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Título

Deletion of the calmodulin-binding domain of Grb7 impairs cell attachment to the extracellular matrix and migration

Autor García-Palmero, Irene ; Villalobo, Antonio
Palabras clave Calmodulin
Cell migration
Cytoskeleton
Grb7
Cell adhesion
Fecha de publicación 2013
EditorElsevier
Citación Biochemical and Biophysical Research Communications 436(23): 271-277 (2013)
ResumenThe adaptor Grb7 is a calmodulin (CaM)-binding protein that participates in signaling pathways involved in cell migration, proliferation and the control of angiogenesis, and plays a significant role in tumor growth, its metastatic spread and tumor-associated neo-vasculature formation. In this report we show that deletion of the CaM-binding site of Grb7, located in the proximal region of its pleckstrin homology (PH) domain, impairs cell migration, cell attachment to the extracellular matrix, and the reorganization of the actin cytoskeleton occurring during this process. Moreover, we show that the cell-permeable CaM antagonists N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7) and N-(4-aminobutyl)-5-chloro-2-naphthalenesulfonamide (W-13) both retard the migration of cells expressing wild type Grb7, but not the migration of cells expressing the mutant protein lacking the CaM-binding site (Grb7Δ), underscoring the proactive role of CaM binding to Grb7 during this process.
URI http://hdl.handle.net/10261/113128
DOI10.1016/j.bbrc.2013.05.092
Identificadoresdoi: 10.1016/j.bbrc.2013.05.092
issn: 0006-291X
e-issn: 1090-2104
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