IndraLab

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UCHL1 activates AKT. 10 / 13
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"UCHL1 activated Akt and Erk1/2, which process also required enzymatic activity and was necessary for mediating cell migration and invasion."
26018507
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"Finally, we demonstrated that overexpression of UCH-L1 led to activation of Akt as evidenced by upregulation of phosphorylated Akt."
28636190
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"Additionally, it might be possible that activation of Akt signaling by UCH-L1 [XREF_BIBR, XREF_BIBR] might also contribute to its control over p53, as Akt is an established negative regulator of p53 activity [XREF_BIBR, XREF_BIBR]."
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"Together, these data suggest UCH-L1 elicits at least some of its cellular effects through Akt dependent signaling and that stimulation of Akt by UCH-L1 is a potential mechanism of UCH-L1-mediated oncogenesis (XREF_FIG)."
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"Similarly, the deubiquitinating enzyme UCHL1 has been shown to enhance AKT pathway activation by suppressing the levels of PHLPP1 an effect found to drive the development of lymphoma in vivo [206]."
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"While UCH-L1 has been shown to inhibit alpha 2 -adrenergic receptor (AR) agonist mediated activation of ERK via a direct association with alpha 2A -AR receptor implicating a role of UCH-L1 in neuro-protection XREF_BIBR, it has also been documented that UCH-L1 up-regulates oncogenic beta-catenin and TCF and Akt signaling to induce tumor cell proliferation and migration contributing to tumor progression XREF_BIBR, XREF_BIBR."
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"Nevertheless, stimulation of Akt by UCH-L1 and the subsequent promotion of prosurvival signaling may contribute to the function of UCH-L1 in oncogenesis."
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"UCHL1 activated Akt and Erk1/2, which process also required enzymatic activity and was necessary for mediating cell migration and invasion."
26018507
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"These findings demonstrated that UCHL1 promoted cell proliferation, migration, and invasion depending on its de-ubiquitinase activity by activating Akt and Erk1/2, which may account for its higher positive expression rate in liver metastases from gastric cancer."
26018507
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"Moreover, we observed that UCHL1 promoted the degradation of p110α through autophagy, but paradoxically increased the activity of AKT, thereby promoting polarization of macrophages into pro-inflammatory states."
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