Human connexin26 and connexin30 form functional heteromeric and heterotypic channels.
Human connexin26 and connexin30 form functional heteromeric and heterotypic channels.
复制标题
人连接蛋白26和连接蛋白30形成功能性异聚和异型通道。
DOI：
10.1152/ajpcell.00011.2007
复制
发表时间：
2007
期刊：
影响因子：
--
通讯作者：
Scherer,StevenS
中科院分区：
文献类型：
--
作者：
Yum,SabrinaW;Zhang,Junxian;Valiunas,Virginijus;Kanaporis,Giedrius;Brink,PeterR;White,ThomasW;Scherer,StevenS
分别编码人类间隙连接蛋白连接蛋白26（Cx 26）和连接蛋白连接蛋白30（Cx 30）的基因GJB 2和GJB 6的突变会导致听力损失。Cx 26和Cx 30都在耳蜗中表达，导致异聚半通道和异型间隙连接通道的潜在形成。为了研究它们之间的相互作用，我们在HeLa细胞中单独或一起表达了人Cx 26和Cx 30。当它们一起表达时，Cx 26和Cx 30似乎直接相互作用（通过它们在间隙连接斑块中的共定位，通过免疫共沉淀和通过荧光共振能量转移）。表达Cx 26或Cx 30的刮片加载细胞表明Cx 26同型通道稳健地转移阳离子和阴离子示踪剂，而Cx 30同型通道转移阳离子但不转移阴离子示踪剂。表达Cx 26和Cx 30的细胞也转移了阳离子和阴离子示踪剂的刮加载，和钙黄绿素（阴离子示踪剂）转移率之间的中间同型对应物的荧光恢复后光漂白。光漂白后的荧光恢复也表明，Cx 26和Cx 30形成功能性异型通道，允许钙黄绿素的转移，其不通过同型Cx 30通道。表达Cx 26和/或Cx 30的不同组合的细胞对的电生理记录证明了表达Cx 26和Cx 30的细胞对的独特门控特性。这些结果表明，Cx 26和Cx 30形成功能异聚体和异型通道，其生物物理性质和渗透性不同于其同型对应物。
Mutations inGJB2andGJB6,the genes that encode the human gap junction proteins connexin26 (Cx26) and connexin30 (Cx30), respectively, cause hearing loss. Cx26 and Cx30 are both expressed in the cochlea, leading to the potential formation of heteromeric hemichannels and heterotypic gap junction channels. To investigate their interactions, we expressed human Cx26 and Cx30 individually or together in HeLa cells. When they were expressed together, Cx26 and Cx30 appeared to interact directly (by their colocalization in gap junction plaques, by coimmunoprecipitation, and by fluorescence resonance energy transfer). Scrape-loading cells that express either Cx26 or Cx30 demonstrated that Cx26 homotypic channels robustly transferred both cationic and anionic tracers, whereas Cx30 homotypic channels transferred cationic but not anionic tracers. Cells expressing both Cx26 and Cx30 also transferred both cationic and anionic tracers by scrape loading, and the rate of calcein (an anionic tracer) transfer was intermediate between their homotypic counterparts by fluorescence recovery after photobleaching. Fluorescence recovery after photobleaching also showed that Cx26 and Cx30 form functional heterotypic channels, allowing the transfer of calcein, which did not pass the homotypic Cx30 channels. Electrophysiological recordings of cell pairs expressing different combinations of Cx26 and/or Cx30 demonstrated unique gating properties of cell pairs expressing both Cx26 and Cx30. These results indicate that Cx26 and Cx30 form functional heteromeric and heterotypic channels, whose biophysical properties and permeabilities are different from their homotypic counterparts.
登录
查看更多内容
影响因子：
1.3
作者：
W. Campbell;R. Rew
通讯作者：
R. Rew
DOI：
10.1099/00221287-18-3-621
发表时间：
1958-01-01
期刊：
JOURNAL OF GENERAL MICROBIOLOGY
影响因子：
--
作者：
KIDDER, GW;DUTTA, BN
通讯作者：
DUTTA, BN
利什曼原虫叶酸和甲氨蝶呤转运的生物化学和调节。
DOI：
--
发表时间：
1987
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Ellenberger,TE;Beverley,SM
通讯作者：
Beverley,SM
影响因子：
1.3
作者：
IOVANNISCI, DM;ULLMAN, B
通讯作者：
ULLMAN, B
二氢叶酸还原酶抑制剂
影响因子：
1.5
作者：
R. Ferone
通讯作者：
R. Ferone