snare

V-SNARE that mediates vesicle transport pathways through interactions with t-SNAREs on the target membrane. These interactions are proposed to mediate aspects of the specificity of vesicle trafficking and to promote fusion of the lipid bilayers. May be concerned with increased secretion of cytokines associated with cellular senescence.

Syntaxin-6 (STX6) is a single-pass type IV membrane protein, which belongs to the Syntaxin family. STX6 is mainly localized in the plasma membrane. STX6 contains one t-SNARE coiled-coil homology domain and involved in intracellular vesicle trafficking. When STX6 function is inhibited, internalization through caveolae is dramaticaliy reduced, whereas other endocytic mechanisms are unaffected. It is reported that STX6 is necessary for proper expression of focal adhesion kinase and integrin alpha5 adhesion receptor.

α-Taxilin belongs to the taxilin family. α-Taxilin exists in almost all tissues, with higher expression levels observed in the heart, kidney, liver, and pancreas. α-Taxilin binds to the C-terminal coiled coil region of syntaxin family members STX1A, STX3A, and STX4A, but not when these proteins are complexed with SNAP25, VAMP2 or STXBP1, suggesting that it interacts with syntaxins that do not form the SNARE complex. It is shown that α-Taxilin plays multiple roles in the generation and maintenance of neurons through modulation of the NAC-mediated translational machinary and/or the syntaxin-mediated vesicle traffic in the soma. In addition, α-Taxilin may be involved in intracellular vesicle traffic and potentially in calcium-dependent exocytosis in neuroendocrine cells.

Complexin-2 (CPLX2), a member of the complexin/synaphin family, is a soluble pre-synaptic protein believed to regulate neurotransmitter release from pre-synaptic terminals. Complexins are soluble proteins that regulate the activity of soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes necessary for vesicle fusion. Complexins are unable to bind to monomeric SNARE proteins but bind with high affinity to ternary SNARE complexes and with lower affinity to target SNARE complexes. Complexin 1 (CX1) and complexin 2 (CX2) are presynaptic proteins that modulate neurotransmitter release and are used as markers of inhibitory and excitatory synapses, respectively. CPLX2 is localized in pre-synaptic terminals in mature brain. The G71-P89 region of CPLX2 is essential and sufficient for preferential axonal distribution. CPLX2 participates in the Ca(2+)-sensitive regulatory pathway for zymogen granule exocytosis. Complexin-2 is a key player in normal neurological function, and its downregulation could lead to changes in neurotransmitter release sufficient to cause significant behavioural abnormalities such as depression. It is involved in synaptogenesis and the modulation of neurotransmitter release.

Syntaxin-8 is a single-pass type IV membrane protein which belongs to the syntaxin family. It contains one t-SNARE coil homology domain. STX8 is highly expressed in heart, also found in brain, kidney, liver, lung, placenta, skeletal muscle, spleen and pancreas. STX8 is involved in protein trafficking from early to late endosomes via vesicle fusion and exocytosis. It as a vesicle trafficking protein functions in the early secretory pathway, possibly mediating retrograde transport form cis-golgi membrane to the ER.

E3 ubiquitin-protein ligase which ubiquitinates itself in cooperation with an E2 enzyme UBE2D2/UBC4 and serves as a targeting signal for proteasomal degradation. May play a role in regulation of neuronal functions and may also participate in the formation or breakdown of abnormal inclusions in neurodegenerative disorders. May act as a regulator of synaptic vesicle exocytosis by controlling the availability of SNAP25 for the SNARE complex formation.

Plays an important role in amino acid transport by acting as binding partner of amino acid transporters SLC6A18 and SLC6A19, regulating their trafficking on the cell surface and their activity. May also play a role in trafficking of amino acid transporters SLC3A1 and SLC7A9 to the renal cortical cell membrane. Regulator of SNARE complex function. Stimulator of beta cell replication.

Synaptosomal-associated protein 25, also known as Super protein, Synaptosomal-associated 25 kDa protein, SNAP25 and SNAP, is a cytoplasm and cell membrane protein that belongs to the SNAP-25 family. SNAP25 / SUP contains 2 t-SNARE coiled-coil homology domains. SNAP25 / SUP is a membrane bound protein anchored to the cytosolic face of membranes via palmitoyl side chains in the middle of the molecule. SNAP25 / SUP protein is a component of the SNARE complex, which is proposed to account for the specificity of membrane fusion and to directly execute fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together. SNAP25 / SUP is a Q-SNARE protein contributing two α-helices in the formation of the exocytotic fusion complex in neurons where it assembles with syntaxin-1 and synaptobrevin. SNAP25 / SUP is involved in the molecular regulation of neurotransmitter release. It may play an important role in the synaptic function of specific neuronal systems. SNAP25 / SUP associates with proteins involved in vesicle docking and membrane fusion. SNAP25 / SUP regulates plasma membrane recycling through its interaction with CENPF. SNAP25 / SUP inhibits P/Q- and L-type voltage-gated calcium channels located presynaptically and interacts with the synaptotagmin C2B domain in Ca2+-independent fashion. In glutamatergic synapses SNAP25 / SUP decreases the Ca2+ responsiveness, while it is naturally absent in GABAergic synapses.

Synaptobrevin Homolog YKT6 (YKT6) is an enzyme that belongs to the Synaptobrevin family. YKT6 contains a longin domain and a v-SNARE coiled-coil homology domain. YKT6 is highly conserved from yeast to human and it can functionally complement the loss of the yeast homolog in the yeast secretory pathway. It is a membrane associated, isoprenylated protein that functions at the endoplasmic reticulum-Golgi transport step. YKT6 is considered as one of the SNARE recognition molecules implicated in vesicular transport between secretory compartments.

Involved in the targeting and/or fusion of transport vesicles to their target membrane. Major SNARE protein of synaptic vesicles which mediates fusion of synaptic vesicles to release neurotransmitters. Essential for fast vesicular exocytosis and activity-dependent neurotransmitter release as well as fast endocytosis that mediates rapid reuse of synaptic vesicles. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1. VAMP2 Protein, Rat, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 14.1 kDa and the accession number is P63045.

STX3, also known as syntaxin 3, belongs to the syntaxin family. STX3 is a target membrane protein (t-SNARE) that is needed for membrane fusion. Membrane fusion requires the formation of a complex between a vesicle protein (v-SNARE) and t-SNAREs. STX3, together with syntaxin 2, are predominantly localized at the plasma membrane. Syntaxin 2 cycles between the plasma membrane and the perinuclear compartment whereas syntaxin 3 cycles between the plasma membrane and the trans-Golgi network. It is possible that this cycling has an important role in the regulation of t-SNARE function.

CPLX3, also known as complexin 3, belongs to the complexin/synaphin family. As a SNARE-binding protein, complexin (CPX), can act either as a facilitator or as an inhibitor of membrane fusion, constituting a controversial dilemma. CPX acts sequentially on assembling SNAREpins, first facilitating zippering by nearly doubling the distance at which v- and t-SNAREs can engage and then clamping them into a half-zippered fusion-incompetent state. Specifically, the central helix of CPX allows SNAREs to form this intermediate energetic state at 9-15 nm but not when the bilayers are closer than 9 nm. Stabilizing the activated-clamped state at separations of less than 9 nm requires the accessory helix of CPX, which prevents membrane-proximal assembly of SNAREpins. CPLX3 binds to the SNARE core complex containing SNAP25, VAMP2 and STX1A.

SNARE that acts to regulate protein transport between late endosomes and the trans-Golgi network.

NAPA (NSF Attachment Protein Alpha) is a Protein Coding gene. This gene encodes a member of the soluble NSF attachment protein (SNAP) family. SNAP proteins play a critical role in the docking and fusion of vesicles to target membranes as part of the 20S NSF-SNAP-SNARE complex. NAPA represents an anti-apoptotic protein that promotes resistance to cisplatin in cancer cells by inducing the degradation of the tumor suppressor p53. NAPA overexpression decreased the ubiquitination and degradation of synoviolin and reduced p53 protein level. The combination of cisplatin and knockdown of NAPA represents a novel and attractive strategy to eradicate p53-sensitive cancer cells. NAPA-73 as one of the earliest neuronal markers may reflect a difference between the central and peripheral nervous systems.

STX8, also known as syntaxin 8, directly interacts with HECTd3. STX8 forms the SNARE complex with syntaxin 7, vti1b and endobrevin. STX8 belongs to the syntaxin family. Members of this family are key molecules implicated in diverse vesicle docking and membrane fusion events. STX8 physically interacts with cystic fibrosis transmembrane conductance regulator (CFTR): recombinant syntaxin 8 binds CFTR in vitro and both proteins co-immunoprecipitate in HT29 cells. Syntaxin 8 regulates CFTR-mediated currents in chinese hamster ovary (CHO) cells stably expressing CFTR and syntaxin 8. STX8 contributes to the regulation of CFTR trafficking and chloride channel activity by the SNARE machinery.