Premium
ERK Activation Requires CaM Kinases in MCF‐7 Breast Cancer Cells
Author(s) -
Abell Ellen,
Schmitt John M.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.699.7
Subject(s) - mapk/erk pathway , carbachol , microbiology and biotechnology , phosphorylation , kinase , chemistry , signal transduction , receptor , biology , biochemistry
A key signaling pathway involved in regulating cell growth and proliferation throughout the body is the ERK signaling pathway. ERK is activated via numerous pathways including intracellular calcium release downstream of G‐Protein Coupled Receptors (GPCRs). Carbachol, a GPCR‐agonist, both increases intracellular calcium and ERK activation in MCF‐7 cells. ERK activation and control of cell growth may act through the transcription factor Elk‐1. Our goal was to elucidate the specific proteins and kinases upstream of ERK in MCF‐7 cells treated with carbachol. Secondly, we wanted to investigate the potential involvement of Elk‐1 downstream of ERK. Carbachol treatment of MCF‐7 cells triggered ERK and Elk‐1 phosphorylation within 5 minutes. Interestingly, transfection of cells with shRNAs directed to either CaM KKα or CaM KIγ significantly inhibited carbachol activation of ERK. Phosphorylation of Elk‐1, following carbachol stimulation, was also blocked in siERK2 transfected cells, suggesting that ERK2 is required for carbachol's activation of Elk‐1. Our results suggest that carbachol treatment of MCF‐7 cells activates ERK and cell growth through CaM KK, CaMKI, and an Elk‐1‐dependent pathway.