Sentences with word «syntaxin»

We generated knockin / knockout mice that expressed only open syntaxin - 1B.

In mammalian cells the SM protein Munc18 - 1, which interacts with the SNARE protein syntaxin, is an essential component of the tethering machinery.

When elevating calcium ion concentration directly at the presynaptic terminal with the use of caged calcium, cleavage of SNAP - 25 by botulinum toxin A (BoNT / A) produced a strong reduction in the calcium sensitivity for release, whereas cleavage of syntaxin using BoNT / C1 and synaptobrevin using tetanus toxin (TeNT) produced an all - or - nothing block without changing the kinetics of remaining vesicles.

Working with James Sutcliffe, Ph.D., associate professor of Molecular Physiology and Biophysics and of Psychiatry, the researchers identified inherited variations in the dopamine transporter gene and in the gene for syntaxin 1 (STX1), a protein that regulates the transporter, in two families of children with ASD.

When syntaxin is folded, though, the bubbles can't stick to it and the nerve cell can't pass on its signal.

«It [UNC - 13] grabs syntaxin and opens it up like a catapult,» Jorgensen says.

The team concluded that UNC - 13 does indeed unfold syntaxin and is therefore vital to the dispatch of nerve signals and memory.

The researchers knew that syntaxin comes in two forms.

To test this theory, they modified the gene encoding syntaxin in a strain of the nematode worm Caenorhabditis elegans so that the protein would remain unfolded.

When the scientists eliminated UNC - 13 in worms that produced normal syntaxin, however, the flow of neurotransmitters stopped, paralyzing the animals.

Subsequent work by Montecucco, Südhof, and Reinhard Jahn (Max Planck Institute, G ttingen) demonstrated that additional neurotoxins attack syntaxin and SNAP - 25.

Scheller established that synaptotagmin clutches a brain protein that he named syntaxin.

Work by Scheller, Jahn, John Heuser (Washington University School of Medicine, St. Louis), and others advanced the concept that VAMP / synaptobrevin and syntaxin form coils that wrap around each other along their lengths, thus drawing together the membranes in which they're embedded.

In contrast to vesicle - dwelling synaptotagmin and VAMP / synaptobrevin, syntaxin concentrates in the cell membrane — at spots where neurotransmitters are released from nerve cells.

Scheller found, for instance, that VAMP / synaptobrevin on vesicles clasps plasma membrane - bound syntaxin, and that SNAP - 25 helps them pair up.

Rothman also proposed that SNAP - 25, VAMP / synaptobrevin and syntaxin represent members of a large family of proteins, different forms of which are involved in membrane fusion in all cells, and in different compartments within cells.

Richmond's team suspected that UNC - 13 opened syntaxin, thus allowing signals to flow.

Assembly of two SNARE complexes by coil - coiling of the vesicle SNARE protein syb2 (blue) and the two presynaptic membrane SNARE proteins syntaxin - 1A (red) and SNAP - 25 (green) drives fusion.

Thus, the closed conformation of syntaxin - 1 gates the initiation of the synaptic vesicle fusion reaction, which is then mediated by SNARE - complex / Munc18 -1 assemblies.

Although SNARE complexes containing open syntaxin - 1 and Munc18 - 1 are essential for exocytosis, the function of closed syntaxin - 1 is unknown.

Binding of Munc18 - 1 to syntaxin - 1 was impaired in syntaxin - 1BOpen synapses, and the size of the readily releasable vesicle pool was decreased; however, the rate of synaptic vesicle fusion was dramatically enhanced.

During synaptic vesicle fusion, the soluble N - ethylmaleimide - sensitive factor — attachment protein receptor (SNARE) protein syntaxin - 1 exhibits two conformations that both bind to Munc18 - 1: a «closed» conformation outside the SNARE complex and an «open» conformation in the SNARE complex.

Before the fusion of synaptic vesicles with the plasma membrane, a protein complex is thought to form between VAMP — an integral membrane protein of the vesicle — and two proteins associated with the plasma membrane, SNAP - 25 and syntaxin.

In 1993, Scheller, in collaboration with Rothman, found that VAMP / synaptobrevin, syntaxin, and SNAP - 25 associate stably with one another to form the so - called «SNARE complex».

Because the two molecules bound to one another Scheller proposed that VAMP, the synaptic vesicle protein, bridges to syntaxin, the plasma membrane protein — thereby providing a scaffold onto which the molecular machinery that catalyzes membrane fusion can be assembled.

Axel Brunger (Yale University) and Jahn confirmed and extended these ideas when they reported the high - resolution structure of VAMP / synaptobrevin, syntaxin, and SNAP - 25 in 1998.

Südhof had discovered a protein, complexin, that strongly adheres to the VAMP / synaptobrevin, syntaxin, and SNAP - 25 bundle.

Three proteins stuck: VAMP / synaptobrevin, syntaxin, and SNAP - 25, a protein reported previously to reside on cell membranes of nerve termini.

Each SNARE complex consists of four Î ± - helices aligned in parallel, with syb2 and syntaxin - 1A contributing one helix and SNAP - 25 contributing two helices.

Remarkably he found that these proteins, when exposed to brain extracts, formed a complex with the vesicle protein VAMP and two plasma membrane proteins, syntaxin and SNAP - 25, precisely the proteins that Scheller had identified earlier.

In particular, he characterized the first synaptic vesicle membrane associated protein, v - SNARE or VAMP, and the first plasma membrane associated target proteins, t - SNAREs or syntaxin and SNAP - 25.

We identified interactions between the TGN - localized putative t - SNAREs syntaxin 6, syntaxin 16, and Vti1a, and two early / recycling endosomal v - SNAREs, VAMP3 / cellubrevin, and VAMP4.

In 1992, Scheller isolated the first t - SNARE and called it syntaxin, based on the Greek «putting together in order.»

Only three proteins stuck: VAMP / synaptobrevin, syntaxin and a third called SNAP - 25 (which dwells mainly in the plasma membrane).

Scheller, Südhof and other investigators also demonstrated that the bacterial poisons tetanus toxin and botulinum toxin block neurotransmitter release, by cleaving apart the vesicle and membrane associated proteins synaptobrevin, SNAP - 25 and syntaxin.