scholarly journals Microenvironment regulation of extracellular signal-regulated kinase activity in chondrocytes: Effects of culture configuration, interleukin-1, and compressive stress

2003 ◽  
Vol 48 (3) ◽  
pp. 689-699 ◽  
Author(s):  
Kelvin W. Li ◽  
Aaron S. Wang ◽  
Robert L. Sah
Keyword(s):  
Compressive Stress ◽  
Kinase Activity ◽  
Interleukin 1 ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal

scholarly journals Multiregion Quantification of Extracellular Signal-regulated Kinase Activity in Renal Cell Carcinoma

2020 ◽  
Vol 3 (3) ◽  
pp. 360-364 ◽  
Author(s):  
Christian R. Hoerner ◽  
Rustin Massoudi ◽  
Thomas J. Metzner ◽  
Laurel Stell ◽  
Jennifer J. O’Rourke ◽  
...  
Keyword(s):  
Renal Cell Carcinoma ◽  
Cell Carcinoma ◽  
Renal Cell ◽  
Kinase Activity ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal

scholarly journals Roles for TAB1 in regulating the IL-1-dependent phosphorylation of the TAB3 regulatory subunit and activity of the TAK1 complex

2008 ◽  
Vol 409 (3) ◽  
pp. 711-722 ◽  
Author(s):  
Heidi Mendoza ◽  
David G. Campbell ◽  
Kerry Burness ◽  
James Hastie ◽  
Natalia Ronkina ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Transforming Growth Factor ◽  
Interleukin 1 ◽  
Mitogen Activated Protein Kinase ◽  
Regulatory Subunit ◽  
Hek 293 ◽  
Human Embryonic Kidney Cells ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
P38α Mapk

The protein kinase TAK1 (transforming growth factor-β-activated kinase 1), which has been implicated in the activation of MAPK (mitogen-activated protein kinase) cascades and the production of inflammatory mediators by LPS (lipopolysaccharide), IL-1 (interleukin 1) and TNF (tumour necrosis factor), comprises the catalytic subunit complexed to the regulatory subunits, termed TAB (TAK1-binding subunit) 1 and either TAB2 or TAB3. We have previously identified a feedback-control mechanism by which p38α MAPK down-regulates TAK1 and showed that p38α MAPK phosphorylates TAB1 at Ser423 and Thr431. In the present study, we identified two IL-1-stimulated phosphorylation sites on TAB2 (Ser372 and Ser524) and three on TAB3 (Ser60, Thr404 and Ser506) in human IL-1R cells [HEK-293 (human embryonic kidney) cells that stably express the IL-1 receptor] and MEFs (mouse embryonic fibroblasts). Ser372 and Ser524 of TAB2 are not phosphorylated by pathways dependent on p38α/β MAPKs, ERK1/2 (extracellular-signal-regulated kinase 1/2) and JNK1/2 (c-Jun N-terminal kinase 1/2). In contrast, Ser60 and Thr404 of TAB3 appear to be phosphorylated directly by p38α MAPK, whereas Ser506 is phosphorylated by MAPKAP-K2/MAPKAP-K3 (MAPK-activated protein kinase 2 and 3), which are protein kinases activated by p38α MAPK. Studies using TAB1−/− MEFs indicate important roles for TAB1 in recruiting p38α MAPK to the TAK1 complex for the phosphorylation of TAB3 at Ser60 and Thr404 and in inhibiting the dephosphorylation of TAB3 at Ser506. TAB1 is also required to induce TAK1 catalytic activity, since neither IL-1 nor TNFα was able to stimulate detectable TAK1 activity in TAB1−/− MEFs. Surprisingly, the IL-1 and TNFα-stimulated activation of MAPK cascades and IκB (inhibitor of nuclear factor κB) kinases were similar in TAB1−/−, MEKK3−/− [MAPK/ERK (extracellular-signal-regulated kinase) kinase kinase 3] and wild-type MEFs, suggesting that another MAP3K (MAPK kinase kinase) may mediate the IL-1/TNFα-induced activation of these signalling pathways in TAB1−/− and MEKK3−/− MEFs.

scholarly journals Feedforward regulation of mRNA stability by prolonged extracellular signal-regulated kinase activity

FEBS Journal ◽  
2015 ◽  
Vol 282 (4) ◽  
pp. 613-629 ◽  
Author(s):  
Takeshi Nagashima ◽  
Norihiko Inoue ◽  
Noriko Yumoto ◽  
Yuko Saeki ◽  
Shigeyuki Magi ◽  
...  
Keyword(s):  
Mrna Stability ◽  
Kinase Activity ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal

scholarly journals Inhibition of extracellular signal-regulated kinase activity by sorafenib increases sensitivity to DNR in K562 cells

2013 ◽  
Vol 29 (5) ◽  
pp. 1895-1901 ◽  
Author(s):  
RUO-ZHI XIAO ◽  
CHENG-MING HE ◽  
MU-JUN XIONG ◽  
XING-XING RUAN ◽  
LI-LIN WANG ◽  
...  
Keyword(s):  
Kinase Activity ◽  
K562 Cells ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal
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