The Mitogen-activated Protein Kinase (MAPK) Cascades

1
The Mitogen-activated Protein Kinase (MAPK)
Cascades
SIGMA-ALDRICH
2
The Mitogen-activated Protein Kinase (MAPK)
Cascades Several MAPK cascades have been
identified in mammalian cells, including the
extracellular signal-related kinase pathways
(ERK1/2, ERK5) and the stress activated kinase
pathways (JNK/SAPK, p38 MAPK). These pathways are
linked to many G protein-linked cell surface
receptors and receptor tyrosine kinases. Thus,
most cytokines, growth factors, hormones, and
neurotransmitters can selectively activate these
cascades via receptor activation of intracellular
second messengers. All MAPK pathways operate
through sequential phosphorylation events to
phosphorylate transcription factors and regulate
gene expression. They can also phosphorylate
cytosolic targets to regulate intracellular
events. These cascades are implicated in the
regulation of cellular proliferation,
differentiation, development, cell cycle, and
transmission of oncogenic signals. Courtesy of
Rony Seger, Ph.D., Dept. Membrane Research and
Biophysics, Weizmann Institute of Science,
Rehovot, Israel. References Lowes, V.L., et al.,
Integration of signals from receptor tyrosine
kinases and G protein-coupled receptors.
Neurosignals, 11, 5-19 (2002). Tamura, S., et
al., Regulation of stress-activated protein
kinase signaling pathways by protein
phosphatases. Eur. J. Biochem., 269, 1060-1066
(2002). Seger, R., and Krebs, E.G., The MAPK
signaling cascade. FASEB J., 9, 726-735 (1995).