PRRT2

The PRRT2 gene is located on chromosome 16p11. 2 and contains four exons. The PRRT2 protein is a type II transmembrane protein of proline-rich region (PRD) encoded by three exons (2 ~ 4 extrons) and consists of 340 amino acids in length.
Rossi (2016) confirmed the new topology of PRRT2 protein by in vivo immunolabeling, immunocolloidal gold electron microscopy, cell surface biotinylation, and computer modeling: N-terminal (1-268 aa) localization of the PRD domain In the cytoplasm, the short C-terminus of only 2 amino acids is extracellular, separated by a cytoplasmic ring of approximately 28 amino acids (290-317 aa). Although similar to other members of the Dispanins family, the PRRT2 protein differs in that only the second hydrophobic fragment (M2) actually crosses the plasma membrane, while the first hydrophobic fragment (M1) is due to approximately 279 proline in between. The appearance of the α-helix produces a back-folding that destroys the α-helix structure, thus forming a Helix-loop-helix structure, which mainly binds to the inner surface of the plasma membrane, and the result is that M1 does not cross.
The PRRT2 gene-encoded protein is highly conserved. By DNAMAN V6 multiple sequence alignment, the sequence similarity of the C-terminal domain increased to more than 90% in mammals, especially the two hydrophobic domains (M1 and M2) were extremely conserved.
Recent studies have confirmed that PRRT2 is a presynaptic membrane protein that is enriched in presynaptic terminals and begins to express at the onset of embryonic synapses, with peak expression during postnatal synapse formation and rearrangement. In addition to interacting with SNAP25, it interacts with the rapidly synchronizing release of the Ca2+ receptor synaptotagmin (Syt) 1/2 (a synaptic binding protein) and confers Ca2+ sensitivity to the SNARE complex, thereby promoting the synaptic vesicle cells. Spit process. Moreover, in primary neurons cultured in vitro, knockdown of the expression level of PRRT2 results in a decrease in the number of synapses, changes in the ultrastructure of synapses, and severely impair the formation of synaptic connections.