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Study reveals the mechanism controlling abscission through integration of Aurora B kinase (show AURKB Proteins) and B56-bound PP2A phosphatase activities on the kinesin motor protein (show KIF16B Proteins) MKlp2 (show KIF20A Proteins). MKlp2 (show KIF20A Proteins) 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 (show EYA3 Proteins) as a regulator of PP2A, a major cellular Ser (show SIGLEC1 Proteins)/Thr (show TRH Proteins) phosphatase, and uncovers a mechanism of controlling the stability of a critical oncogene (show RAB1A Proteins), c-Myc (show MYC Proteins).
Authors demonstrated CFTR (show CFTR Proteins) 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 (show ARPP19 Proteins) 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 (show NFKB1 Proteins) in hepatocellular carcinoma cells through impairing PP2A/I2PP2A interaction and stimulating PP2A-dependent p65 (show GORASP1 Proteins) dephosphorylation at Ser536
BIR (show KCNJ11 Proteins) domain of XIAP (show XIAP Proteins) 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 (show MAPK1 Proteins) kinases/MAPKs, their downstream effector c-Jun (show JUN Proteins); and in turn inhibiting transcription of c-Jun (show JUN Proteins)-regulated miR (show MLXIP Proteins)-200a
T-type channel signaling is redirected towards the activation of the kinase Akt1 (show AKT1 Proteins), leading to increased expression of the anti-apoptotic protein survivin (show BIRC5 Proteins), and a decrease in the pro-apoptotic mediator FoxO3A (show FOXO3 Proteins). Finally, in iPAH cells, Akt1 (show AKT1 Proteins) is no longer able to regulate caspase 9 (show CASP9 Proteins) activation, whereas T-type channel overexpression reverses PP2A defect in iPAH cells but reinforces the deleterious effects of Akt1 (show AKT1 Proteins) activation
Evidence for PPP2R4 as a haploinsufficient tumor suppressor gene, defining a high-penetrance genetic mechanism for PP2A (show PPP2R2B Proteins) inhibition in human cancer.
data indicate that PTPalpha (show PTPRA Proteins) and FAK (show PTK2 Proteins), which are enriched in FAs (show FAS Proteins), interact with IP3R1 (show ITPR1 Proteins) at adjacent ER sites to spatially sequester IL-1 (show IL1A Proteins)-induced Ca(2 (show CA2 Proteins)+) signalling
findings show that ectopic expression of the phosphotyrosyl phosphatase activator PTPA induces cell death in mammalian cells via a mechanism involving caspase-3 (show CASP3 Proteins)-dependent apoptosis
oxidative stress regulates the phosphorylation status of nonribosomal rpS3 (show RPS3 Proteins) by both activating PKCdelta (show PKCd Proteins) and blocking the PP2A (show PPP2R2B Proteins) interaction with rpS3 (show RPS3 Proteins)
results suggested that PPFIA1 (show PPFIA1 Proteins) functioned with PP2A (show PPP2R2B Proteins) to promote the dephosphorylation of Kif7, triggering Kif7 localization to the tips of primary cilia and promoting Gli (show GLI1 Proteins) 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