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The observations suggest a novel role of ATR (show ANTXR1 Proteins) kinase in mediating its own signal attenuation via PPM1D recruitment to chromatin as an essential mechanism for restarting the stalled forks, cell cycle re-entry and cellular recovery from replication stress.
NF-kappaB served as a positive transcriptional regulator of WIP1 to activate its expression and affect its function in colorectal cancer cells.
ese results enhance our understanding of the molecular mechanisms that govern nucleoli formation by demonstrating that PPM1D regulates nucleolar formation by regulating NPM phosphorylation status through a novel signalling pathway, PPM1D-CDC25C-CDK1-PLK1
These data support the notion that Wip1 contributes to the formation of the ERMs in PDR membranes via NF-kappaB (show NFKB1 Proteins) signaling.
In an in vitro model of the blood-brain barrier, LPS (show IRF6 Proteins) raised Wip1 expression. Wip1 knockdown increased permeability and decreased transepithelial electrical resistance, protein expression of ZO-1 (show TJP1 Proteins), and occluding. Wip1 silencing augmented TNF-alpha (show TNF Proteins), IL-1beta (show IL1B Proteins), IL-12 (show IL12A Proteins), and IL-6 (show IL6 Proteins). Sonic hedgehog (show SHH Proteins) signaling was activated by Wip1 overexpression and inhibited by silencing. Wip1 may protect the BBB against LPS (show IRF6 Proteins) damage via SHH (show SHH Proteins) signal...
Studies suugest Wip1 role in tumorigenesis through regulation of p53 (show TP53 Proteins) and p38MAPK (show MAPK14 Proteins) pathways.
The inhibition of Wip1 might fortify p53 (show TP53 Proteins)-mediated tumor suppression by Mdm2 (show MDM2 Proteins) antagonists.
Wip1 suppressed ovarian cancer cell invasion, migration, epithelial to mesenchymal transition (EMT (show ITK Proteins)), and ovarian cancer metastasis in xenograft animal models.
model reproduces the observed cellular phenotypes in experiments: oscillatory (for low DNA damage) regulated by negative feedback loops involving mainly p53 (show TP53 Proteins) and Mdm2 (show MDM2 Proteins) and apoptotic or senescent (for high DNA damage) regulated by the positive p53 (show TP53 Proteins)/Wip1/miR-16 (show GDE1 Proteins) feedback loop
This suggests an important cross-talk between SHH and WIP1 pathways that accelerates tumorigenesis and supports WIP1 inhibition as a potential treatment strategy for MB.
Obtained results suggest that Wip1 deficiency sensitizes cells to sodium butyrate and to MEK (show MDK Proteins)/ERK (show EPHB2 Proteins) inhibitors independently from Wip1 main target protein - p53 (show TP53 Proteins). Data acquired give insights into role of Wip1 in cellular responses to treatment with HDAC (show HDAC3 Proteins) and MEK (show MDK Proteins)/ERK (show EPHB2 Proteins) inhibitors.
Wip1 modulates macrophage migration and phagocytosis via Rac1-GTPase (show RACGAP1 Proteins) and PI3K/AKT (show AKT1 Proteins) signalling pathways.
The results suggest that Wip1 could protect the heart from MI-induced ischemic injury.
These data collectively indicate that Wip1 modulates host sensitivity to colitis by intrinsically regulating immune cells.
Wip1 phosphatase plays a vital role in regulating hippocampal synaptic plasticity by modulating the phosphorylation of CaMKII (show CAMK2G Proteins).
Findings indicate that the PPM1D-Ulk1 (show ULK1 Proteins) axis plays a pivotal role in genotoxic stress-induced autophagy.
WIP1 phosphatase plays a pro-adipogenic role by interacting directly with PPARgamma (show PPARG Proteins) and dephosphorylating p-PPARgamma (show PPARG Proteins) S112 in vitro and in vivo.
this study shows that knock out of Wip1 in mouse aggravates colonic inflammation and increases neutrophils migration
the data indicate that the WIP1 phosphatase functions to maintain insulin (show INS Proteins) sensitivity and glucose homeostasis.
The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. The expression of this gene is induced in a p53-dependent manner in response to various environmental stresses. While being induced by tumor suppressor protein TP53/p53, this phosphatase negatively regulates the activity of p38 MAP kinase, MAPK/p38, through which it reduces the phosphorylation of p53, and in turn suppresses p53-mediated transcription and apoptosis. This phosphatase thus mediates a feedback regulation of p38-p53 signaling that contributes to growth inhibition and the suppression of stress induced apoptosis. This gene is located in a chromosomal region known to be amplified in breast cancer. The amplification of this gene has been detected in both breast cancer cell line and primary breast tumors, which suggests a role of this gene in cancer development.
protein phosphatase 1D
, protein phosphatase 1D magnesium-dependent, delta isoform
, protein phosphatase 2C delta isoform
, protein phosphatase Wip1
, wild-type p53-induced phosphatase 1
, p53-induced protein phosphatase 1
, protein phosphatase 2C isoform delta
, protein phosphatase magnesium-dependent 1 delta
, protein phosphatase, Mg2+/Mn2+ dependent 1D L homeolog
, protein phosphatase, Mg2+/Mn2+ dependent, 1D
, protein phosphatase 1D magnesium-dependent, delta