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Pannexin1 is part of the pore forming unit of the P2X 7 receptor death complex
Author(s) -
Locovei Silviu,
Scemes Eliana,
Qiu Feng,
Spray David C.,
Dahl Gerhard
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.12.056
Subject(s) - purinergic receptor , gap junction , pannexin , microbiology and biotechnology , receptor , biophysics , chemistry , programmed cell death , xenopus , connexin , apoptosis , biology , biochemistry , intracellular , gene
The purinergic receptor P2X 7 is part of a complex signaling mechanism participating in a variety of physiological and pathological processes. Depending on the activation scheme, P2X 7 receptors in vivo are non‐selective cation channels or form large pores that can mediate apoptotic cell death. Expression of P2X 7 R in Xenopus oocytes results exclusively in formation of a non‐selective cation channel. However, here we show that co‐expression of P2X 7 R with pannexin1 in oocytes leads to the complex response seen in many mammalian cells, including cell death with prolonged ATP application. While the cation channel activity is resistant to carbenoxolone treatment, this gap junction and hemichannel blocking drug suppressed the currents induced by ATP in pannexin1/P2X 7 R co‐expressing cells. Thus, pannexin1 appears to be the molecular substrate for the permeabilization pore (or death receptor channel) recruited into the P2X 7 R signaling complex.