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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. De plus, nous expédions PPP4C Anticorps (125) et et beaucoup plus de produits pour cette protéine.
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Protein phosphatase 4 cooperates with Smads to promote BMP signaling in dorsoventral patterning of zebrafish embryos
PP4 (Montrer ANXA5 Protéines) regulates breast cancer cell survival and identifies a novel PP4c-PEA15 (Montrer PEA15 Protéines) signalling axis in the control of breast cancer cell survival.
Knockdown of Alpha4 preferentially impacts the expression of PP4c and PP6c (Montrer PPP6C Protéines) compared to expression levels of PP2Ac (Montrer PPP2CA Protéines).
Data show that protein phosphatase 4 catalytic subunit (PP4C) knockdown decreases glioma cell proliferation.
mutual regulatory mechanisms exist between PP4 (Montrer ANXA5 Protéines) and SAF-A (Montrer HNRNPU Protéines). Interactions between PP4 (Montrer ANXA5 Protéines) and SAF-A (Montrer HNRNPU Protéines) 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 (Montrer ANXA5 Protéines) and Wip1 (Montrer PPM1D Protéines) are differentially required to counteract the p53 (Montrer TP53 Protéines)-dependent cell cycle arrest in G1 and G2, by antagonizing early or late p53 (Montrer TP53 Protéines)-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 (Montrer BANF1 Protéines) Ser (Montrer SIGLEC1 Protéines)-4 to be protein phosphatase 4 catalytic subunit.
Recombinant gamma-tubulin (Montrer TUBG1 Protéines) can be phosphorylated by Cdk1 (Montrer CDK1 Protéines)-cyclin B or Brsk1 (Montrer BRSK1 Protéines) and dephosphorylated by Ppp4c-R2-R3A in vitro.
LCMT-1 (Montrer LCMT1 Protéines) homozygous knock-out MEFs exhibited hyperphosphorylation of HDAC3 (Montrer HDAC3 Protéines), a reported target of the methylation-dependent PP4R1 (Montrer PPP4R1 Protéines)-PP4c complex. Collectively, our data suggest that LCMT-1 (Montrer LCMT1 Protéines) coordinately regulates the carboxyl methylation of PP2A (Montrer PPP2R2B Protéines)-related phosphatases and, consequently, their holoenzyme assembly and function.
T cell-specific ablation of PP4 (Montrer ANXA5 Protéines) resulted in defective adaptive immunity, impaired T cell homeostatic expansion, and inefficient T cell proliferation.
Data show that protein phosphatase 4 (PP4 (Montrer ANXA5 Protéines)) is an important regulator in inflammatory related insulin (Montrer INS Protéines) resistance.
Thus, serine/threonine phosphatase PP4 (Montrer ANXA5 Protéines) functions as a novel feedback negative regulator of RNA virus-triggered innate immunity.
Taken together, our results establish a novel role for PP4 (Montrer ANXA5 Protéines) in CSR (Montrer SCARA3 Protéines), and reveal crucial functions for PP4 (Montrer ANXA5 Protéines) in the maintenance of genomic stability, GC formation, and B cell-mediated immune responses.
PP4 (Montrer ANXA5 Protéines) overexpression was observed to lead to a decreased pACC1Ser79/ACC1 (Montrer ACACA Protéines) 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 (Montrer CRTC2 Protéines).
Protein phosphatase 4 has a role in apoptosis.
PP4 is essential for thymocyte development and pre-TCR signaling
PP4 (Montrer ANXA5 Protéines) negatively regulated LPS (Montrer TLR4 Protéines)-induced and TRAF6 (Montrer TRAF6 Protéines)-mediated NF-kappaB (Montrer NFKB1 Protéines) activation by inhibiting the ubiquitination of TRAF6 (Montrer TRAF6 Protéines).
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