Format

Send to

Choose Destination
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.

Author information

1
University Center of Biomedical Research, Universidad de Colima, Avenida 25 de Julio 965 Col. Villa San Sebastián, C.P. 28045, Colima, Colima, Mexico. joelcerna@ucol.mx

Abstract

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.

PMID:
18677563
DOI:
10.1007/s11064-008-9802-x
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Springer
Loading ...
Support Center