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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

PH domain and leucine rich repeat protein phosphatase 2

Top mentioned proteins: Akt, PI3K, V1a, PTEN, miR
Papers using PHLPP2 antibodies
A simplified method for quantifying cell migration/wound healing in 96-well plates
Jia W et al., In Cell Death & Disease, 2009
... PHLPP1 and PHLPP2 antibodies were purchased from Bethyl Laboratories, Inc ...
Akt blocks breast cancer cell motility and invasion through the transcription factor NFAT
Gao Tianyan et al., In Oncogene, 2004
... The anti-PHLPP1 and anti-PHLPP2 antibodies were obtained from Bethyl Laboratory (Montgomery, TX, USA) ...
Papers on PHLPP2
PHLPP2 down regulation influences nuclear Nrf2 stability via Akt-1/Gsk3β/Fyn kinase axis in acetaminophen induced oxidative renal toxicity: Protection accorded by morin.
Kakkar et al., Lucknow, India. In Food Chem Toxicol, Feb 2016
In this study, we demonstrate that acetaminophen (a classic analgesic) posit nephrotoxicity both in vitro and in vivo via PHLPP2 activation.
mTORC1-independent Raptor prevents hepatic steatosis by stabilizing PHLPP2.
Pajvani et al., New York City, United States. In Nat Commun, Dec 2015
Free Raptor levels in liver decline with age and in obesity; restoration of free Raptor levels reduces liver triglyceride content, through reduced β-TrCP-mediated degradation of the Akt phosphatase, PHLPP2.
Photoreceptor Neuroprotection: Regulation of Akt Activation Through Serine/Threonine Phosphatases, PHLPP and PHLPPL.
Anderson et al., Oklahoma City, United States. In Adv Exp Med Biol, Dec 2015
Akt signaling is known to be regulated by the serine/threonine phosphatases, PHLPP (PH domain and leucine rich repeat protein phosphatase) and PHLPPL (PH domain and leucine rich repeat protein phosphatase-like).
Suppression in PHLPP2 induction by morin promotes Nrf2-regulated cellular defenses against oxidative injury to primary rat hepatocytes.
Kakkar et al., Lucknow, India. In Redox Biol, Dec 2015
We have previously demonstrated PHLPP2-mediated suppression of Nrf2 responses during oxidant attack.
MiR-32 contributed to cell proliferation of human breast cancer cells by suppressing of PHLPP2 expression.
Ma et al., Guangzhou, China. In Biomed Pharmacother, Oct 2015
Mechanically, data from luciferase reporter assays revealed that miR-32 directly targeted to the 3'-untranslated region (3'-UTR) of PHLPP2.
Morin mitigates acetaminophen-induced liver injury by potentiating Nrf2 regulated survival mechanism through molecular intervention in PHLPP2-Akt-Gsk3β axis.
Kakkar et al., Lucknow, India. In Apoptosis, Oct 2015
The effects were observed to be a result of molecular intervention in the activity of PHLPP2, a phosphatase previously reported by us to subdue cellular Nrf2 responses via Fyn kinase activation.
PHLPP2 Downregulation Contributes to Lung Carcinogenesis Following B[a]P/B[a]PDE Exposure.
Huang et al., Wenzhou, China. In Clin Cancer Res, Sep 2015
We evaluated here the role of novel target PHLPP2 in lung inflammation and carcinogenesis upon B[a]P/B[a]PDE exposure.
MYC Drives Pten/Trp53-Deficient Proliferation and Metastasis due to IL6 Secretion and AKT Suppression via PHLPP2.
Trotman et al., New York City, United States. In Cancer Discov, Jun 2015
Here, we show that cell-cell communication by IL6 drives the AKT-MYC switch through activation of the AKT-suppressing phosphatase PHLPP2, when PTEN and p53 are lost together, but not separately.
miR-93 promotes cell proliferation in gliomas through activation of PI3K/Akt signaling pathway.
Song et al., Guangzhou, China. In Oncotarget, May 2015
We demonstrated that miR-93 activated PI3K/Akt signaling through directly suppressing PTEN, PHLPP2 and FOXO3 expression via targeting their 3'UTRs.
Expression and role of oncogenic miRNA-224 in esophageal squamous cell carcinoma.
Shi et al., Nanjing, China. In Bmc Cancer, 2014
Western blot was used to quantify the level of PH domain leucine-rich repeat protein phosphatase 1 (PHLPP1) and PHLPP2 in ESCC tissues.
Mir-135a enhances cellular proliferation through post-transcriptionally regulating PHLPP2 and FOXO1 in human bladder cancer.
Chen et al., Guangzhou, China. In J Transl Med, 2014
The expressions of p21, p27, CyclinD1, Ki67, PHLPP2 and FOXO1 are measured by Western blotting assay.
Turning off AKT: PHLPP as a drug target.
Trotman et al., San Diego, United States. In Annu Rev Pharmacol Toxicol, 2013
Pleckstrin homology domain leucine-rich repeat protein phosphatase (PHLPP) isozymes comprise a novel tumor suppressor family whose two members, PHLPP1 and PHLPP2, are deleted as frequently as PTEN in cancers such as those of the prostate.
MicroRNAs of the miR-17∼92 family are critical regulators of T(FH) differentiation.
Xiao et al., Los Angeles, United States. In Nat Immunol, 2013
Mechanistically, the miR-17∼92 family controlled the migration of CD4(+) T cells into B cell follicles by regulating signaling intensity from the inducible costimulator ICOS and kinase PI(3)K by suppressing expression of the phosphatase PHLPP2.
PHLPP-mediated dephosphorylation of S6K1 inhibits protein translation and cell growth.
Gao et al., Lexington, United States. In Mol Cell Biol, 2011
Knockdown of PHLPP1 or PHLPP2 resulted in an increase in S6K1 phosphorylation.
Ras-associating domain proteins: a new class of cyclic nucleotide-gated channel modulators.
Rajala et al., Oklahoma City, United States. In Adv Exp Med Biol, 2011
PHLPP1 and PHLPP2 have an effect on retinal rod CNG channel sensitivity.
Identification of PHLPP1 as a tumor suppressor reveals the role of feedback activation in PTEN-mutant prostate cancer progression.
Trotman et al., United States. In Cancer Cell, 2011
This genetic setting initially triggers a growth suppressive response via p53 and the Phlpp2 ortholog, and reveals spontaneous Trp53 inactivation as a condition for full-blown disease.
Mst1 is an interacting protein that mediates PHLPPs' induced apoptosis.
Pardee et al., Boston, United States. In Mol Cell, 2010
The PHLPP2 dephosphorylate Mst1 on the T387 inhibitory site, which activate Mst1 and its downstream effectors p38 and JNK to induce apoptosis.
Depletion of Pleckstrin homology domain leucine-rich repeat protein phosphatases 1 and 2 by Bcr-Abl promotes chronic myelogenous leukemia cell proliferation through continuous phosphorylation of Akt isoforms.
Ohnishi et al., Hamamatsu, Japan. In J Biol Chem, 2009
Bcr-Abl represses the expression of PHLPP1 and PHLPP2 and continuously activates Akt1, -2, and -3 via phosphorylation on Ser-473, resulting in the proliferation of CML cells
Common polymorphism in the phosphatase PHLPP2 results in reduced regulation of Akt and protein kinase C.
Newton et al., San Diego, United States. In J Biol Chem, 2009
A functional polymorphism that impairs the activity of PHLPP2 and correlates with elevated Akt phosphorylation and increased PKC levels, was identified.
PHLiPPing the switch on Akt and protein kinase C signaling.
Newton et al., San Diego, United States. In Trends Endocrinol Metab, 2008
The two isoforms of this recently discovered family, PHLPP1 and PHLPP2, control the amplitude and duration of signaling of Akt and PKC by catalyzing the dephosphorylation of the hydrophobic phosphorylation motif, a C-terminal phosphorylation switch that controls these kinases.
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