Differential oligomerization of endoplasmic reticulum-retained connexin43/connexin32 chimeras.
Differential oligomerization of endoplasmic reticulum-retained connexin43/connexin32 chimeras.
复制标题
内质网保留的连接蛋白43/连接蛋白32嵌合体的差异寡聚化。
DOI：
10.1080/cac.10.4-6.319.322
复制
发表时间：
2003
影响因子：
--
通讯作者：
Koval,Michael
中科院分区：
文献类型：
--
作者：
Maza,Jose;Mateescu,Madalina;DasSarma,Jayasri;Koval,Michael
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.
