ArticleMolecular and cellular biochemistry2026
NDRG1-PTEN association modulates PTEN C-terminal tail phosphorylation in insulin-resistant neurons.
Article in Molecular and cellular biochemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
N-myc Downstream Regulated Gene-1 (NDRG1), implicated in the regulation of the PI3K-Akt pathway, regulates the expression of Phosphatase and TENsin homolog (PTEN), a key insulin signaling regulator. However, NDRG1's role in the insulin signaling pathway is not understood. This study aimed to clarify whether and how NDRG1 regulates PTEN C-terminal phosphorylation at residues S380/T382/T383 in the context of neuronal insulin signaling and resistance. It was found that NDRG1 associates with PTEN and regulates its phosphorylation at residues S380/T382/T383 in mouse hippocampal neurons. Co-immunoprecipitation and immunofluorescence microscopy indicated that pairwise associations between NDRG1-PTEN and Protein Phosphatase 2A (PP2A)-PTEN are upregulated by insulin stimulation and are further augmented in insulin-resistance. Deletion of the NDRG1 C-terminal region markedly reduced detectable PTEN co-immunoprecipitation, suggesting a role for this region in NDRG1-PTEN association. Silencing NDRG1 increased PTEN C-terminal phosphorylation at residues S380/T382/T383. Additionally, data from PP2A-specific inhibitor and siRNA support the involvement of PP2A in PTEN C-terminal dephosphorylation. We also utilized a phospho-dead NDRG1 mutant to demonstrate that phosphorylation of NDRG1 at T346 plays a role in the modulation of PTEN C-terminal phosphorylation. Thus, our results suggest that NDRG1 modulates PTEN C-terminal phosphorylation at residues S380/T382/T383 in neuronal cells and neuronal insulin-resistance affects this regulation by NDRG1.
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