Differential oligomerization of endoplasmic reticulum-retained connexin43/connexin32 chimeras

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 i...

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Bibliographic Details
Published in:Cell communication & adhesion 2003-07, Vol.10 (4-6), p.319-322
Main Authors: Maza, Jose, Mateescu, Madalina, Das Sarma, Jayasri, Koval, Michael
Format: Article
Language:English
Subjects:
Animals
Cell Communication - physiology
Cell Membrane - metabolism
Chimera - metabolism
Connexin 43 - metabolism
Connexins - metabolism
Dimerization
Endoplasmic Reticulum - metabolism
Gap Junction beta-1 Protein
Gap Junctions - metabolism
HeLa Cells
Humans
Protein Sorting Signals - physiology
Protein Transport - physiology
Rats
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Summary: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.
ISSN:1541-9061
DOI:10.1080/714040446