Dp71f Modulates GSK3- beta Recruitment to the beta 1-Integrin Adhesion Complex

Previously, it was shown that Dp71f binds to the beta 1-integrin adhesion complex to modulate PC12 cell adhesion. The absence of Dp71f led to a failure in the beta 1-integrin adhesion complex formation. One of the structural proteins which links the beta 1-integrin cytoplasmic domain to the actin cy...

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Veröffentlicht in:Neurochemical research 2009-03, Vol.34 (3), p.438-444
Hauptverfasser: CortEs, Joel Cerna, Montalvo, Eliud Alfredo Garcia, MuNiz, JesUs, Mornet, Dominique, Garrido, Efrain, Centeno, Federico, Cisneros, Bulmaro
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container_end_page 444
container_issue 3
container_start_page 438
container_title Neurochemical research
container_volume 34
creator CortEs, Joel Cerna
Montalvo, Eliud Alfredo Garcia
MuNiz, JesUs
Mornet, Dominique
Garrido, Efrain
Centeno, Federico
Cisneros, Bulmaro
description Previously, it was shown that Dp71f binds to the beta 1-integrin adhesion complex to modulate PC12 cell adhesion. The absence of Dp71f led to a failure in the beta 1-integrin adhesion complex formation. One of the structural proteins which links the beta 1-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 beta 1-integrin complex and that a reduced expression of Dp71f induces a reduced GSK3- beta recruitment to the beta 1-integrin complex. In addition, the present work establishes that adhesion of PC12 cells to laminin does not influence the phosphorylation status of Dp71f.
doi_str_mv 10.1007/s11064-008-9802-x
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title Dp71f Modulates GSK3- beta Recruitment to the beta 1-Integrin Adhesion Complex
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