Modulation of Ca 2 1 entry by polypeptides of the inositol 1,4,5-trisphosphate receptor (IP3R) that bind transient receptor potential (TRP): Evidence for roles of TRP and IP3R in store depletion-activated Ca 2 1 entry
Modulation of Ca 2 1 entry by polypeptides of the inositol 1,4,5-trisphosphate receptor (IP3R) that bind transient receptor potential (TRP): Evidence for roles of TRP and IP3R in store depletion-activated Ca 2 1 entry
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发表时间:
1999
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通讯作者:
Guylain Boulay;Darren M. Brown;Ning Qin;Meisheng Jiang;Alexander Dietrich;Michael Xi Zhu;Zhangguo Chen;M. Birnbaumer;Katsuhiko Mikoshiba;Lutz Birnbaumer
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作者:
Guylain Boulay;Darren M. Brown;Ning Qin;Meisheng Jiang;Alexander Dietrich;Michael Xi Zhu;Zhangguo Chen;M. Birnbaumer;Katsuhiko Mikoshiba;Lutz Birnbaumer
Homologues of Drosophilia transient receptor potential (TRP) have been proposed to be unitary subunits of plasma membrane ion channels that are activated as a consequence of active or passive depletion of Ca 2 1 stores. In agreement with this hypothesis, cells expressingTRPsdisplaynovelCa 2 1 -permeablecationchannelsthat can be activated by the inositol 1,4,5-trisphosphate receptor (IP3R) protein. Expression of TRPs alters cells in many ways, including up-regulation of IP3Rs not coded for by TRP genes, and proof that TRP forms channels of these and other cells is still missing. Here, we document physical interaction of TRP and IP3R by coimmunoprecipitation and glutathione S -transferase-pulldown experiments and identify two regions of IP3R, F2q and F2g, that interact with one region of TRP, C7. These interacting regions were expressed in cells with an unmodified complement of TRPs and