Protein tyrosine Phosphatase, Receptor Type, E Proteins (PTPRE)

Human Protein tyrosine Phosphatase, Receptor Type, E (PTPRE) interaction partners

1. these data demonstrate that HCV infection reduces PTPRE expression in the liver and peripheral blood mononuclear cell sof (show GJA1 Proteins) infected humans

2. Epidermal growth factor receptor (EGFR (show EGFR Proteins))-mediated positive feedback of protein-tyrosine phosphatase epsilon (PTPepsilon) on ERK1/2 and AKT (show AKT1 Proteins) protein pathways is required for survival of human breast cancer cells.

3. Studies indicate that RAD50 (show RAD50 Proteins) and PTPRE of crude associations with asthma at a Bonferroni-corrected level of significance, while IL4R (show IL4R Proteins), CCL5 (show CCL5 Proteins) and TBXA2R (show TBXA2R Proteins) of nominal significance.

4. Transfection of cells with different PTPepsilon constructs and activator protein-1 (show FOSB Proteins) reporter gene indicates that the catalytic activity of PTPepsilon is involved in the regulation of the mitogen-activated protein kinase (show MAPK1 Proteins) cascade.

5. Characterization, expression and functional aspects of an alternative spliced isoform of protein tyrosine phosphatase epsilon

6. interactions between RPTP-domain1s and RPTP-domain 2s are a common but specific mechanism that is likely to be regulated- domain2s and the wedge structures are crucial determinants of binding specificity, thus regulating cross-talk between RPTPs (show PTPRS Proteins)

7. Functions to prevent inappropriate activation and to terminate prolonged, rather than acute, activation of ERK (show EPHB2 Proteins) in the cytosol.

8. cyt-PTP epsilon is dimerized and phosphorylated in the absence of direct interaction between the PTP and extracellular molecules

9. Transgenic mice overexpressing catalytically inactive transmembrane protein tyrosine phosphatase epsilon provide unexpected insight into the cell-cell interactions that occur between oligodendrocytes and the cells which they myelinate.

10. Protein-tyrosine phosphatase epsilon regulates Shc signaling in a kinase-specific manner: increasing coherence in tyrosine phosphatase signaling

Mouse (Murine) Protein tyrosine Phosphatase, Receptor Type, E (PTPRE) interaction partners

1. GRB2 (show GRB2 Proteins) physically links cyt (show CYGB Proteins)-PTPe with Src (show SRC Proteins) and enables cyt (show CYGB Proteins)-PTPe to activate Src (show SRC Proteins) downstream of activated integrins in osteoclast-like cells.

2. PTPs (show PTS Proteins) alpha and epsilon play distinct roles in osteoclasts.

3. Multifaceted modulation of K+ channels by protein-tyrosine phosphatase epsilon tunes neuronal excitability.

4. Integrin activation regulates cyt (show CYGB Proteins)-PTPe via Src (show SRC Proteins)-dependent Y638 phosphorylation. cyt (show CYGB Proteins)-PTPe affects osteoclast podosome stability by a feedback loop ensuring proper Src (show SRC Proteins) activation downstream of integrins, linking their signaling with Src (show SRC Proteins) activation.

5. Findings demonstrate that PTPalpha (show PTPRA Proteins) is a critical regulator of Fyn (show FYN Proteins) activation and of specific Fyn (show FYN Proteins) signaling events during differentiation, and is essential for promoting OPC differentiation and central nervous system myelination.

6. RPTPepsilon is a physiological activator of Src in Neu-induced mammary tumors.

7. cyt-PTP epsilon is dimerized and phosphorylated in the absence of direct interaction between the PTP and extracellular molecules

8. PTPepsilon as a phosphatase required for optimal structure, subcellular organization, and function of osteoclasts

9. Receptor-like protein tyrosine phosphatase (show ACP1 Proteins) zeta/RPTP beta (show PTPRB Proteins) is expressed on tangentially aligned neurons in early mouse neocortex.

10. Protein tyrosine phosphatase epsilon activates Yes and Fyn (show FYN Proteins) in mammary tumor cells.