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The interaction between PPP1CC2 and AKAP4 (show AKAP4 Proteins) in human spermatozoa.
Aurkb (show AURKB Proteins) phosphorylates Oct4 (show POU5F1 Proteins)(S229) during G2/M phase, leading to the dissociation of Oct4 (show POU5F1 Proteins) from chromatin, whereas PP1 binds Oct4 (show POU5F1 Proteins) and dephosphorylates Oct4 (show POU5F1 Proteins)(S229) during M/G1 transition, which resets Oct4 (show POU5F1 Proteins)-driven transcription for pluripotency and the cell cycle.
avidity for the substrate plays an important role in imparting specificity on the PPP1R15B-PP1G-actin ternary complex.
PP1 directly interacts with IRF3 (show IRF3 Proteins) and dephosphorylates IRF3 (show IRF3 Proteins) at Ser385 and Ser396, resulting in the suppression of TLR- and RLR (show DHX58 Proteins)-triggered IFN-beta (show IFNB1 Proteins) production.
The endogenous Ppp1cc promoter normally functions in the testis to maintain a sufficient level of PPP1CC2 expression for normal spermatogenesis to occur.
In mouse testis, PPP1CC2 can form a complex with TSSK1 (show TSSK1B Proteins) mediated by the direct interaction of each with the kinase substrate protein TSKS (show TSKS Proteins). Interaction between PPP1CC2 and TSKS (show TSKS Proteins) is mediated through an RVxF docking motif on the TSKS (show TSKS Proteins) surface.
Spermatogenic defects observed in the global Ppp1cc knockout mice and in mice expressing low levels of PPP1CC2 in testis are due to compromised functions of PPP1CC2 in meiotic and postmeiotic germ cells.
The present study focused on TGF-beta (show TGFB1 Proteins)-modulation of paxillin (show PXN Proteins) and the serine/threonine protein phosphatase PP-1, and the impact on cellular motility.
Results identify protein phosphatase 1 (show PPP1CB Proteins) (PP1) as regulator of period and light-induced resetting of the mammalian circadian clock.
Thrombin (show F2 Proteins)-stimulated PP1cgamma(-/-) platelets showed decreased alpha(IIb)beta(3) activation despite comparable levels of alpha(IIb)beta(3), PAR3 (show F2RL2 Proteins), PAR4 (show F2RL3 Proteins) expression and normal granule secretion.
Data suggest that PPP1CC catalyzes hydrolysis of an assortment of substrates (aryl methylphosphonates, fluorophosphate esters, phosphorothioate esters, phosphodiesters); conservative mutation of R221 to K results in a mutant that is more effective catalyst toward monoanionic substrates; PPP1CC does not catalyze the hydrolysis of a sulfate ester, which is unexpected.
PP1gamma is upregulated in hepatocellular carcinoma (HCC (show FAM126A Proteins)) cell lines and HCC (show FAM126A Proteins) specimens and promotes cancer cell proliferation through regulation of p53 (show TP53 Proteins). High expression of PP1gamma in HCC (show FAM126A Proteins) cells contributed to doxorubicin resistance.
knock-down of PP1gamma alleviates glioma proliferation by reducing p65 (show GORASP1 Proteins) transportation into the nucleus.
Although no obvious defects in the progression of mitosis were observed, the timing of dephosphorylation of the mutant Ki67 (show MKI67 Proteins) in anaphase was delayed, indicating that Ki67 (show MKI67 Proteins) itself is one of the substrates of PP1gamma-Ki67 (show MKI67 Proteins).
the lipin-1 (show LPIN1 Proteins) N-terminal domain is important for its catalytic activity, nuclear localization, and binding to PP-1cgamma
Protein phosphatase 1gamma promotes the alternative splicing of CaMKIIdelta through its interaction with alternative splice factor.
PPP1C (show PPP1CA Proteins) isoforms have distinct contribution to the outside-in alphaIIbbeta3 signalling-dependent functions in HEK293 alphaIIbbeta3 cells.
Findings indicate that phosphatases PP1alpha (show PPP1CA Proteins) and PP1gamma are key regulators of RIG-I (show DDX58 Proteins) and MDA5 (show IFIH1 Proteins) antiviral signaling.
When the Px(T)PxR (show NR1I2 Proteins) motif is deleted or mutated via insertion of a phosphorylation site mimic (T311D), PP-1c fails to bind to all three ASPP proteins, ASPP1 (show PPP1R13B Proteins), ASPP2 (show TP53BP2 Proteins) and iASPP (show PPP1R13L Proteins).
Depletion of PP1gamma enhances the localization of the SMN (show STMN1 Proteins) complex and snRNPs to Cajal bodies.
The protein encoded by this gene belongs to the protein phosphatase family, PP1 subfamily. PP1 is an ubiquitous serine/threonine phosphatase that regulates many cellular processes, including cell division. It is expressed in mammalian cells as three closely related isoforms, alpha, beta/delta and gamma, which have distinct localization patterns. This gene encodes the gamma isozyme. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
protein phosphatase 1, catalytic subunit, gamma isoform
, serine/threonine-protein phosphatase PP1-gamma catalytic subunit
, PP1C gamma 1
, PP1C gamma 2
, protein phosphatase 1C catalytic subunit
, serine/threonine phosphatase 1 gamma
, protein serine-threonine phosphatase catalytic subunit PP-1b
, protein phosphatase type 1 catalytic subunit gamma isoform
, protein phosphatase 1 gamma 1
, protein phosphatase 1-gamma 1
, serine/threonine-protein phosphatase PP1-gamma catalytic subunit A