Abstract
Epidermal Growth Factor (EGF) is an important regulator of normal epithelial and carcinoma cell migration. The mechanism by which EGF induces cell migration is not fully understood. A recent report in Nature Cell Biology (Katz et al., 2007) demonstrates that EGF regulates migration through a switch in the expression of two tensin isoforms, weakening the association of beta1 integrin with the actin cytoskeleton in focal adhesions.
MeSH terms
-
Actins / metabolism
-
Breast Neoplasms / pathology
-
Cell Adhesion / physiology
-
Cell Adhesion Molecules / metabolism
-
Cell Line, Tumor
-
Cell Movement / drug effects
-
Cell Movement / physiology*
-
Cytoskeleton / metabolism
-
Epidermal Growth Factor / metabolism
-
Epidermal Growth Factor / pharmacology
-
Female
-
Focal Adhesions / physiology
-
HeLa Cells
-
Humans
-
Integrin beta1 / metabolism
-
Microfilament Proteins / chemistry
-
Microfilament Proteins / genetics
-
Microfilament Proteins / metabolism*
-
Models, Biological
-
Protein Isoforms / genetics
-
Protein Isoforms / metabolism
-
Protein Structure, Tertiary
-
Receptor, ErbB-2 / genetics
-
Receptor, ErbB-2 / metabolism
-
Tensins
Substances
-
Actins
-
Cell Adhesion Molecules
-
Integrin beta1
-
Microfilament Proteins
-
Protein Isoforms
-
Tensins
-
Epidermal Growth Factor
-
Receptor, ErbB-2