Death-Associated Protein Kinase 2 Proteins (DAPK2)

Human Death-Associated Protein Kinase 2 (DAPK2) interaction partners

1. study reveals a unique calmodulin-independent mechanism for DAPK2 activation, critical to its function as a novel downstream effector of AMPK in autophagy

2. This study suggests that miR-520g contributes to tumor progression and drug resistance by post-transcriptionally downregulating DAPK2 in patients with epithelial ovarian cancer

3. Thyroid hormone promotes selective autophagy via induction of DAPK2-SQSTM1 cascade, which in turn protects hepatocytes from diethylnitrosamine-induced hepatotoxicity or carcinogenesis.

4. miR-520h suppresses Death-associated protein kinase 2 (DAPK2) expression, as restoring DAPK2 abolished miR-520h-promoted drug resistance, and knockdown of DAPK2 mitigated cell death caused by the depletion of miR-520h.

5. that Death-associated protein kinase 2 effector functions are influenced by the protein's subcellular localization

6. This study links adipocyte expression of an autophagy-regulating kinase, lysosome-mediated clearance and fat cell lipid accumulation; it demonstrates obesity-related attenuated autophagy in adipocytes, and identifies DAPK2 dependence in this regulation.

7. DAPK2 is a novel kinase of mTORC1 and is a potential new member of this multiprotein complex, modulating mTORC1 activity and autophagy levels under stress and steady-state conditions.

8. DAPK2 regulates oxidative stress in cancer cells by preserving mitochondrial function

9. DAPK2-induced apoptosis is negatively regulated by Akt and 14-3-3 proteins.

10. DAPK2 is upregulated in uterosacral ligaments in pelvic organ prolapse

11. The defect in chemotaxis in DAPK2-inactive granulocytes is likely a result of reduced polarization of the cells, mediated by a lack of MLC phosphorylation, resulting in radial F-actin and pseudopod formation.

12. The tumor suppressor gene DAPK2 is induced by the myeloid transcription factors PU.1 and C/EBPalpha during granulocytic differentiation but repressed by PML-RARalpha in APL.

13. DRP-1 and ZIPk most likely evolved from their ancient ancestor gene DAPk by two gene duplication events that occurred close to the emergence of vertebrates

14. Sodium butyrate induced DAPK1/2 expression in human gastric cancer cells and this expression prompted apoptosis by decreasing FAK levels.

15. High frequency of promoter hypermethylation of the death-associated protein-kinase gene in nasopharyngeal carcinoma and its detection in the peripheral blood of patients

16. distinct methylation pattern in bladder cancer with frequent methylation of RARbeta, DAPK, E-cadherin, and p16.

17. gene expression in colorectal and gastric cancer silenced by DNA methylation and histone deacetylation

18. Results implicate a novel role for DAPK2 in the regulation of normal myelopoiesis.

19. DAPK2 as a novel Sp1-dependent target gene for E2F1 and KLF6 in cell death response.

20. beta-catenin-induced down-regulation of DAPk-2 represents a novel signaling mechanism by which beta-catenin promotes the survival of malignant epithelial cells

Mouse (Murine) Death-Associated Protein Kinase 2 (DAPK2) interaction partners

1. Thyroid hormone promotes selective autophagy via induction of DAPK2-SQSTM1 cascade, which in turn protects hepatocytes from diethylnitrosamine-induced hepatotoxicity or carcinogenesis.

2. This study links adipocyte expression of an autophagy-regulating kinase, lysosome-mediated clearance and fat cell lipid accumulation; it demonstrates obesity-related attenuated autophagy in adipocytes, and identifies DAPK2 dependence in this regulation.

3. DAPK2 is strongly and specifically expressed in interstitial cells of the cortex, providing a useful marker for this important cell population

4. The defect in chemotaxis in DAPK2-inactive granulocytes is likely a result of reduced polarization of the cells, mediated by a lack of MLC phosphorylation, resulting in radial F-actin and pseudopod formation.

5. These results suggest that DAPK2 is one of the targets of cGK-I in apoptosis induction.

6. The crystal and solution structures of murine DAPK2 were determined in the presence of the autoinhibitory domain, with and without bound nucleotides in the active site. Dimers of DAPK2 had a conformation that did not permit protein substrate binding.

7. DAPK2 was substantially up-modulated during late erythropoiesis