Protein Phosphatase, Mg2+/Mn2+ Dependent, 1A Proteine (PPM1A)

Human Protein Phosphatase, Mg2+/Mn2+ Dependent, 1A (PPM1A) Interaktionspartner

1. Enzyme kinetics of PPM1Acat toward a phosphopeptide substrate supported a random-order, bi-substrate mechanism, with substantial interaction between the bound substrate and the labile metal ion

2. PPM1A as a negative threshold regulator of M1-type monocyte-to-macrophage differentiation.

3. Here the authors establish PPM1A as a checkpoint target used by Mycobacterium tuberculosis to suppress macrophage apoptosis. Overproduction of PPM1A suppressed apoptosis of Mycobacterium tuberculosis-infected macrophages by a mechanism that involves inactivation of the c-Jun N-terminal kinase (JNK).

4. Present study suggests that HBx-induced degradation of PPM1a is a novel mechanism for over-activation of TGF-beta pathway in HCC development.

5. Findings show that HCV infection and replication decreased PPM1A abundance, mediated by NS3, in hepatoma cells. Compared to normal liver tissues, the expression of PPM1A was significantly decreased in the HCC tumor tissues and adjacent non-tumor tissues through its regulation by NS3 which promotes its ubiquitination and proteasomal degradation.

6. These data suggest that PPM1A, which had previously been shown to play a role in the antiviral response to Herpes Simplex virus infection, also governs the antibacterial response of macrophages to bacteria, or at least to Mycobacterium tuberculosis infection

7. establish PPM1A as a novel repressor of the SMAD3 pathway in renal fibrosis

8. Report a tumor-suppressive function of PPM1A and an independent relationship to Smad4 in pancreatic ductal adenocarcinoma.

9. hydrogen/deuterium exchange-mass spectrometry and molecular dynamics to characterize conformational changes in PP2Calpha between the active and inactive states

10. In a nested case control study of ischemic stroke, there was an epigenome-wide association for cg04985020 (PPM1A; P=1.78x10(-07)) with vascular recurrence in patients treated with aspirin.

11. findings demonstrate a novel regulatory circuit in which STING and TBK1 reciprocally regulate each other to enable efficient antiviral signaling activation, and PPM1A dephosphorylates STING and TBK1

12. The TGF-beta/Smad signaling system decreases its activity through strong negative regulation. We provide evidence for a new negative feedback loop through PPM1A upregulation.

13. Loss of PPM1A is associated with the development of tumor invasion in bladder cancer patients.

14. PPM1A is a RelA phosphatase that regulates NF-kappaB activity and that PPM1A has tumor suppressor-like activity.

15. a nuclear envelope-localized mechanism of inactivating TGF-beta signaling in which MAN1 competes with transcription factors for binding to Smad2 and Smad3 and facilitates their dephosphorylation by PPM1A.

16. phosphatase activity toward phosphopeptide substrates by PP2Calpha and Wip1 requires the binding of a Mg(2)+ ion to the low-affinity site.

17. PPM1A negatively regulates ERK by directly dephosphorylating its pThr202 position early in epidermal growth factor stimulation. Additional kinetic studies reveal that key residues participate in phospho-ERK recognition by PPM1A.

18. Studies indicate that phosphatase PPM1G is a component of the spliceosome and binds to protein YB-1 to affect alternative splicing.

19. PPM1A inhibits HIV-1 infection and gene expression. PPM1A depletion in resting CD4+ T cells increases HIV-1 gene expression.

20. High expression of LMP2 and low expression of PPM1A might play an important role in the motility and invasiveness of trophoblast cells and malignant transformation of hydatidiform mole.

Mouse (Murine) Protein Phosphatase, Mg2+/Mn2+ Dependent, 1A (PPM1A) Interaktionspartner

1. VRK1 self-represses its activity to phosphorylate PXR through cyclin-dependent kinase 2 (CDK2) in high glucose conditions, resulting in the repression of the PCK1 gene. This PXR phosphorylation was also observed in fasting mouse livers. Thus, the VRK1-CDK2-PXR-PP2Calpha-SGK2 pathway can be a novel physiological cell signaling that regulates gluconeogenesis in response to glucose.

2. findings demonstrate a novel regulatory circuit in which STING and TBK1 reciprocally regulate each other to enable efficient antiviral signaling activation, and PPM1A dephosphorylates STING and TBK1

3. the studies presented here position PPM1A as a new player in the wound healing-inflammation-angiogenesis axis in mouse, reveal its crucial role in homeostasis on injury, and highlight its potential as a therapeutic mediator in pathologic conditions

4. a nuclear envelope-localized mechanism of inactivating TGF-beta signaling in which MAN1 competes with transcription factors for binding to Smad2 and Smad3 and facilitates their dephosphorylation by PPM1A.

5. Although a non-myristoylated mutation (G2A) of PPM1A and PPM1B prevented membrane association, this relocalization did not likely cause the decreased activity towards AMPKalpha.

6. we found that PPM1A mRNA is synthesized at the beginning of the maturation process and remains elevated in the mature oocytes, promoting the accumulation of PPM1A protein

7. Protein phosphatase PPM1A regulates the nuclear export of Smad2/3 through targeting nuclear exporter RanBP3.

8. Ppm1a, through suppressing Smad2 signaling, plays a critical role in re-epithelialization during wound healing

9. Molecular cloning and expression analysis of MPP alpha-2, a novel transcript detected in a differential screen of pituitary libraries (MPPalpha 2)

10. Protein phosphatase 1alpha is required for lung growth and morphogenesis.

11. These data suggest that up-regulation of potassium-chloride cotransport in transgenic mouse red cells is mainly secondary to oxidative damage.