Tomas Vomastek — Biochemistry & Redox Biology Seminar Series
“MAPK/ERK Signaling in Cell Migration”
4:00 pm –
5:00 pm
Beadle Center
Room: N172
1901 Vine St
Lincoln NE 68503
Lincoln NE 68503
Additional Info: BEAD
Contact:
Carol Hegel, (402) 472-2932, chegel@unl.edu
Dr. Tomas Vomastek, Institute of Microbiology, Academy of Sciences of the Czech Republic, will present the seminar “MAPK/ERK Signaling in Cell Migration” on Tues., Oct. 22, 2013 at 4:00 PM in N172 Beadle Center.
The ERK signaling cascade, comprised of protein kinases Raf, MEK and ERK, is an integral part of evolutionarily conserved signaling cascades that enable eukaryotic cells to sense and read a multitude of extracellular signals. ERK signaling converts extracellular signals into a variety of specific intracellular biological responses such as cell differentiation, cell movement and cell proliferation. Extracellular stimuli activate Raf which phosphorylates and activates MEK which in turn phosphorylates and activates ERK. ERK is a key regulator of intracellular responses as at the level of ERK the linear cascade splits into separate signaling branches that enable ERK to phosphorylates plethora of substrates ultimately bringing about adequate biological response.
We investigate the basic concept by which ERK signaling regulates cell migration, an important process in many physiological and pathological events like embryonic development, wound healing and the dissemination of cancer disease. We focus on the role of ERK in two related areas, the establishment of migratory polarity of adhering cells and conversion of static epithelium to autonomously migrating mesenchymal-like cells. We identified several candidate ERK substrates involved in the regulation of these processes. Our data suggest that ERK regulates cell migration through the control of activity of multiple substrates rather than through the control of a single master effector protein.
The ERK signaling cascade, comprised of protein kinases Raf, MEK and ERK, is an integral part of evolutionarily conserved signaling cascades that enable eukaryotic cells to sense and read a multitude of extracellular signals. ERK signaling converts extracellular signals into a variety of specific intracellular biological responses such as cell differentiation, cell movement and cell proliferation. Extracellular stimuli activate Raf which phosphorylates and activates MEK which in turn phosphorylates and activates ERK. ERK is a key regulator of intracellular responses as at the level of ERK the linear cascade splits into separate signaling branches that enable ERK to phosphorylates plethora of substrates ultimately bringing about adequate biological response.
We investigate the basic concept by which ERK signaling regulates cell migration, an important process in many physiological and pathological events like embryonic development, wound healing and the dissemination of cancer disease. We focus on the role of ERK in two related areas, the establishment of migratory polarity of adhering cells and conversion of static epithelium to autonomously migrating mesenchymal-like cells. We identified several candidate ERK substrates involved in the regulation of these processes. Our data suggest that ERK regulates cell migration through the control of activity of multiple substrates rather than through the control of a single master effector protein.