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Primary or familial hemophagocytic lymphohistiocytosis (FHLH) is an autosomal recessive disorder of immune dysfunction caused by mutations in Perforin, Munc 13-4, Syntaxin 11 and STBX2 genes (2-5).
We have explored the potential interaction between syntaxin 1A and DAT in rat striatal neurons by examining the ability of botulinum toxin C (BoNT/C), which cleaves syntaxin 1A, to affect DAT phosphorylation and transport activity.
Then, the lysates were separated by SDS-PAGE and probed with specific antibodies: SNAP-25 (Abcam, ab66066), SNAP-23 (Abcam, ab3340), syntaxin (Santa Cruz, sc-12736), Vamp2 (Abcam, ab6276), Munc-18 (SYSY, 116002), Phospho-Synaptotagmin (R&D Systems, PPS085), [beta]-ACTIN (Abcam, ab6276), TUBULIN (Abcam, ab15246), and Na/K ATPase (Millipore, 05-369).
Syntaxin will be responsible for the discovery of new therapeutic candidates and Ipsen will apply its skills to pharmacological, preclinical and clinical assessments of the newly discovered compounds.
The SNARE domain of syntaxin mediates a membrane fusion process, involving vesicular transport along the exocytic and endocytic pathways.
Speciality pharmaceutical company Ipsen (Euronext:IPN) and Syntaxin, a biotechnology company, announced today a global strategic collaboration to explore the discovery and development of new compounds in the field of botulinum toxins.
The JBD sequence, fully conserved in both isoforms of Syntaxin (residues 148-155), has been mapped on the structure of Syntaxin-1 [48], which we have chosen as a representative structure also for Syntaxin-2, because they share a sequence identity of 64.4% and sequence similarity of 80% (Figure 3(c)).
A group of proteins that are directly involved in the exocytosis of SVs is the SNARE (SNAP Soluble NSF Attachment Protein REceptor) complex formed by synaptobrevin, syntaxin, and synaptosomal-associated protein 25 (SNAP25), which mediates SV fusion with the AZ plasma membrane [18].
Syntaxin 1A protein is located in the presynaptic region and forms the SNARE complex with SNAP-25 and VAMP2; the SNARE complex is critical in neurotransmission (14).
Then the cleaved light chain passes through the vesicle into the nerve terminal cytoplasm, and cleaves SNAP-25 and syntaxin to prevent the formation of the SNARE protein complex on the membrane, which allows the neurotransmitters to bind and pass into the muscle and contract.
Syntaxin 6-mediated Golgi translocation plays an important role in nuclear functions of EGFR through microtubule-dependent trafficking.
The autosomal dominant form most commonly occurs as result of microdeletions in STX16, the gene encoding syntaxin 16, while the sporadic form has predilection to GNAS microdeletions involving exon NESP55 (6,7).
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