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Differential Oligomerization of Endoplasmic Reticulum-Retained Connexin43/Connexin32 Chimeras

机译:内质网保留的连接蛋白43 /连接蛋白32嵌合体的差异寡聚。

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摘要

To examine early events in connexin oligomerization, we made connexin constructs containing a C-terminal di-lysine based endoplasmic reticulum (ER) retention/retrieval signal (HKKSL). Previously, we found that both Cx32-HKKSL and Cx43-HKKSL were retained in the ER. However, Cx32-HKKSL oligomerized into hexameric hemichannels, but Cx43-HKKSL was retained as an apparent monomer. To define elements that prevent Cx43-HKKSL Oligomerization in the ER, we made a series of HKKSL-tagged Cx43/Cx32 chimeras. When expressed by HeLa cells, some chimeras were retained in the ER as apparent monomers, whereas others oligomerized in the ER. To date, the second and third transmembrane domains and the cytoplasmic loop domain provide the minimal sufficient Cx43 element to inhibit ER Oligomerization.
机译:为了检查连接蛋白低聚的早期事件,我们制备了包含C末端基于二赖氨酸的内质网(ER)保留/检索信号(HKKSL)的连接蛋白构建体。以前,我们发现Cx32-HKKSL和Cx43-HKKSL都保留在ER中。但是,Cx32-HKKSL低聚为六聚半通道,但Cx43-HKKSL被保留为明显的单体。为了定义阻止ER中Cx43-HKKSL寡聚的元素,我们制备了一系列带有HKKSL标签的Cx43 / Cx32嵌合体。当由HeLa细胞表达时,一些嵌合体作为明显的单体保留在ER中,而其他嵌合体则在ER中寡聚。迄今为止,第二和第三跨膜结构域和胞质环结构域提供了最小的足以抑制ER寡聚的Cx43元件。

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