Protein tyrosine Phosphatase, Non-Receptor Type 5 (Striatum-Enriched) Proteins (PTPN5)

Mouse (Murine) Protein tyrosine Phosphatase, Non-Receptor Type 5 (Striatum-Enriched) (PTPN5) interaction partners

1. STEP61 degradation is an important event in BDNF (show BDNF Proteins)-mediated effects.

2. STEP61 regulates BDNF (show BDNF Proteins) expression, with implications for cognitive functioning in CNS disorders.

3. The study provides further insight into the mechanisms of regulation of STEP61 and also offers a molecular basis for the Zn(2+)-induced sustained activation of ERK2 (show MAPK1 Proteins).

4. These results indicate that STEP61 is a novel substrate of parkin (show PARK2 Proteins), although further studies are necessary to determine whether elevated STEP61 levels directly contribute to the pathophysiology of PD.

5. Abeta (show APP Proteins) regulating STEP61 activity is mediated by Abeta (show APP Proteins) binding to alpha7 nAChRs

6. Increased STEP and calpain activation contribute to altered NMDAR (show GRIN1 Proteins) localization in an Huntington's disease mouse model.

7. genetically reducing STEP significantly diminishes seizures and restores select social and nonsocial anxiety-related behaviors in Fmr1 (show FMR1 Proteins)(KO) mice

8. the first study to identify Pyk2 (show PTK2B Proteins) as a substrate for STEP.

9. Increased STEP61 plays a role in (show APP Proteins)amyloid Abeta-mediated internalization of th (show GRIA1 Proteins)e (AMP (show GRIA2 Proteins)AR) subuni (show GRIN1 Proteins)ts GluA1/GluA2 (formerly GluR1/GluR2).

10. STEP pathway is severely downregulated in the presence of mutant huntingtin (show HTT Proteins) and may participate in compensatory mechanisms activated by striatal neurons that lead to resistance to excitotoxicity.

Human Protein tyrosine Phosphatase, Non-Receptor Type 5 (Striatum-Enriched) (PTPN5) interaction partners

1. validated the functional importance of an identified interaction network by characterizing a distinct novel interaction between PTPN5 and Mob1a (show MOBKL1B Proteins).

2. This current study demonstrated that spinal STEP61 regulated LTP (show SCP2 Proteins) of C fiber-evoked field potentials, one of the extensively studied cellular models of central sensitization.

3. a dual role for PSD-95 (show DLG4 Proteins) in stabilizing synaptic NMDARs by binding directly to GluN2B (show GRIN2B Proteins) but also by promoting synaptic exclusion and degradation of the negative regulator STEP61.

4. Data suggest that PP5 (show PPP5C Proteins)/PTPN5 is overexpressed in liver samples from patients with hepatocellular carcinoma (HCC (show FAM126A Proteins)); overexpression of PP5 (show PPP5C Proteins)/PTPN5 appears to correlate with tumor burden/stage. Inhibition of PP5 (show PPP5C Proteins)/PTPN5 suppresses proliferation and promotes apoptosis of HCC (show FAM126A Proteins) cells; inhibition of PP5 (show PPP5C Proteins)/PTPN5 involves activation of AMPK (show PRKAA1 Proteins).

5. A rare missense variant in the PTPN5 gene (rs56234898; minor allele frequency 1.5%) was significantly associated with decreased severity of Post-Burn Hypertrophic Scarring(P = 1.3x10-6).

6. The results imply a model in which PTPN5 may play a role in normal cognitive functioning and contribute to aspects of the neuropathology of schizophrenia.

7. This study identified a novel role for PTPN5 in mediating the development of stress-related cognitive and morphological changes.

8. STEP(61kDa) is required for Abeta (show APP Proteins) transgene-mediated internalization of GluA1 (show GRIA1 Proteins)/GluA2 (show GRIA2 Proteins) glutamate (show GRIN1 Proteins) receptors in a transgenic mousemodel.

9. STEP contributes to aspects of the pathophysiology in Alzheimer's disease; loss of GluN1 (show GRIN1 Proteins)/GluN2B (show GRIN2B Proteins) subunits from neuronal membranes and Abeta (show APP Proteins)-mediated NMDAR (show GRIN1 Proteins) internalization are discussed

10. determined high-resolution structures of all of the human family members of Mitogen-Activated Protein Kinase (show MAPK1 Proteins)-specific protein tyrosine phosphatases