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Hombauer, Weismann, Mudrak, Stanzel, Fellner, Lackner, Ogris: Generation of active protein phosphatase 2A is coupled to holoenzyme assembly. dans PLoS biology 2007
Show all 8 Pubmed References
PP2B-Abeta limits platelet response to vascular injury by suppressing outside-in alphaII b beta3 integrin signaling
TRPV1 activation in endothelial cells may elicit a Ca(2+) -dependent effect on PP2B-PKC signalling, which leads to dephosphorylation of eNOS
PP2A activation via rapid, non-nuclear ER signaling may be a novel target for therapeutic approaches to inhibit vascular smooth muscle proliferation, which plays a central role in atherosclerosis and restenosis.
This study provides evidence that CaBP4 is dephosphorylated by PP2A in the retina.
generated conditional null alleles of Ppp2ca and Ppp2cb by flanking with loxP sites exons 3 to 5 of Ppp2ca and exon 3 of Ppp2cb. Ppp2ca(fl/fl) mice did not display any visible phenotype
calcineurin signaling plays a critical role in regulating skeletal muscle fiber type switching but not hypertrophy
Protein phosphatase 2Ac (alpha) can negatively regulate integrin alpha(IIb)beta(3) signaling by suppressing the ERK1/2 signaling pathway
PP-2A is less abundant than PP-1 in the mouse eye and appear to be highly regulated by various regulatory subunits; the genes encoding PP-1alpha/beta, PP-2Aalpha/beta, PP-2A-Aalpha/beta, and PP-2A-B alpha/beta/gamma are all differentially expressed.
PP2A/C provides a dual inhibitory effect on Bcl2's survival function by both dephosphorylating Bcl2 and enhancing p53-Bcl2 binding.
PPP2CA may act as an oncogene in the progression of colorectal cancer
High PP2A expression is associated with Colorectal Cancer Cell Invasiveness.
PP2A overexpression is associated with lung metastasis in colorectal cancer .
Suspension survival mediated by PP2A-STAT3-Col XVII determines tumor initiation and metastasis in cancer stem cells.
alpha-Syn bound to PP2A Calpha by the hydrophobic interaction and upregulated its activity. Blocking the hydrophobic domain of alpha-Syn or hydrophilic mutation on the residue I123 in PP2A Calpha all reduced PP2A activity upregulation by alpha-Syn.
The results showed SNPs near PPP2CA were associated with decreased expression of PPP2CA mRNA in PBMCs from patients with SLE and suggested that the mRNA expression of the gene may be correlated with the pathogenesis of SLE.
This study demonstrated an association of PPP2CA (rs10491322 and rs7704116) with systemic lupus erythematosus susceptibility in a Chinese Han population. Furthermore, the minor allele of PPP2CA rs10491322 as a risk factor was correlated with immunologic disorders for systemic lupus erythematosus.
RAB9 competes with the catalytic subunit PPP2CA in binding to PPP2R1A. This competitive association has an important role in controlling the PP2A catalytic activity.
Results show that miR-199b is a tumor suppressor emerges as a potential contributing mechanism to inhibit PP2A via PP2A inhibitor SET (SET) overexpression in metastatic colorectal cancer (mCRC).
Data show that protein phosphatase-2A (PP2A) was upregulated in lung adenocarcinoma cell lines that were transfected with midline 1 E3 ubiquitin-protein ligase (MID1)-siRNA, suggesting MID1 negatively regulates PP2A in lung adenocarcinoma.
B55alpha-PP2A mutations in acute myeloid leukemia have roles in leukemogenesis by promoting AKT T308 phosphorylation and sensitivity to AKT inhibitor-induced growth arrest
This work has significantly advanced our understanding of the RACK1/PP2A complex and suggests a pro-carcinogenic role for the RACK1/PP2A interaction. This work suggests that approaches to target the RACK1/PP2A complex are a viable option to regulate PP2A activity and identifies a novel potential therapeutic target in the treatment of breast cancer.
Moreover, PP2Acalpha2-overexpressed cells demonstrated increased expression of IGBP1, activated mTORC1 signaling to reduce basal autophagy and increased anchorage-independent growth. Our study provides new insights into the complex mechanisms of PP2A regulation.
protein phosphatase 2A (PP2A)-mediated Raf-MEK-ERK signaling was involved in glutaminolysis in endothelial cells.
Studies indicate that protein phosphatase methylesterase-1 (PME-1) negatively regulates protein phosphatase 2A (PP2A) activity by highly complex mechanisms.
Binding of PP2A and Akt increased in response to cAMP or phosphatidic acid (PA), suggesting that their binding is directly responsible for the inactivation of Akt during decidualization.
Knockdown of Alpha4 preferentially impacts the expression of PP4c and PP6c compared to expression levels of PP2Ac.
these data support a role for the novel PP2Ac-CIN85 complex in supporting integrin-dependent platelet function by dampening the phosphatase activity.
PP2Ac upregulation has a poor prognostic impact on the overall survival of hepatocellular carcinoma (HCC) patients and contributes to the aggressiveness of HCC. PP2Ac may represent a potential therapeutic target for HCC.
Data show that downregulating proto-oncogene protein Akt (p-Akt) by inhibiting PP2A inhibitor SET-mediated protein phosphatase 2A (PP2A) inactivation determined the pro-apoptotic effects of EMQA and paclitaxel combination treatment.
This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. This gene encodes an alpha isoform of the catalytic subunit.
, protein phosphatase 2a, catalytic subunit, beta isoform
, serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
, protein phosphatase 2 (formerly 2A), catalytic subunit, alpha isoform
, protein phosphatase 2A catalytic subunit, alpha isoform
, replication protein C
, serine/threonine protein phosphatase 2A, catalytic subunit, alpha isoform
, serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform