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The protein encoded by PTP4A2 belongs to a small class of the protein tyrosine phosphatase (PTP) family.
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a critical role for PRL2 phosphatase in mediating Notch and c-Kit signals in early T cell progenitors, is reported.
Oncogenic PRL-2 controls tumor growth by modulating intracellular magnesium levels through binding with the CNNM3 (show CNNM3 Proteins) magnesium transporter.
PTP4A2 plays critical roles in regulating hematopoietic stem cell self-renewal and mediating SCF (show KITLG Proteins)/KIT signaling.
PRL2 promotes Kit-mediated PI3K/Akt signaling by reducing the level of PTEN that normally antagonizes the pathway.
Phosphatase of regenerating liver 2 (PRL2) is essential for placental development by down-regulating PTEN (Phosphatase and Tensin (show TNS1 Proteins) Homologue Deleted on Chromosome 10) and activating Akt (show AKT1 Proteins) protein
identified a critical role for PRL2 phosphatase in the proliferation and survival of human AML cells. Further, we demonstrated that PRL2 is essential for the leukemogenic potential of AML1-ETO9a in vivo
Our findings highlight the important role of miR (show MLXIP Proteins)-29c in regulating CRC (show CALR Proteins) EMT (show ITK Proteins) via GSK-3b/b-catenin signaling by targeting GNA13 (show GNA13 Proteins) and PTP4A and provide new insights into the metastatic basis of colorectal cancer
PTP4A2 expression is correlated with overall survival in progestin receptor-positive breast carcinomas.
Results suggest that TRP32 (show TXNL1 Proteins) maintains the reduced state of PRL (show PRL Proteins) and thus regulates the biological function of PRL (show PRL Proteins).
Studies indicate that PRL-1 (show PLRG1 Proteins) and PRL-2 and PRL-3 are oncogenes and belong to the few phosphatases that lead to the development of cancer.
Results suggest a model in which PRL-2 promotes cell migration and invasion through an ERK1/2-dependent signaling pathway.
PRL-2 plays an important role in lung cancer and can be a biomarker of lung cancer, substituting for the function of other PRLs.
Overexpression of the protein tyrosine phosphatase (show ACP1 Proteins) PRL-2 correlates with breast tumor formation and progression.
Mouse pre-B-cells transfected with human PRL-2 had higher growth responses to Epo (show EPO Proteins) or IL-3 (show IL-3 Proteins), shorter cell cycle, less Epo (show EPO Proteins) requirement for survival, more cell migration, less cell adhesion, change to an immature cell morphology, & more Bmi-1 (show BMI1 Proteins) expression.
PRL-2 can promote cell adhesion and invasion activity of human hepatocellular carcinoma cells.
The protein encoded by this gene belongs to a small class of the protein tyrosine phosphatase (PTP) family. PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. PTPs in this class contain a protein tyrosine phosphatase catalytic domain and a characteristic C-terminal prenylation motif. This PTP has been shown to primarily associate with plasmic and endosomal membrane through its C-terminal prenylation. This PTP was found to interact with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), and thus may function as a regulator of GGT II activity. Overexpression of this gene in mammalian cells conferred a transformed phenotype, which suggested its role in tumorigenesis. Alternatively spliced transcript variants have been described. Related pseudogenes exist on chromosomes 11, 12 and 17.
, protein tyrosine phosphatase type IVA 2
, protein tyrosine phosphatase 4a2
, protein tyrosine phosphatase type IVA, member 2
, protein-tyrosine phosphatase 4a2
, protein-tyrosine phosphatase of regenerating liver 2
, phosphatase of regenerating liver 2
, protein tyrosine phosphatase IVA
, protein tyrosine phosphatase IVA2