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C-terminal cytoplasmic fragment of PcdhgC5 acts as a scaffold for CaMKP and CaMKI to regulate CaMKP activity.
The POPX2 phosphatase regulates cancer cell motility and invasiveness.
The binding of POPX2 (PPM1F) to mDia1 or to an mDia-containing complex greatly decreases the ability of mDia1 to activate transcription from the serum response element (SRE).
PPM1F overexpression suppressed cell proliferation and invasion and counteracted the tumour-promoting role of miR-590, but PPM1F knockdown reversed these effects.
POPX2 is a negative regulator of TAK1 signaling pathway and modulates apoptosis through the regulation of TAK1 activity.
PPM1F could work downstream of alpha9-nAchR to promote nicotine-induced carcinogenic signals. Thus, PPM1F expression could be used for prognostic diagnosis, or inhibited as a potential strategy for cancer prevention and therapy.
This study, combined with our previous findings, suggests that a single ubiquitously expressed phosphatase POPX2 influences cancer metastasis via modulating multiple biological processes including MAPK signaling and exosome cytokine secretion.
Overexpression of PPM1F is associated with metastasis of hepatocellular carcinoma.
POPX2 affects trafficking by determining the phosphorylation status of KIF3A at serine 690.
POPX2 might regulate cell motility through its regulation of the MAPK1/3, leading to changes in the cytoskeleton and cell motility.
hCaMKP activity is reversibly regulated by oxidation/reduction at Cys-359
FHOD1 and PPM1F (direct regulators of the actin cytoskeleton) were identified as novel targets of miR-200c. Expression levels of FHOD1 and PPM1F were inversely correlated with miR-200c level in breast cancer cell lines and breast cancer patient samples.
Data identify a biochemical pathway through which POPX2 exerts its apparent cellular function: the regulation of activity of glycogen synthase kinase-3, which in turn modulates extracellular signal-regulated kinase and cell motility.
The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. (POPX1; POPX2)
PPM1F plays a key role in the regulation of CaMKII intracellularly
The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase can interact with Rho guanine nucleotide exchange factors (PIX), and thus block the effects of p21-activated kinase 1 (PAK), a protein kinase mediating biological effects downstream of Rho GTPases. Calcium/calmodulin-dependent protein kinase II gamma (CAMK2G/CAMK-II) is found to be one of the substrates of this phosphatase. The overexpression of this phosphatase or CAMK2G has been shown to mediate caspase-dependent apoptosis. An alternatively spliced transcript variant has been identified, but its full-length nature has not been determined.
ca(2+)/calmodulin-dependent protein kinase phosphatase
, caM-kinase phosphatase
, calcium/calmodulin-dependent protein kinase phosphatase
, partner of PIX2
, protein phosphatase 1F
, Ca(2+)/calmodulin-dependent protein kinase phosphatase
, CaM-kinase phosphatase
, PP2C phosphatase
, partner of PIX 2
, protein fem-2 homolog
, protein phosphatase 1F (PP2C domain containing)