Journal
CELL COMMUNICATION AND ADHESION
Volume 12, Issue 5-6, Pages 237-247Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15419060500511875
Keywords
gap junction; di-lysine motif; assembly; Golgi apparatus
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Funding
- NHLBI NIH HHS [P01 HL019737, P01 HL019737-300018, P01 HL019737-26] Funding Source: Medline
- NIGMS NIH HHS [R01 GM061012, GM61012, R01 GM061012-06] Funding Source: Medline
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We have used connexin constructs containing a C-terminal di-lysine-based endoplasmic reticulum (ER) retention/retrieval signal (HKKSL) transfected into HeLa cells to study early events in connexin oligomerization. Using this approach, we found that Cx43-HKKSL stably expressed at moderate levels by HeLa cells was retained in the ER and prevented from oligomerization. However, Cx43-HKKSL stably overexpressed by HeLa cells escaped from the ER and localized to a perinuclear region of the cell that included the Golgi apparatus. Overexpressed Cx43-HKKSL oligomerized into hexamers and also formed Triton X-100 insoluble, intracellular complexes that resembled gap junctions. Thus, the ability of HeLa cells to inhibit Cx43 oligomerization was saturable. HeLa cells stably overexpressing Cx43-HKKSL may provide a useful model system to evaluate pharmacologic agents and/or cDNAs encoding chaperones with the potential to regulate initial steps in Cx43 oligomerization.
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