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CASK (LIN2) interacts with Cx43 in wounded skin and their coexpression affects cell migration
Lucrecia Márquez-Rosado1, Deepika Singh, Hector Rincón-Arano
1Molecular Diagnostics Program, Human Biology and Public Health Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, WA 98109, USA.
Journal of Cell Science
|March 6, 2012
Summary
Mammalian CASK protein directly interacts with connexin 43 (Cx43), a gap junction component. This interaction influences cellular migration and wound healing, particularly during early connexin life cycle stages.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Gap junctions in vertebrates are formed by connexin proteins.
- CASK (LIN2) is a mammalian protein involved in cellular processes.
Purpose of the Study:
- To investigate the direct interaction between CASK and connexin 43 (Cx43).
- To explore the functional consequences of CASK-Cx43 interaction on cellular migration and wound healing.
Main Methods:
- Co-immunoprecipitation assays
- In vitro binding assays
- Far western blotting
- Immunoprecipitation studies
- Functional assays using MDCK cells
- Immunofluorescence microscopy
Main Results:
- Mammalian CASK directly interacts with Cx43, primarily with its hypophosphorylated form.
- Coexpression of CASK and Cx43 abrogates the inhibitory effect on cell migration seen with individual expression.
- CASK and Cx43 colocalize in mouse brain astrocytes and human foreskin during wound healing.
- CASK is mobilized to the plasma membrane during wounding, colocalizing with Cx43 and CADM1.
Conclusions:
- CASK interacts with Cx43 early in the connexin life cycle.
- The CASK-Cx43 interaction plays a role in plasma membrane targeting.
- This interaction impacts cellular processes such as migration and wound healing.
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