scholarly journals Brassinosteroid Signal Transduction: From Receptor Kinase Activation to Transcriptional Networks Regulating Plant Development

2011 ◽  
Vol 23 (4) ◽  
pp. 1219-1230 ◽  
Author(s):  
Steven D. Clouse
Keyword(s):  
Signal Transduction ◽  
Plant Development ◽  
Transcriptional Networks ◽  
Receptor Kinase ◽  
Kinase Activation

scholarly journals Lysophosphatidylcholines activate G2A inducing Gαi-1-/Gαq/11- Ca2+ flux, Gβγ-Hck activation and clathrin/β-arrestin-1/GRK6 recruitment in PMNs

2010 ◽  
Vol 432 (1) ◽  
pp. 35-45 ◽  
Author(s):  
Samina Y. Khan ◽  
Nathan J. D. McLaughlin ◽  
Marguerite R. Kelher ◽  
Phillip Eckels ◽  
Fabia Gamboni-Robertson ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Subcellular Fractionation ◽  
Physical Interaction ◽  
Polymorphonuclear Leucocytes ◽  
Digital Microscopy ◽  
Receptor Kinase ◽  
Kinase Activation ◽  
Protein Receptor ◽  
Rapid Activation ◽  
Standard Techniques

Lyso-PCs (lysophosphatidylcholines) are a mixture of lipids that accumulate during storage of cellular blood components, have been implicated in TRALI (transfusion-related acute lung injury) and directly affect the physiology of neutrophils [PMNs (polymorphonuclear leucocytes)]. Because the G2A receptor, expressed on PMNs, has been reported to recognize lyso-PCs, we hypothesize that lyso-PC activation of G2A causes the increases in cytosolic Ca2+ via release of Gα and Gβγ subunits, kinase activation, and the recruitment of clathrin, β-arrestin-1 and GRK6 (G-protein receptor kinase 6) to G2A for signal transduction. PMNs were isolated by standard techniques, primed with lyso-PCs for 5–180 s, and lysed for Western blot analysis, immunoprecipitation or subcellular fractionation, or fixed and smeared on to slides for digital microscopy. The results demonstrated that lyso-PCs cause rapid activation of the G2A receptor through S-phosphorylation and internalization resulting in Gαi-1 and Gαq/11 release leading to increases in cytosolic Ca2+, which was inhibited by an antibody to G2A or intracellular neutralization of these subunits. Lyso-PCs also caused the release of the Gβγ subunit which demonstrated a physical interaction (FRET+) with activated Hck (haemopoietic cell kinase; Tyr411). Moreover, G2A recruited clathrin, β-arrestin-1 and GRK6: clathrin is important for signal transduction, GRK6 for receptor de-sensitization, and β-arrestin-1 both propagates and terminates signals. We conclude that lyso-PC activation of G2A caused release of Gαi-1, Gαq/11 and Gβγ, resulting in cytosolic Ca2+ flux, Hck activation, and recruitment of clathrin, β-arrestin-1 and GRK6.

scholarly journals Regulation of lysophosphatidic acid receptor-stimulated response by G-protein-coupled receptor kinase-2 and beta-arrestin1 in FRTL-5 rat thyroid cells

2002 ◽  
Vol 174 (1) ◽  
pp. 103-110 ◽  
Author(s):  
L Iacovelli ◽  
L Capobianco ◽  
GM D'Ancona ◽  
A Picascia ◽  
A De Blasi
Keyword(s):  
Signal Transduction ◽  
Cell Proliferation ◽  
G Protein ◽  
Pertussis Toxin ◽  
Lysophosphatidic Acid ◽  
Camp Accumulation ◽  
Receptor Kinase ◽  
Kinase Activation ◽  
Rat Thyroid ◽  
G Protein Coupled

Lysophosphatidic acid (LPA) is a naturally occurring phospholipid that activates a variety of biological activities including cell proliferation. Three mammalian LPA receptor (LPAr) subtypes have been identified by molecular cloning, named lp(A1), lp(A2) and lp(A3), that are coupled to heterotrimeric G-proteins for signal transduction. The LPAr are endogenously expressed in the rat thyroid cell line FRTL-5 and we used the FRTL-5 cells permanently transfected to obtain moderate overexpression of G-protein-coupled receptor kinase-2 (GRK2) or beta-arrestin1 to study whether GRK2 and beta-arrestin1 desensitise LPAr-mediated signalling and regulate LPA-stimulated functional effects. Using RT-PCR we documented that lp(A1), lp(A2) and lp(A3) receptors are all expressed in FRTL-5 cells. We then analysed the signal transduction of the LPAr in FRTL-5 cells. Exposure to LPA did not stimulate inositol phosphate formation nor cAMP accumulation but reduced forskolin-stimulated cAMP. LPA was also able to stimulate MAP kinase activation and this effect was abolished by pertussis toxin pretreatment. These results suggest that LPAr are mainly coupled to a pertussis toxin-sensitive G-protein in FRTL-5 cells. In order to investigate whether GRKs and arrestins are involved in the regulation of LPAr-mediated signalling, we used the FRTL-5 cell line permanently transfected to overexpress GRK2 (named L5GRK2 cells) or beta-arrestin1 (L5betaarr1 cells). The ability of LPA to inhibit forskolin-stimulated cAMP accumulation was blunted in L5GRK2 and more markedly in L5betaarr1. The MAP kinase activation was also blunted in L5GRK2 and in L5betaarr1B cells. Exposure to 20 microM LPA increased the phosphorylation of extracellular signal-regulated kinases ERK1/2 by approximately 3-fold in L5pBJI cells (FRTL-5 cells transfected with the empty vector pBJI) while it induced a modest increase in L5betaarr1 and was ineffective in L5GRK2. We measured [3H]thymidine uptake in L5betaarr1B and in L5 GRK2 cells to test whether GRK2 and beta-arrestin1 could have a role in the regulation of LPAr-mediated cell proliferation. The mitogenic response induced by 35 microM LPA was substantially blunted in L5betaarr1 (-69+/-6%) and in L5GRK2 (-69.8+/-4.5%) cells as compared with L5pBJI. Our findings document that the receptor-mediated responses elicited by LPA are regulated by GRK2 and beta-arrestin1 in FRTL-5 cells and indicate that this mechanism is potentially important for the control of the LPA-stimulated proliferative response.

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 Phosphatidylinositol-3 kinase activation induced upon Fc gamma RIIIA-ligand interaction.

1994 ◽  
Vol 179 (2) ◽  
pp. 551-558 ◽  
Author(s):  
P Kanakaraj ◽  
B Duckworth ◽  
L Azzoni ◽  
M Kamoun ◽  
L C Cantley ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Nk Cells ◽  
Protein Tyrosine Kinase ◽  
Kinase Activity ◽  
Phosphatidylinositol 3 Kinase ◽  
Ligand Interaction ◽  
Kinase Activation ◽  
Phosphorylated Proteins ◽  
Affinity Receptor ◽  
Do So

Induced activation of protein tyrosine kinase(s) is a central event in signal transduction mediated via the low affinity receptor for IgG (Fc gamma RIIIA, CD16) in natural killer (NK) cells. Tyrosine phosphorylation may affect the function of several protein directly, or indirectly by inducing their association with other tyrosine phosphorylated proteins. Here, we report that Fc gamma RIII stimulation induces activation of phosphatidylinositol (PI)-3 kinase in NK cells. Phosphotyrosine immunoprecipitates from Fc gamma RIII-stimulated NK cells contain PI-kinase activity and PI-3 kinase can be directly precipitated from them. Conversely, a series of tyrosine-phosphorylated proteins is coprecipitated with PI-3 kinase from the stimulated, but not from control cells. Analogous results obtained using Jurkat T cells expressing transfected Fc gamma RIIIA alpha ligand binding chain in association with gamma 2 or zeta 2 homodimers indicate that both complexes transduce this effect, although the Fc gamma RIIIA-zeta 2 complexes do so with greater efficiency. Accumulation of phosphoinositide D3 phosphorylated products in stimulated cells confirms PI-3 kinase activation, indicating the participation of this enzyme in Fc gamma RIIIA-mediated signal transduction.

scholarly journals BSKs Mediate Signal Transduction from the Receptor Kinase BRI1 in Arabidopsis

Science ◽  
2008 ◽  
Vol 321 (5888) ◽  
pp. 557-560 ◽  
Author(s):  
W. Tang ◽  
T.-W. Kim ◽  
J. A. Oses-Prieto ◽  
Y. Sun ◽  
Z. Deng ◽  
...  
Keyword(s):  
Signal Transduction ◽  
Receptor Kinase
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