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- W3131254523 abstract "P2X receptors (P2XR) are trimeric ATP-gated ion channels consisting of seven isoforms, P2X1-P2X7, which are permeable to cations. A hallmark of the 595 residues long P2X7R subunit is that its 2nd transmembrane domain (TM2) is linked with a cytoplasmic domain that is significantly larger than that of any other P2XR. From the partial or complete loss of the ATP4--activated ion channel activity due to various C-terminal deletions, we know that this endodomain plays an important functional role. Interestingly, several human P2X7 (hP2X7) splice variants were identified, including four C-terminally truncated variants named hP2X7B, hP2XE, hP2XG and hP2X7J. The amino acid sequences of P2X7A and P2X7B are identical up to Leu346, which lies approximately in the middle of TM2. The subsequent hP2X7B-unique part comprises the C-terminal portion of TM2 (347VRDSLFHALG356), followed by a very short cytoplasmic domain of only eight residues in total (357KWFGEGSD364). Here, we compared the P2X7AR and hP2X7BR as ATP4--gated cation channels and their oligomeric structure and expression on the cell surface. Shortening the hP2X7B variant C-terminal to Leu346 to study only the hP2X7A-identical portion reduced surface expression and homotrimeric assembly. On the other hand, if the truncation mutant contained all TM2 residues including Gly356, but without the eight residues of the cytoplasmic tail, homotrimeric assembly and surface expression was as efficient as with the full-length hP2X7B. ATP4--induced currents mediated by hP2X7BR desensitized relatively quickly as compared to the hP2X7AR, which has a non-desensitizing phenotype. The desensitizing behavior of hP2X7BR supports the view that the long C-terminal endodomain of the non-desensitizing hP2X7AR serves as a gating module that by forming a cytoplasmic cap, stabilizes the ATP4--induced open state of the P2X7AR.However, C-terminal endodomain is not absolutely needed for the channel function." @default.
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- W3131254523 date "2021-02-01" @default.
- W3131254523 modified "2023-09-25" @default.
- W3131254523 title "Electrophysiological and Biochemical Characterization of the Human P2X7B Receptor Inxenopus Laevisoocytes" @default.
- W3131254523 doi "https://doi.org/10.1016/j.bpj.2020.11.1423" @default.
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