anti-DEP Domain Containing 2 (DEPDC2) Antibodies

Human DEP Domain Containing 2 (DEPDC2) interaction partners

1. Study demonstrates that miR-637 inhibites melanoma cell proliferation by activation of AKT signaling pathway and induces apoptosis through regulation of Bcl-2/Bax expression via targeting P-REX2a.

2. MiR-338-3p suppresses the TNF-alpha-induced lipogenesis in sebocytes by targeting PREX2a and down-regulating PI3K/AKT signaling.

3. Data suggest that PREX1 and PREX2 share similarities in amino acid sequence, domain structure, activation by PIP(3) [phosphatidylinositol 3,4,5-triphosphate] and G-protein-coupled receptors beta/gamma subunits; expression of PREX1 and PREX2 is altered in many cancers. [REVIEW]

4. complex signaling mechanisms that involve PREX2, PI3K/AKT/PTEN and downstream epigenetic machinery to deregulate expression of key cell cycle regulators

5. PREX2 was identified as a frequently mutated gene in human melanoma. .. mutation of PREX2 can accelerate human melanoma growth.

6. The rapid tumor onset observed in this replication attempt, compared to the original study, makes the detection of accelerated tumor growth in PREX2 expressing NRAS(G12D) melanocytes extremely difficult.

7. Elevated PREX2 protein expression is associated with pathogenesis of hepatocellular carcinoma.

8. knockdown of PREX2a may effectively inhibit the malignant phenotype of glioma.

9. The results of the present study suggested that PREX2a may act as an oncogene in osteosarcoma via the inhibition of PTEN activity and activation of PI3K signaling.

10. findings identify PREX2 as a mediator of NRAS-mutant melanoma development that acts through the PI3K/PTEN/Akt pathway to regulate gene expression of a cell cycle regulator

11. second messengers activate the Rac1 signal, which sets in motion a cascade whereby PAKs phosphorylate and negatively regulate PREX2 to decrease Rac1 activation.

12. PREX2 mutants are likely selected in cancer to escape PTEN-mediated inhibition of invasion.

13. CXCL9 is involved in the invasion ability of hepatocellular carcinoma cells possibly through up-regulation of its potential effector PREX2.

14. Results demonstrate that miR-338-3p affects gastric cancer progression through PTEN-AKT signaling by targeting P-Rex2a in gastric cancer cells

15. P-REX2 PH-domain-mediated inhibition of PTEN has a role in regulating insulin sensitivity and glucose homeostasis

16. MiR-338-3p affects the PTEN/Akt pathway by down-regulating PREX2a.

17. Studies indicate relevance of P-Rex1 and P-Rex2a, in breast tumorigenesis, and suggest that the exchange factors Vav2 and Vav3 play synergistic roles in breast cancer by sustaining tumor growth, neoangiogenesis, and metastasis.

18. Analysis of whole-genome sequence data identified PREX2 (phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 2)--a PTEN-interacting protein and negative regulator of PTEN in breast cancer--as a significantly mutated gene with a mutation frequency of approximately 14% in an independent extension cohort of 107 human melanomas

19. suggests that aberrant control of PTEN by P-REX2a may represent a key tumorigenic mechanism, in agreement with recent studies supporting the pathological relevance of several other proposed PTEN regulators

20. P-REX2 may serve as a novel link between Rac activation and the PI-3 kinase pathway.

Mouse (Murine) DEP Domain Containing 2 (DEPDC2) interaction partners

1. complex signaling mechanisms that involve PREX2, PI3K/AKT/PTEN and downstream epigenetic machinery to deregulate expression of key cell cycle regulators

2. P-REX2 PH-domain-mediated inhibition of PTEN has a role in regulating insulin sensitivity and glucose homeostasis

3. This study demonistrated that the P-Rex2, a GEF that specifically activates Rac small GTPases, is expressed in a cell- and synapse-specific manner in the retina.

4. PI3K/P-Rex/Rac pathway is required for late phase long-term potentiation in the mouse cerebellum

5. P-Rex1 and P-Rex2 are important regulators of Purkinje cell morphology and cerebellar function