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Study reveals the mechanism controlling abscission through integration of Aurora B kinase (zeige AURKB Proteine) and B56-bound PP2A phosphatase activities on the kinesin motor protein (zeige KIF16B Proteine) MKlp2 (zeige KIF20A Proteine). MKlp2 (zeige KIF20A Proteine) is an essential protein for promoting abscission, which may regulate tethering and stabilizing of the PM to the microtubule cytoskeleton at the intercellular bridge through its previously uncharacterized lipid association motif.
These results suggest that loss of specific PP2A regulatory subunits is functionally important in breast tumourigenesis, and support strategies to enhance PP2A activity as a therapeutic approach in breast cancer.
High expression of PP2A is associated with cisplatin resistant gastric cancer.
Study identifies Eya3 (zeige EYA3 Proteine) as a regulator of PP2A, a major cellular Ser (zeige SIGLEC1 Proteine)/Thr (zeige TRH Proteine) phosphatase, and uncovers a mechanism of controlling the stability of a critical oncogene (zeige RAB1A Proteine), c-Myc (zeige MYC Proteine).
Authors demonstrated CFTR (zeige CFTR Proteine) and PP2AA interact in the cytosol, resulting in PP2A complex inactivation and increased degradation of PP2A substrates via the lysosomal/proteasome pathway.
Together, the results suggest a complex antagonistic interplay between the control of ARPP-16 (zeige ARPP19 Proteine) by MAST3 and PKA that creates a mechanism whereby cAMP mediates PP2A disinhibition.
An imbalanced regulation in protein kinases and protein phosphatases is the direct cause of tau hyperphosphorylation in Alzheimer's disease; GSK-3beta and PP2A are the most implicated. (Review)
Isoliensinine suppresses NF-kappaB (zeige NFKB1 Proteine) in hepatocellular carcinoma cells through impairing PP2A/I2PP2A interaction and stimulating PP2A-dependent p65 (zeige GORASP1 Proteine) dephosphorylation at Ser536
BIR (zeige KCNJ11 Proteine) domain of XIAP (zeige XIAP Proteine) activated the protein phosphatase 2 (PP2A) activity by decreasing the phosphorylation of PP2A at Tyr307 in its catalytic subunit, PP2A-C. Such activated PP2A prevented the deviant phosphorylation and activation of MAPK (zeige MAPK1 Proteine) kinases/MAPKs, their downstream effector c-Jun (zeige JUN Proteine); and in turn inhibiting transcription of c-Jun (zeige JUN Proteine)-regulated miR (zeige MLXIP Proteine)-200a
T-type channel signaling is redirected towards the activation of the kinase Akt1 (zeige AKT1 Proteine), leading to increased expression of the anti-apoptotic protein survivin, and a decrease in the pro-apoptotic mediator FoxO3A (zeige FOXO3 Proteine). Finally, in iPAH cells, Akt1 (zeige AKT1 Proteine) is no longer able to regulate caspase 9 (zeige CASP9 Proteine) activation, whereas T-type channel overexpression reverses PP2A defect in iPAH cells but reinforces the deleterious effects of Akt1 (zeige AKT1 Proteine) activation
Evidence for PPP2R4 as a haploinsufficient tumor suppressor gene, defining a high-penetrance genetic mechanism for PP2A (zeige PPP2R2B Proteine) inhibition in human cancer.
data indicate that PTPalpha (zeige PTPRA Proteine) and FAK (zeige PTK2 Proteine), which are enriched in FAs (zeige FAS Proteine), interact with IP3R1 (zeige ITPR1 Proteine) at adjacent ER sites to spatially sequester IL-1 (zeige IL1A Proteine)-induced Ca(2 (zeige CA2 Proteine)+) signalling
findings show that ectopic expression of the phosphotyrosyl phosphatase activator PTPA induces cell death in mammalian cells via a mechanism involving caspase-3 (zeige CASP3 Proteine)-dependent apoptosis
oxidative stress regulates the phosphorylation status of nonribosomal rpS3 (zeige RPS3 Proteine) by both activating PKCdelta (zeige PKCd Proteine) and blocking the PP2A (zeige PPP2R2B Proteine) interaction with rpS3 (zeige RPS3 Proteine)
results suggested that PPFIA1 (zeige PPFIA1 Proteine) functioned with PP2A (zeige PPP2R2B Proteine) to promote the dephosphorylation of Kif7, triggering Kif7 localization to the tips of primary cilia and promoting Gli (zeige GLI1 Proteine) transcriptional activity.
Protein phosphatase 2A is one of the four major Ser/Thr phosphatases and is implicated in the negative control of cell growth and division. Protein phosphatase 2A holoenzymes are heterotrimeric proteins composed of a structural subunit A, a catalytic subunit C, and a regulatory subunit B. The regulatory subunit is encoded by a diverse set of genes that have been grouped into the B/PR55, B'/PR61, and B''/PR72 families. These different regulatory subunits confer distinct enzymatic specificities and intracellular localizations to the holozenzyme. The product of this gene belongs to the B' family. This gene encodes a specific phosphotyrosyl phosphatase activator of the dimeric form of protein phosphatase 2A. Alternative splicing results in multiple transcript variants encoding different isoforms.
PP2A phosphatase activator
, PP2A subunit B' isoform PR53
, phosphotyrosyl phosphatase activator
, protein phosphatase 2A, regulatory subunit B' (PR 53)
, serine/threonine-protein phosphatase 2A activator
, serine/threonine-protein phosphatase 2A regulatory subunit B'
, PP2A, subunit B', PR53 isoform
, serine/threonine-protein phosphatase 2A regulatory subunit 4
, protein tyrosine phosphatase, receptor type, A
, protein phosphatase 2 regulatory subunit 4
, protein phosphatase 2A activator, regulatory subunit 4
, protein phosphatase 2A regulatory subunit 4
, protein phosphatase 2A, regulatory subunit B (PR 53)
, protein phosphatase 2 phosphatase activator L homeolog
, protein phosphatase 2A regulatory subunit 4 L homeolog