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Connexin45 interacts with zonula occludens-1 in osteoblastic cells.
J G Laing1, R N Manley-Markowski, M Koval
1Department of Internal Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA. laing@id.wustl.edu
Cell Communication & Adhesion
|June 18, 2002
Summary
Connexin45 (Cx45) interacts with the tight junction protein ZO-1 in cells. This direct interaction suggests a functional link between connexins and tight junctions, impacting cellular permeability.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Connexin43 (Cx43) and Connexin45 (Cx45) are co-expressed in various tissues.
- Cx45 expression in ROS cells reduced dye permeability compared to Cx43 expressing cells, indicating potential Cx43-Cx45 interaction.
Purpose of the Study:
- To investigate the potential interaction between Cx45 and other cellular proteins.
- To identify proteins that associate with Cx45 in ROS/Cx45 cells.
Main Methods:
- Isolation of Cx45 from Cx45-transfected ROS cells under mild detergent conditions.
- Co-purification and immunofluorescence studies to detect Cx45 and ZO-1 association.
- Binding assays using Cx45-derived peptides and ZO-1.
Main Results:
- Cx45 co-purified with the tight junction protein ZO-1.
- Immunofluorescence confirmed colocalization of Cx45 and ZO-1 in ROS/Cx45 cells.
- ZO-1 directly bound to peptides derived from the carboxyl terminus of Cx45.
Conclusions:
- Cx45 directly interacts with ZO-1 in ROS/Cx45 cells.
- This interaction suggests a functional link between gap junctions and tight junctions.
- The findings provide insight into the molecular mechanisms governing cellular permeability.
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