Basal Extracellular Signal-Regulated Kinase Activity Modulates Cell-Cell and Cell-Matrix Interactions
AUTOR(ES)
Lu, Qun
FONTE
American Society for Microbiology
RESUMO
Suppression of the basal extracellular signal-regulated kinase (ERK) activity in PC12 cells markedly altered their phenotype. Wild-type cells grew in a dissociated pattern adherent to the substrate. The stable expression of an ERK inhibitory mutant resulted in the formation of calcium-dependent aggregates which were less adherent to the substrate. Concomitantly, the cells reorganized their actin cytoskeleton and increased their expression of several adherens junction proteins, particularly cadherin. Metabolic labeling demonstrated an increased synthesis of cadherin and β-catenin in these cells. Nontransfected PC12 cells and a ras-transformed MDCK cell line also formed aggregates and increased their expression of adherens junction proteins following treatment with the selective MEK inhibitor PD98059. A peptide containing the HAV cadherin recognition sequence attenuated the aggregation. These studies suggest that in PC12 and epithelial cells, ERKs are pivotally positioned to enhance substrate interactions when active or to release homotypic interactions when suppressed.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=108907Documentos Relacionados
- Cell-cell and cell-matrix interactions differentially regulate the expression of hepatic and cytoskeletal genes in primary cultures of rat hepatocytes.
- Extracellular Signal-Regulated Kinase Activity Is Sustained Early during Human Cytomegalovirus Infection
- Extracellular signal-regulated kinase 2 is necessary for mesoderm differentiation
- Activation of extracellular signal-regulated kinase in proliferative glomerulonephritis in rats.
- Protein Kinase A and B-Raf Mediate Extracellular Signal-Regulated Kinase Activation by Thyrotropin