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Neurochem Res. 2009 Mar;34(3):438-44. doi: 10.1007/s11064-008-9802-x. Epub 2008 Aug 2.

Dp71f modulates GSK3-beta recruitment to the beta1-integrin adhesion complex.

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University Center of Biomedical Research, Universidad de Colima, Avenida 25 de Julio 965 Col. Villa San Sebastián, C.P. 28045, Colima, Colima, Mexico.


Previously, it was shown that Dp71f binds to the beta1-integrin adhesion complex to modulate PC12 cell adhesion. The absence of Dp71f led to a failure in the beta1-integrin adhesion complex formation. One of the structural proteins which links the beta1-integrin cytoplasmic domain to the actin cytoskeleton is ILK. GSK3-beta is an ILK substrate and the carboxi-terminal region of dystrophin 427 is a substrate for hierarchical phosphorylation by GSK3-beta. 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-beta occurs. This interaction was corroborated by in vitro pulldown assays. We show that GSK3-beta is recruited to the beta1-integrin complex and that a reduced expression of Dp71f induces a reduced GSK3-beta recruitment to the beta1-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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