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Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. Additionally we are shipping PPP4C Antibodies (125) and and many more products for this protein.
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Protein phosphatase 4 cooperates with Smads to promote BMP signaling in dorsoventral patterning of zebrafish embryos
PP4 (show ANXA5 Proteins) regulates breast cancer cell survival and identifies a novel PP4c-PEA15 (show PEA15 Proteins) signalling axis in the control of breast cancer cell survival.
Knockdown of Alpha4 preferentially impacts the expression of PP4c and PP6c (show PPP6C Proteins) compared to expression levels of PP2Ac (show PPP2CA Proteins).
Data show that protein phosphatase 4 catalytic subunit (PP4C) knockdown decreases glioma cell proliferation.
mutual regulatory mechanisms exist between PP4 (show ANXA5 Proteins) and SAF-A (show HNRNPU Proteins). Interactions between PP4 (show ANXA5 Proteins) and SAF-A (show HNRNPU Proteins) played a role in prometaphase/metaphase transition.
These data suggested a potential role of PP4C in tumor progression.
Stathmin plays an essential role of in Merkel cell polyomavirus small tumor antigen-mediated microtubule destabilization and cell motility and this process is regulated by cellular phosphatase catalytic subunit of protein phosphatase 4.
PP4 (show ANXA5 Proteins) and Wip1 (show PPM1D Proteins) are differentially required to counteract the p53 (show TP53 Proteins)-dependent cell cycle arrest in G1 and G2, by antagonizing early or late p53 (show TP53 Proteins)-mediated responses, respectively
Results show PP4C as a fostriecin-sensitive phosphatase and demonstrate that the suppression of PP4C triggers mitotic slippage/apoptosis.
Data indicate that the major phosphatase responsible for dephosphorylation of of BAF (show BANF1 Proteins) Ser (show SIGLEC1 Proteins)-4 to be protein phosphatase 4 catalytic subunit.
Recombinant gamma-tubulin (show TUBG1 Proteins) can be phosphorylated by Cdk1 (show CDK1 Proteins)-cyclin B or Brsk1 (show BRSK1 Proteins) and dephosphorylated by Ppp4c-R2-R3A in vitro.
LCMT-1 (show LCMT1 Proteins) homozygous knock-out MEFs exhibited hyperphosphorylation of HDAC3 (show HDAC3 Proteins), a reported target of the methylation-dependent PP4R1 (show PPP4R1 Proteins)-PP4c complex. Collectively, our data suggest that LCMT-1 (show LCMT1 Proteins) coordinately regulates the carboxyl methylation of PP2A (show PPP2R2B Proteins)-related phosphatases and, consequently, their holoenzyme assembly and function.
T cell-specific ablation of PP4 (show ANXA5 Proteins) resulted in defective adaptive immunity, impaired T cell homeostatic expansion, and inefficient T cell proliferation.
Data show that protein phosphatase 4 (PP4 (show ANXA5 Proteins)) is an important regulator in inflammatory related insulin (show INS Proteins) resistance.
Thus, serine/threonine phosphatase PP4 (show ANXA5 Proteins) functions as a novel feedback negative regulator of RNA virus-triggered innate immunity.
Taken together, our results establish a novel role for PP4 (show ANXA5 Proteins) in CSR (show SCARA3 Proteins), and reveal crucial functions for PP4 (show ANXA5 Proteins) in the maintenance of genomic stability, GC formation, and B cell-mediated immune responses.
PP4 (show ANXA5 Proteins) overexpression was observed to lead to a decreased pACC1Ser79/ACC1 (show ACACA Proteins) ratio and subsequently an increased intracellular triglyceride content in mouse primary hepatocytes.
Mammalian SMEK/PP4C proteins are involved in the regulation of hepatic glucose metabolism through dephosphorylation of CRTC2 (show CRTC2 Proteins).
Protein phosphatase 4 has a role in apoptosis.
PP4 is essential for thymocyte development and pre-TCR signaling
PP4 (show ANXA5 Proteins) negatively regulated LPS (show TLR4 Proteins)-induced and TRAF6 (show TRAF6 Proteins)-mediated NF-kappaB (show NFKB1 Proteins) activation by inhibiting the ubiquitination of TRAF6 (show TRAF6 Proteins).
Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C- PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on Ser-140 (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase (By similarity). In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin.
protein phosphatase 4, catalytic subunit
, catalytic subunit
, serine/threonine-protein phosphatase 4 catalytic subunit A
, protein phosphatase 4 (formerly X), catalytic subunit
, protein phosphatase X, catalytic subunit
, serine/threonine-protein phosphatase 4 catalytic subunit
, protein phosphatase X