam, ab3347), Vimentin (Santacruz, sc73259, ...
Anchored multiplex PCR for targeted next-generation sequencing.
Boston, United States. In Nat Med, 2014
On the basis of our experience with performing AMP on 986 clinical FFPE samples, we show its potential as both a robust clinical assay and a powerful discovery tool, which we used to identify new therapeutically important gene fusions: ARHGEF2-NTRK1 and CHTOP-NTRK1 in glioblastoma, MSN-ROS1, TRIM4-BRAF, VAMP2-NRG1, TPM3-NTRK1 and RUFY2-RET in lung cancer, FGFR2-CREB5 in cholangiocarcinoma and PPL-NTRK1 in thyroid carcinoma.
How could SNARE proteins open a fusion pore?
Göttingen, Germany. In Physiology (bethesda), 2014
The SNARE (Soluble NSF Attachment protein REceptor) complex, which in mammalian neurosecretory cells is composed of the proteins synaptobrevin 2 (also called VAMP2), syntaxin, and SNAP-25, plays a key role in vesicle fusion.
Ca²⁺-regulated secretory granule exocytosis in pancreatic and parotid acinar cells.
Madison, United States. In Cell Calcium, 2014
Studies indicate the early phase is triggered by Ca(2+) and involves the SG proteins VAMP2 (vesicle associated membrane protein2), Ca(2+)-sensing protein synatotagmin 1 (syt1) and the accessory protein complexin 2. The molecular details for regulation of VAMP8-mediated SG exocytosis and the prolonged phase of secretion are still emerging.
Exocytosis and synaptic vesicle function.
Galveston, United States. In Compr Physiol, 2014
In synapses of the central nervous system, synaptobrevin 2, a major vesicular SNARE protein, forms a ternary SNARE complex with the plasma membrane SNARE proteins, syntaxin 1 and SNAP25.
Turning CALM into excitement: AP180 and CALM in endocytosis and disease.
Berlin, Germany. In Biol Cell, 2012
Recent work shows that the assembly protein 180 (AP180) N-terminal homology (ANTH) domain containing proteins AP180 and clathrin assembly lymphoid myeloid leukaemia (CALM) not only regulate the assembly of the endocytic machinery but also act as sorters for a subset of SNAREs, the vesicle-associated membrane proteins (VAMPs), most notably VAMP/synaptobrevin 2 at synapses.
SNARE proteins: one to fuse and three to keep the nascent fusion pore open.
New Haven, United States. In Science, 2012
We found that although only one SNARE per nanodisc is required for maximum rates of bilayer fusion, efficient release of content on the physiologically relevant time scale of synaptic transmission apparently requires three or more SNARE complexes (SNAREpins) and the native transmembrane domain of vesicle-associated membrane protein 2 (VAMP2).
The molecular basis for the endocytosis of small R-SNAREs by the clathrin adaptor CALM.
Cambridge, United Kingdom. In Cell, 2011
Here, we show that the R-SNAREs VAMP8, VAMP3, and VAMP2, which cycle between the plasma membrane and endosomes, bind directly to the ubiquitously expressed, PtdIns4,5P(2)-binding, endocytic clathrin adaptor CALM/PICALM.