Polo-Like Kinase 2 (PLK2) Kits ELISA

Human Polo-Like Kinase 2 (PLK2) interaction partners

1. The phosphorylation by Plk2, like CDK5, shifts the ratio of GAP activity of synGAP to produce a greater decrease in active Ras than in active Rap, which would produce a shift toward a decrease in the number of surface AMPA receptors in neuronal dendrites.

2. The p53 dependence of Plk2 loss and tumor suppressor function in relationship to mTOR signaling may have therapeutic implications.

3. FOXD1 promoted the expression of Plk2 mRNA and protein in colorectal cancer cells.

4. we discovered that PLK2 might be inactivated in microsatellite-instability high colorectal cancers, suggesting that PLK2 could be a tumor-suppressing gene in these cancers.

5. study demonstrates that PLK-2 activity can rapidly change cellular alpha-synuclein levels in cell models and in mice brains, but this process does not require phosphorylation of S129. Instead, it operates via regulation of alpha-synuclein mRNA transcription in an open reading frame-dependent manner

6. Findings indicate the interaction network of viral oncogene HPV16 E7, miR-27b and PLK2, and support the potential strategies using antisense nucleic acid of miR-27b for therapy of cervical cancer.

7. CHOP negatively regulates Polo-like kinase 2 expression via recruiting C/EBPalpha to the upstream-promoter in human osteosarcoma cell line during ER stress

8. Plk2 represents an independent prognostic marker and regulates tumor growth and apoptosis by targeting Fbxw7/Cyclin E pathway in colorectal carcinoma.

9. PLK2 kinase has a role in mediating alpha-synuclein selective autophagic degradation

10. PLK2, functional kinase and polo-box domains were required for interaction with PFV Gag. Fluorescently-tagged PFV Gag, through its chromatin tethering function, selectively relocalized ectopically expressed eGFP-tagged PLK proteins to mitotic chromosomes i

11. Develop a DDS for continuous intracellular delivery of PLK2.

12. Structural analysis of the polo-box domain of human PLK2 has been presented.

13. our study demonstrates a novel mechanism of PLK2 in promoting tumor progression, whereby it directly binds to enriched TAp73, catalyzes Ser48 phosphorylation of TAp73, and inhibits TAp73 transcriptional activity

14. Data suggest wild-type SNCA (alpha-synuclein) binding to synaptosome membrane is not affected by phosphorylation by PLK2; A30P SNCA, a Parkinson disease mutation, binding is greatly increased; endocytosis of SNCA fibrils follows similar pattern.

15. Decreased PLK2 protein expression due to promoter hypermethylation was negatively correlated with JAK2 overexpression, a common occurrence in hematological malignancies.

16. PLK2 SNPs were associated with Alzheimer disease and mild cognitive impairment. PLK2-rs15009 CC and GG genotypes and CC genotype at PLK2-rs702723 were protective for AD.

17. PLK2 indirectly activates ROCK2 via phosphorylating nucleophosmin during centrosome amplification.

18. these findings reveal a conserved PLK2-RAP1 pathway that is crucial to regulate endothelial tip cell behavior in order to ensure proper vascular development and patterning in vertebrates.

19. Silencing of polo-like kinase 2 increases cell proliferation and decreases apoptosis in SGC-7901 gastric cancer cells.

20. Unique PLK2-dependent protein phosphorylation sites identified by mass spectrometry.

Mouse (Murine) Polo-Like Kinase 2 (PLK2) interaction partners

1. Plk2 acts as coordinator of cell proliferation and early lineage commitment in cardiac progenitor cells downstream of Yes-associated protein 1.

2. study demonstrates that PLK-2 activity can rapidly change cellular alpha-synuclein levels in cell models and in mice brains, but this process does not require phosphorylation of S129. Instead, it operates via regulation of alpha-synuclein mRNA transcription in an open reading frame-dependent manner

3. miR-146a regulates lineage negative bone marrow cell senescence and apoptosis by suppressing Plk2 expression that, in turn, activates p16Ink4a/p19Arf and p53 signaling.

4. PLK2, functional kinase and polo-box domains were required for interaction with PFV Gag. Fluorescently-tagged PFV Gag, through its chromatin tethering function, selectively relocalized ectopically expressed eGFP-tagged PLK proteins to mitotic chromosomes i

5. These results support a significant role for a PLK kinase in phosphorylating alpha-synuclein at Ser129 in the brain, and suggest that PLK2 is responsible for this activity under physiological conditions.

6. In support of a tumor suppressor function for Plk2, loss of Plk2 increased the formation of lesions in multiparous glands. Collectively, these results demonstrate a novel role for Plk2 in regulating mammary gland development.

7. c-Fos and polo-like kinase 2 induction is impaired in the limbic system of fear-conditioned alpha-synuclein transgenic mice

8. PLK2 inhibition is a tractable CNS pharmacological target that does not cause genotoxicity at doses and exposures that engage the target in the sensory retina.

9. perturbation of Plk2 disrupts Ras and Rap signaling, prevents homeostatic shrinkage and loss of dendritic spines, and impairs proper memory formation.

10. CIB co-immunoprecipitated with Snk and inhibited the kinase activity of Snk, suggesting that CIB is a negative regulator for Snk kinase activity.

11. there is a mitotic checkpoint wherein p53-dependent activation of Snk/Plk2 prevents mitotic catastrophe following spindle damage

12. Embryos of Plk2(Snk)-deficient mice show retarded growth and skeletal development late in gestation.

13. PLK2 directly phosphorylates alpha-synuclein at Ser-129 in an in vitro biochemical assay

Caenorhabditis elegans (C. elegans) Polo-Like Kinase 2 (PLK2) interaction partners

1. The authors found that SYP-4 is phosphorylated dependent on Polo-like kinases PLK-1/2. They propose a model in which Polo-like kinases recognize crossover designation and phosphorylate SYP-4 thereby stabilizing the synaptonemal complex and making chromosomes less permissive for further double-strand break formation.

2. Here we show that CHK-2 promotes pairing and synapsis by phosphorylating a family of zinc finger proteins that bind to specialized regions on each chromosome known as pairing centers, priming their recruitment of the Polo-like kinase PLK-2.

3. Polo kinases, via their polo box domains, bind to and regulate the activity of two key polarity proteins, MEX-5 and MEX-6.