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The protein encoded by PLK2 is a member of the polo family of serine\\/threonine protein kinases that have a role in normal cell division.
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Structural analysis of the polo (show PLK1 ELISA Kits)-box domain of human PLK2 has been presented.
our study demonstrates a novel mechanism of PLK2 in promoting tumor progression, whereby it directly binds to enriched TAp73 (show TP73 ELISA Kits), catalyzes Ser48 phosphorylation of TAp73 (show TP73 ELISA Kits), and inhibits TAp73 (show TP73 ELISA Kits) transcriptional activity
Data suggest wild-type SNCA (alpha-synuclein (show SNCA ELISA Kits)) binding to synaptosome membrane is not affected by phosphorylation by PLK2; A30P SNCA (show SNCA ELISA Kits), a Parkinson disease mutation, binding is greatly increased; endocytosis of SNCA (show SNCA ELISA Kits) fibrils follows similar pattern.
Decreased PLK2 protein expression due to promoter hypermethylation was negatively correlated with JAK2 (show JAK2 ELISA Kits) overexpression, a common occurrence in hematological malignancies.
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.
PLK2 indirectly activates ROCK2 (show ROCK2 ELISA Kits) via phosphorylating nucleophosmin (show NPM1 ELISA Kits) during centrosome amplification.
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.
Silencing of polo-like kinase 2 increases cell proliferation and decreases apoptosis in SGC (show SGCB ELISA Kits)-7901 gastric cancer cells.
Unique PLK2-dependent protein phosphorylation sites identified by mass spectrometry.
the regulation of redox homeostasis by PLK2 promotes the survival of cells with dysfunctional mitochondria
These results support a significant role for a PLK (show PLK1 ELISA Kits) kinase in phosphorylating alpha-synuclein (show SNCA ELISA Kits) at Ser129 in the brain, and suggest that PLK2 is responsible for this activity under physiological conditions.
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.
c-Fos and polo-like kinase 2 induction is impaired in the limbic system of fear-conditioned alpha-synuclein (show SNCA ELISA Kits) transgenic mice
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.
perturbation of Plk2 disrupts Ras and Rap (show LRPAP1 ELISA Kits) signaling, prevents homeostatic shrinkage and loss of dendritic spines, and impairs proper memory formation.
CIB (show CIB1 ELISA Kits) co-immunoprecipitated with Snk (show ATP1A4 ELISA Kits) and inhibited the kinase activity of Snk (show ATP1A4 ELISA Kits), suggesting that CIB (show CIB1 ELISA Kits) is a negative regulator for Snk (show ATP1A4 ELISA Kits) kinase activity.
there is a mitotic checkpoint (show BUB3 ELISA Kits) wherein p53 (show TP53 ELISA Kits)-dependent activation of Snk/Plk2 prevents mitotic catastrophe following spindle damage
PLK2 directly phosphorylates alpha-synuclein (show SNCA ELISA Kits) at Ser (show SIGLEC1 ELISA Kits)-129 in an in vitro biochemical assay
The protein encoded by this gene is a member of the polo family of serine/threonine protein kinases that have a role in normal cell division. This gene is most abundantly expressed in testis, spleen and fetal tissues, and its expression is inducible by serum, suggesting that it may also play an important role in cells undergoing rapid cell division. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, serine/threonine-protein kinase PLK2
, serine/threonine-protein kinase SNK
, serum-inducible kinase
, polo-like kinase 2 (Drosophila)