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results identify a novel role of PHLPP in regulating aPKC and cell polarity.
Low PHLPP2 expression is associated with luminal breast cancer.
miR (show MLXIP Proteins)-3117 contributes to the proliferation of HepG2 by targeting PHLPPL.
Overexpression of PHLPP2 without its 3'UTR attenuated the effects of miR (show MLXIP Proteins)-181a on cell proliferation and apoptosis in keloid fibroblast cells.
Suggest that direct PHLPP2 downregulation is required for miR (show MLXIP Proteins)-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 (show ALDH7A1 Proteins), but also elucidate a novel molecular mechanisms underlying lung inflammation and carcinogenesis upon B[a]P/B[a]PDE (show ALDH7A1 Proteins) exposure.
Results showed that PHLPP1 and PHLPP2 gene expression are down-regulated in esophageal squamous cell carcinoma. Their promotor is a target for mir (show MLXIP Proteins)-224.
Data show that both serine/threonine phosphatases PHLPP and dephosphorylated the physiological substrates of Akt1 (show AKT1 Proteins) and Akt3 (show AKT3 Proteins) with similar efficiencies.
Aberrant expression of PHLPP1 and PHLPP2 correlates with poor prognosis in patients with hypopharyngeal squamous cell carcinoma
miR (show MLXIP Proteins)-135a promotes cell proliferation in bladder cancer by targeting PHLPP2 and FOXO1 (show FOXO1 Proteins), and is performed as an onco-
PHLPP is a negative regulator of RAF1 (show RAF1 Proteins), 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