Abstract
The role of SNARE [soluble NSF (N-ethylmaleimide-sensitive factor) accessory protein receptor] protein in cellular trafficking, membrane fusion and vesicle release in synaptic nerve terminals is described. The purpose of this review is to highlight the role of SNAREs in vital inflammatory conditions in maturing dendritic cells in order to retain the capacity to present new antigens together with altered cytokine secretory functions. This role of SNAREs can be used as novel targets for therapy in inflammatory diseases. The essential mechanism of SNAREs proteins for regulation of tumour formation through multiple signals and transportation pathways is also discussed. Finally, this review summarizes the current knowledge of SNARE proteins in regulating endocytosis in cancer cells and the possible therapeutic applications related to the pathogenesis of tumor formation.
Highlights
Fusion of plasma membrane is achieved by the cooperation of various proteins, such as soluble NEM-sensitive factor (NSF) accessory protein receptor (SNARE) proteins, Rab GTPases and their effectors, and soluble NSF accessory protein receptor (SNARE) chaperones
Most of them contain one SNARE motif except four SNAREs (SNAP-23, Synaptosome associated proteins (SNAP)-25, SNAP-29/GS32, and SNAP-47) contain two SNARE motifs. Both syntaxin and vesicle-associated membrane protein (VAMP) are attached to the membrane by a carboxy-terminal trans-membrane domain, whereas SNAP-25 is peripherally attached to the membrane by palmitoylation of four cysteine residues in the central region of the protein [9]
One SNARE motif from synaptobrevin (v-SNARE) on a synaptic vesicle and three SNARE motifs provided by syntaxin-1 and SNAP25 (t-SNAREs) from the plasma membrane assemble into a tight trans-SNARE complex that brings the two membranes into close apposition
Summary
Fusion of plasma membrane is achieved by the cooperation of various proteins, such as SNARE proteins, Rab GTPases and their effectors, and SNARE chaperones. SNARE proteins bring two membrane lipid bilayers into close proximity, which induces the fusion of the two close positioned membranes [1] These SNAREs proteins have a characteristic coiled-coil SNARE motif of approximately 70 amino acids comprising heptad repeats. Most of them contain one SNARE motif except four SNAREs (SNAP-23, SNAP-25, SNAP-29/GS32, and SNAP-47) contain two SNARE motifs Both syntaxin and VAMP are attached to the membrane by a carboxy-terminal trans-membrane domain, whereas SNAP-25 is peripherally attached to the membrane by palmitoylation of four cysteine residues in the central region of the protein [9]. When the ionic layer of SNARE complex showed in crystal structure comprises one arginine (R) (contributed by synaptobrevin) and three glutamine (Q) residues (contributed by Stx1A and SNAP-25) in the central position of the four-helix bundle. Syntaxin-16 has the Habc region that can fold into a three-helix bundle and intra-molecularly interact with the SNARE motif, thereby preventing its assembly into a SNARE complex [11]
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