• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Cell communication & adhesion >Fusion of GFP to the Carboxyl Terminus of Connexin43 Increases Gap Junction Size in HeLa Cells
【24h】

Fusion of GFP to the Carboxyl Terminus of Connexin43 Increases Gap Junction Size in HeLa Cells

机译：GFP与Connexin43羧基末端的融合增加HeLa细胞中的间隙连接大小。

获取原文
获取原文并翻译 | 示例
       
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

The pattern of gap junctional coupling between cells is thought to be important for the proper function of many types of tissues. At present, little is known about the molecular mechanisms that control the size and distribution of gap junctions. We addressed this issue by expressing connexin43 (Cx43) constructs in HeLa cells, a connexin-deficient cell line. HeLa cells expressing exogenously introduced wild-type Cx43 formed small, punctate gap junctions. By contrast, cells expressing Cx43-GFP formed large, sheet-like gap junctions. These results suggest that the GFP tag, which is fused to the carboxyl terminus of Cx43, alters gap junction size by masking the carboxyl terminal amino acids of Cx43 that comprise a zonula occludins-1 (ZO-1) binding site. We are currently testing this hypothesis using deletion and dominant-negative constructs that directly target the interaction between Cx43 and ZO-1.
机译：细胞之间的间隙连接偶联的模式被认为对于许多类型的组织的正常功能很重要。目前，关于控制间隙连接的大小和分布的分子机制知之甚少。我们通过在HeLa细胞（一种连接蛋白缺陷细胞系）中表达连接蛋白43（Cx43）构建体来解决此问题。表达外源导入的野生型Cx43的HeLa细胞形成小的点状间隙连接。相比之下，表达Cx43-GFP的细胞形成了大的片状间隙连接。这些结果表明，与Cx43羧基末端融合的GFP标签通过掩盖Cx43的羧基末端氨基酸（小带occludins-1（ZO-1）结合位点）来改变间隙连接大小。我们目前正在使用直接针对Cx43与ZO-1之间相互作用的缺失和显性负性构建物测试这一假设。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号