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PHLPP2 stabilization by p27 mediates its inhibition of bladder cancer invasion by promoting autophagic degradation of MMP2 protein.
miR493 acted as a onco-miR in prostate cancer cells and promoted cell proliferation via inhibiting tumor suppresser PHLPP2 expression and activating Akt signaling pathway.
DualLuciferase activity assay demonstrated that the tumor suppressor PH domain and leucine rich repeat protein phosphatase 2 (PHLPP2) was a target of miR125b, which inhibited PHLPP2 and directly bound to the 3'untranslated region of PHLPP2, resulting in elevated Akt signaling.
MiR-141-3p targets PHLPP2 at its 3'-untranslated region.
miR135a may protect human umbilical vein endothelial cell from mechanical stretch - induced injury by inhibiting PHLPP2 to activate PI3k/Akt signaling pathway.
TMCO1 recruited the PH domain and leucine-rich repeat protein phosphatase 2 (PHLPP2) to dephosphorylate pAKT1(serine 473) (S473). Mutagenesis at S60 of the TMCO1 protein released TMCO1-induced cell-cycle arrest and restored the AKT pathway in BFTC905 cells. Stable TMCO1 (wild-type) overexpression suppressed, whereas T33A and S60A mutants recovered, tumor size in xenograft mice.
Cheliensisin A (Chel A)treatment led to PH domain and Leucine rich repeat Protein Phosphatases (PHLPP2) protein degradation and subsequently increased in c-Jun phosphorylation, which could be attenuated by inhibition of autophagy mediated by Beclin 1.
Results show that MiR-27a directly targets PHLPP2 by binding to its 3'-UTR to inhibit its expression, and that downregulation of PHLPP2 could rescue the effect of anti-miR-27a in gastric cancer cells.
miR-938 promoted CRC cell proliferation by inhibiting PHLPP2
two PHLPP isozymes, PHLPP1 and PHLPP2, were identified in a search for phosphatases that dephosphorylate Akt, and thus suppress growth factor signaling.
results identify a novel role of PHLPP in regulating aPKC and cell polarity.
Low PHLPP2 expression is associated with luminal breast cancer.
miR-3117 contributes to the proliferation of HepG2 by targeting PHLPPL.
Overexpression of PHLPP2 without its 3'UTR attenuated the effects of miR-181a on cell proliferation and apoptosis in keloid fibroblast cells.
Suggest that direct PHLPP2 downregulation is required for miR-32-induced cell proliferation of breast cancer cells.
Our studies not only first time identify PHLPP2 downregulation by lung carcinogen B[a]P/B[a]PDE, but also elucidate a novel molecular mechanisms underlying lung inflammation and carcinogenesis upon B[a]P/B[a]PDE exposure.
Results showed that PHLPP1 and PHLPP2 gene expression are down-regulated in esophageal squamous cell carcinoma. Their promotor is a target for mir-224.
Data show that both serine/threonine phosphatases PHLPP and dephosphorylated the physiological substrates of Akt1 and Akt3 with similar efficiencies.
Aberrant expression of PHLPP1 and PHLPP2 correlates with poor prognosis in patients with hypopharyngeal squamous cell carcinoma
miR-135a promotes cell proliferation in bladder cancer by targeting PHLPP2 and FOXO1, and is performed as an onco-
PHLPP2 silencing increased the phosphorylation of glycogen synthase kinase (GSK)-3beta and promoted the nuclear translocation of nuclear factor (erythroid-derived 2)-like 2 (Nrf2). In addition, PHLPP2 inhibition promoted Nrf2/antioxidant response element (ARE) transcriptional activity.
KCTD17, which is up-regulated in liver tissues of obese mice and patients with NAFLD, binds to phosphorylated PHLPP2 to target it for ubiquitin-mediated degradation; this increases expression of genes that regulate lipogenesis to promote hepatic steatosis.
PHLPP is a negative regulator of RAF1, which reduces colorectal cancer cell motility and prevents tumor progression in mice.
Protein phosphatase that mediates dephosphorylation of 'Ser-473' of AKT1, 'Ser-660' of PRKCB isoform beta-II and 'Ser- 657' of PRKCA. AKT1 regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of AKT1 triggers apoptosis and decreases cell proliferation. Also controls the phosphorylation of AKT3. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Inhibits cancer cell proliferation and may act as a tumor suppressor.
PH domain leucine-rich repeat-containing protein phosphatase 2
, PH domain and leucine rich repeat protein phosphatase 2
, PH domain leucine-rich repeat-containing protein phosphatase 2-like
, GTPase activating protein and VPS9 domains 1