Abstract
Previously, it was shown that Dp71f binds to the β1-integrin adhesion complex to modulate PC12 cell adhesion. The absence of Dp71f led to a failure in the β1-integrin adhesion complex formation. One of the structural proteins which links the β1-integrin cytoplasmic domain to the actin cytoskeleton is ILK. GSK3-β is an ILK substrate and the carboxi-terminal region of dystrophin 427 is a substrate for hierarchical phosphorylation by GSK3-β. Dp71f contains the carboxi-terminal domain present in dystrophin 427. By using co-immunoprecipitation assays, in the present work it is demonstrated that in the neuronal PC12 cell line an interaction between Dp71f and GSK3-β occurs. This interaction was corroborated by in vitro pulldown assays. We show that GSK3-β is recruited to the β1-integrin complex and that a reduced expression of Dp71f induces a reduced GSK3-β recruitment to the β1-integrin complex. In addition, the present work establishes that adhesion of PC12 cells to laminin does not influence the phosphorylation status of Dp71f.
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Acknowledgments
I would like to thank Victor Tapia Ramirez for his technical assistance. This work was supported by CONACyT-México.
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Cortés, J.C., Montalvo, E.A.G., Muñiz, J. et al. Dp71f Modulates GSK3-β Recruitment to the β1-Integrin Adhesion Complex. Neurochem Res 34, 438–444 (2009). https://doi.org/10.1007/s11064-008-9802-x
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DOI: https://doi.org/10.1007/s11064-008-9802-x