Publications by authors named "Didong Xie"

Background: Solute carrier (SLC) 22 A1, A2, and A3 are polyspecific transporters transporting organic cations like histamine, serotonin, norepinephrine, dopamine, MPP + , and toxins. The expression of SLC22A1-A3 in cancer is seldom investigated, and the function of SLC22A1-A3 in glioblastoma multiforme (GBM) is never elucidated.

Materials: In our study, we detected the expression of SLC22A1-A3 in 11 fresh GBMs and tumor-adjacent brain tissues with qPCR, and in 129 paraffin-embedded GBMs with immunohistochemistry (IHC).

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Striatal-enriched tyrosine phosphatase (STEP) is an important regulator of neuronal synaptic plasticity, and its abnormal level or activity contributes to cognitive disorders. One crucial downstream effector and direct substrate of STEP is extracellular signal-regulated protein kinase (ERK), which has important functions in spine stabilisation and action potential transmission. The inhibition of STEP activity toward phospho-ERK has the potential to treat neuronal diseases, but the detailed mechanism underlying the dephosphorylation of phospho-ERK by STEP is not known.

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The heavy metal cadmium is a non-degradable pollutant. By screening the effects of a panel of metal ions on the phosphatase activity, we unexpectedly identified cadmium as a potent inhibitor of PPM1A and PPM1G. In contrast, low micromolar concentrations of cadmium did not inhibit PP1 or tyrosine phosphatases.

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Article Synopsis
  • Protein phosphorylation is crucial for cell signaling, with the ERK kinase being a key player activated by phosphorylation at specific sites (Thr202 and Tyr204).
  • Phosphatases like PPM1A regulate ERK activity by dephosphorylating these sites, maintaining proper cellular function in response to external stimuli.
  • The study found that PPM1A directly targets the pThr202 position on ERK early in stimulation, highlighting specific residues that determine the efficiency and specificity of this interaction.
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