scholarly journals MAP kinases in plant signal transduction

1999 ◽  
Vol 55 (2) ◽  
pp. 204-213 ◽  
Author(s):  
C. Jonak ◽  
W. Ligterink ◽  
H. Hirt
Keyword(s):  
Signal Transduction ◽  
Map Kinases ◽  
Plant Signal Transduction

MAP Kinases in Plant Signal Transduction: VersatileTools for Signaling Stress, Cell Cycle, and More

2000 ◽  
pp. 67-79
Author(s):  
Claudia Jonak ◽  
Stefan Kiegerl ◽  
Wilco Ligteri ◽  
Christine Siligan ◽  
Emmanuel Baudouin ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Signal Transduction ◽  
Map Kinases ◽  
Plant Signal Transduction

scholarly journals Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors.

1996 ◽  
Vol 135 (6) ◽  
pp. 1633-1642 ◽  
Author(s):  
S Miyamoto ◽  
H Teramoto ◽  
J S Gutkind ◽  
K M Yamada
Keyword(s):  
Signal Transduction ◽  
Growth Factors ◽  
Growth Factor ◽  
Map Kinase ◽  
Tyrosine Kinases ◽  
Map Kinases ◽  
Egf Receptor ◽  
Growth Factor Receptor ◽  
Kinase Activation ◽  
Transient Activation

Integrins mediate cell adhesion, migration, and a variety of signal transduction events. These integrin actions can overlap or even synergize with those of growth factors. We examined for mechanisms of collaboration or synergy between integrins and growth factors involving MAP kinases, which regulate many cellular functions. In cooperation with integrins, the growth factors EGF, PDGF-BB, and basic FGF each produced a marked, transient activation of the ERK (extracellular signal-regulated kinase) class of MAP kinase, but only if the integrins were both aggregated and occupied by ligand. Transmembrane accumulation of total tyrosine-phosphorylated proteins, as well as nonsynergistic MAP kinase activation, could be induced by simple integrin aggregation, whereas enhanced transient accumulation of the EGF-receptor substrate eps8 required integrin aggregation and occupancy, as well as EGF treatment. Each type of growth factor receptor was itself induced to aggregate transiently by integrin ligand-coated beads in a process requiring both aggregation and occupancy of integrin receptors, but not the presence of growth factor ligand. Synergism was also observed between integrins and growth factors for triggering tyrosine phosphorylation of EGF, PDGF, and FGF receptors. This collaborative response also required both integrin aggregation and occupancy. These studies identify mechanisms in the signal transduction response to integrins and growth factors that require various combinations of integrin aggregation and ligands for integrin or growth factor receptors, providing opportunities for collaboration between these major regulatory systems.

scholarly journals Signal Transduction by the JNK Group of MAP Kinases

Cell ◽  
2000 ◽  
Vol 103 (2) ◽  
pp. 239-252 ◽  
Author(s):  
Roger J Davis
Keyword(s):  
Signal Transduction ◽  
Map Kinases

scholarly journals Molecular Identification of Cytosolic, Patatin-Related Phospholipases A from Arabidopsis with Potential Functions in Plant Signal Transduction

2002 ◽  
Vol 130 (1) ◽  
pp. 90-101 ◽  
Author(s):  
André Holk ◽  
Steffen Rietz ◽  
Marc Zahn ◽  
Hartmut Quader ◽  
Günther F.E. Scherer
Keyword(s):  
Signal Transduction ◽  
Molecular Identification ◽  
Potential Functions ◽  
Plant Signal Transduction ◽  
Phospholipases A
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