2017年6月23日 · Here, we show that extracellular signal–regulated kinases (ERK1/2) respond to insulin stimulation and integrate insulin signaling to phosphorylate and thus inactivate GSK3β, resulting in increased...

2005年7月22日 · Erk, which is activated by HBX, associates with GSK-3β through a docking motif (291 FKFP) of GSK-3β and phosphorylates GSK-3β at the 43 Thr residue, which primes GSK-3β for its subsequent phosphorylation at Ser9 by p90RSK, resulting in inactivation of GSK-3β and upregulation of β-catenin.

2017年3月27日 · The data presented here demonstrate that APP expression and neuronal exposure to oligomeric Aβ42 enhance Ras/ERK signaling cascade and glycogen synthase kinase 3 (GSK-3) activation.

2005年11月7日 · Glycogen-synthase kinase-3 (GSK-3) and extracellular signal-regulated kinase (ERK) are critical downstream signaling proteins for the PI3-kinase/Akt and...

The inhibition of MEK/ERK by U0126 attenuated the MCP-1-induced phosphorylation of GSK-3β and decreased the expression of Snail, an EMT-related transcription factor, leading to the inhibition of MCF-7 cell migration and invasion.

2022年9月2日 · GSK-3α-mediated MEK-ERK activation is a critical profibrotic signaling circuit in the injured heart, which operates independently of the canonical TGF-β1-SMAD3 pathway. Therefore, strategies to inhibit the GSK-3α-MEK-ERK signaling circuit could prevent adverse fibrosis in diseased hearts.

2008年4月4日 · FGF2 promoted the association between ERK and pGSK3beta (Tyr-216). Inhibitors for GSK3beta (TDZD and LiCl) and ERK (PD98059) protected cells from FGF2-induced apoptosis. On the other hand, inhibitors of GSK3beta, but not PD98059 decreased ERK/pGSK3beta (Tyr-216) association and caused a nuclear translocation of pERK1/2.

2006年1月1日 · Glycogen-synthase kinase-3 (GSK-3) and extracellular signal-regulated kinase (ERK) are critical downstream signaling proteins for the PI3-kinase/Akt and Ras/Raf/MEK-1 pathway, respectively, and regulate diverse cellular processes including embryonic development, cell differentiation and apoptosis.

2007年12月19日 · Here, we found that GSK-3β inhibition using GSK-3β inhibitor TDZD-8 increased the phosphorylation of GSK-3β at Ser9 site as well as the phosphorylation of ERK1/2 and Akt at Ser473 site. In this condition, GSK-3β inhibition increased MMP-9 but not MMP-2 activity in a concentration-dependent manner.

有研究报道，活化ERK在Thr43位点磷酸化可以通过90 ku核糖体S6激酶 (p90RSK)触发GSK-3β丝氨酸9 (Ser9)位点的磷酸化，导致GSK-3β失活 [10]。本研究中，干扰ENST00000452996.1表达后，ERK1/2磷酸化受到抑制，GSK3β在Ser9位点上的磷酸化随即也受到抑制，GSK-3β活性增 …