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
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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其他
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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

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果蝇瞬时受体电位(TRP)的同源物被认为是质膜离子通道的单一亚基,其被激活的结果是主动或被动消耗钙库。与这一假说相一致,表达TRP的细胞显示了新的Ca 2 1 -渗透通道,该通道可被肌醇1,4,5-三磷酸受体(IP 3R)蛋白激活。TRP的表达以多种方式改变细胞,包括上调非TRP基因编码的IP 3R,并且TRP形成这些和其他细胞通道的证据仍然缺失。在这里,我们通过共免疫沉淀和谷胱甘肽S -转移酶下拉实验记录了TRP和IP 3R的物理相互作用,并确定了IP 3R的两个区域,F2 q和F2 g,与TRP的一个区域C7相互作用。这些相互作用区域在具有未修饰的TRP艾德补体的细胞中表达,
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