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Study shows that cnn exon1A-encoded proteins interact with Polo at 2 residues and that this interaction is required for polar body and pericentriolar matrix formation in syncytial embryos.
Cdk1 (show CDK1 ELISA Kits) phosphorylates the conserved centriole protein Sas-4 during mitosis. This creates a Polo-docking site that helps recruit Polo to daughter centrioles.
Polo is an important in vivo regulator of the pathological functions of APP (show APP ELISA Kits).
Both conditions impaired NSC lineage progression. Ca(2 (show CA2 ELISA Kits)) mito homeostasis is influenced by Polo-mediated phosphorylation of a conserved residue in Miro
During pericentriolar matrix formation exon 1A Cnn-Long Form proteins likely bind Polo kinase before phosphorylation by Polo for Cnn transport to the centrosome.
Polo kinase is required for localization and activity of the chromosomal passenger complex in mitosis and meiosis.
Centrioles, which usually separate during the anaphase of the first meiosis, remained held together in a V-shaped configuration suggesting that Polo kinase regulates the proteolysis that breaks centriole linkage to ensure their disengagement.
Results show that Polo kinase positively and negatively regulates Augmin distribution for microtubule nucleation and acentrosomal spindle formation.
Regulation of Polo by Aurora B (show AURKB ELISA Kits) and Map205 is required for cytokinesis.
These data indicate APC (show APC ELISA Kits)(Cort (show CORT ELISA Kits)) ubiquitylates Mtrm at the oocyte-to-embryo transition, thus preventing excessive inhibition of Polo kinase activity due to Mtrm's presence.
Novel roles for Plk and GSK3 (show GSK3b ELISA Kits) regulation of ADAM13 (show ADAM33 ELISA Kits) function in cranial neural crest cell migration.
Plx1-mediated degradation of Bora in interphase generates oscillations in Plx1 activity and is essential for development.
Coordinated interplays between Plx1 and Gwl (show MASTL ELISA Kits) are required for reactivation of these kinases from the G(2)/M DNA damage checkpoint and efficient checkpoint recovery.
the penultimate CRS (show CARS ELISA Kits) serine (Ser (show SIGLEC1 ELISA Kits) 101) of cyclin b1 (show CCNB1 ELISA Kits) is a Plx substrate
Results suggest that polo-like kinase (Plx1) could be the missing regulator that prevents maturation-promoting factor autoamplification in stage IV oocytes.
Plx1 cooperates with CaMKII (show CAMK2G ELISA Kits) to regulate cyclosome regulators, and is necessary for release of cytostatic factor metaphase arrest and sufficient when overexpressed.
Data show that Plx1 couples tension signals to cellular responses through phosphorylation of the 3F3 (show TRIM32 ELISA Kits)/2 epitope and targeting structural and checkpoint proteins to kinetochores.
Polo-like kinase Plx1 is an essential factor for calcium ion-induced meiotic exit during cytostatic factor arrest
Polo-like kinase (Plx1) phosphorylates xTRF1 in vitro and the mitotic xTRF1-chromatin association was significantly impaired when Plx1 was immunodepleted from the extracts (Plx1).
Cdk1 (show CDK1 ELISA Kits) phosphorylation of BubR1 (show BUB1B ELISA Kits) controls spindle checkpoint arrest and plk-mediated formation of the 3F3 (show TRIM32 ELISA Kits)/2 epitope.
Data indicate that the mitotic kinase Polo-like kinase 1 (PLK1) was an important effector of S1P (show MBTPS1 ELISA Kits)-S1P5 (show S1PR5 ELISA Kits) signaling, and a new function of the SphK1 (show SPHK1 ELISA Kits)-S1P (show MBTPS1 ELISA Kits) pathway specifically in the control of mitosis in HeLa cells.
identified Polo-like kinase 1 (PLK1), a major signaling hub in the spindle subnetwork, as phosphorylated at the conserved Tyr (show TYR ELISA Kits)(217) in the kinase domain. Substitution of Tyr (show TYR ELISA Kits)(217) with a phosphomimetic residue eliminated PLK1 activity in vitro and in cells.
PLK1 inhibition mitigates autophagy in cancer cells both under nutrient starvation and sufficiency, and a role of PLK1 in autophagy is also observed in the invertebrate model organism Caenorhabditis elegans.
a novel p53 (show TP53 ELISA Kits)-independent regulation of PLK1 during CRC (show CALR ELISA Kits) differentiation and apoptosis.
Results show that PLK1 is overexpressed in diffuse intrinsic pontine gliomas.
Mutant IDH1 (show IDH1 ELISA Kits) promotes checkpoint adaptation which can be exploited therapeutically with the combination of TMZ and a PLK1 inhibitor, indicating PLK1 inhibitors may be clinically valuable in the treatment of IDH1 (show IDH1 ELISA Kits) mutant gliomas
Genistein induced mitotic arrest by inhibiting Plk1 activity and, consequently, led to mitotic catastrophe and apoptosis. Tumor cells with TP53 (show TP53 ELISA Kits) mutations were more sensitive to cell death by treatment of genistein.
we show that Plk1 phosphorylates Mre11 (show MRE11A ELISA Kits) at S649 during G2 DNA damage recovery and Mre11 (show MRE11A ELISA Kits) phosphorylation at S649/S689 drives premature checkpoint termination and reduced DNA repair
We propose that the DDR (show DDR1 ELISA Kits) targets recruitment of Aurora A (show AURKA ELISA Kits) to the Plk1/Bora complex to prevent activation of Plk1 during DNA damage in G2.
The findings reveal a PLK1-Fbw7 (show FBXW7 ELISA Kits)-Myc (show MYC ELISA Kits) signaling circuit that underlies tumorigenesis and validate PLK1 inhibitors, alone or with Bcl2 (show BCL2 ELISA Kits) antagonists, as potential effective therapeutics for MYC (show MYC ELISA Kits)-overexpressing cancers.
Thus, these results indicated that Plk1 is essential for porcine embryos to complete the first mitotic division. Furthermore, Plk1 regulation was associated with effects on spindle assembly and chromosome arrangement
PLK1 might play a critical role in vascular smooth muscle cell mitosis in hyperplastic intima of the injured vessels.
Data show that Polo-like kinase 1 is activated before M phase promoting factor (MPF (show MSLN ELISA Kits)), which is consistent with its role in activating MPF (show MSLN ELISA Kits) in mammalian oocytes.
CIP2A (show KIAA1524 ELISA Kits) acts as a scaffold for CEP192-mediated microtubule organizing center assembly by recruiting Plk1 and aurora A (show AURKA ELISA Kits) during meiotic maturation in mouse oocytes
Plk1 overexpression may contribute to tumor formation by both inducing chromosomal instability and suppressing the DDR (show DDR1 ELISA Kits) pathway.
Plk1 is essential for the mammalian embryonic development, and its depletion leads to mitotic alterations and lethality at different stages during mammalian development.
Plk1 regulated angiotensin II-dependent activation of RhoA (show RHOA ELISA Kits) and actomyosin dynamics in VSMCs in a mitosis-independent manner. This regulation depended on Plk1 kinase activity. Plk1 haploinsufficiency in mice did not induce obvious cell proliferation defects but did result in arterial structural alterations, which frequently led to aortic rupture and death.
These data implicate the insulin (show INS ELISA Kits)-FoxM1 (show FOXM1 ELISA Kits)/PLK1/CENP-A (show CENPA ELISA Kits) pathway-regulated mitotic cell-cycle progression as an essential component in the beta cell adaptation to delay and/or prevent progression to diabetes.
centrosome maturation occurs during interphase in an MLK (show MUSK ELISA Kits)-dependent manner, independent of the classic mitotic kinase, Plk1.
centrosome protein Dzip1 mediates the assembly of the BBSome-Dzip1-PCM1 (show MBD1 ELISA Kits) complex in the centriolar satellites (CS) at the G0 phase for ciliary translocation of the BBSome. Phosphorylation of Dzip1 at Ser (show SIGLEC1 ELISA Kits)-210 by Plk1 (polo-like kinase 1) during the G2 phase promotes disassembly of this complex, resulting in removal of Dzip1 and the BBSome from the CS.
These findings suggest that Plk1 regulates smooth muscle contraction by modulating vimentin (show VIM ELISA Kits) phosphorylation at Ser (show SIGLEC1 ELISA Kits)-56.
Results indicate that polo-like kinase 1 (PLK1) controls the onset of spindle assembly and spindle formation, and is essential for anaphase-promoting complex/cyclosome (APC (show APC ELISA Kits)/C) activation before anaphase onset in zygotes.
Report the 2.3-A crystal structure of the complex of the N-terminal kinase domain (KD) and a C-terminal Polo-box domain (PBD together with a PBD-binding motif of Drosophila melanogaster microtubule-associated protein (show FAM82A2 ELISA Kits) 205 (Map205(PBM)).
Studies demonstrate that Plk1 is required for embryonic proliferation because its activity is crucial for mitotic integrity.
for the first time that Plk1 can accommodate extended ATP-competitive compounds that project toward the adaptive pocket and help the enzyme order its activation segment
These results reveal a crucial and conserved role of phosphorylation of the N terminus of Bora for Plk1 activation and mitotic entry.
Our data further show that PLK-1 is needed for nuclear envelope breakdown during early embryogenesis
PLK-1 substitutes for Mps1 in controlling spindle checkpoint initiation in C. elegans.
NCAPG2 (show NCAPG2 ELISA Kits) plays an important role in regulating proper chromosome segregation through a functional interaction with PLK1 during mitosis
CDK-1 (show CDK1 ELISA Kits) activates PLK-1 via SPAT (show AGXT ELISA Kits)-1 phosphorylation to promote entry into mitosis.
The result provide key insights into the regulation of homolog pairing and reveal that targeting of plk-1 to the NE by meiotic chromosomes establishes the conserved linkages to cytoskeletal forces needed for homology assessment.
SPAT (show AGXT ELISA Kits)-1 and PLK-1 depletion causes impaired polarity with abnormal length of the anterior and posterior PAR (show AFG3L2 ELISA Kits) domains, and partial plk-1(RNAi) or spat (show AGXT ELISA Kits)-1(RNAi), but not air-1(RNAi), can rescue the lethality of a par-2 (show F2RL1 ELISA Kits) mutant.
Polo kinases, via their polo box domains, bind to and regulate the activity of two key polarity proteins, MEX-5 and MEX-6.
plk-1 asymmetry contributes to asynchronous cell division in C. elegans embryos.
human homolog catalyzes the phosphorylation of a Golgi reassembly stacking protein (GRASP65); may play a role in Golgi apparatus fragmentation and reorganization during mitosis
serine/threonine-protein kinase PLK1
, polo kinase
, polo protein kinase
, cell cycle regulated protein kinase
, polo (Drosophia)-like kinase
, polo like kinase
, serine/threonine-protein kinase 13
, polo-like protein kinase
, polo-like kinase homolog
, polo-like kinase 1
, serine/threonine-protein kinase PLK2
, serine/threonine-protein kinase SNK
, serum-inducible kinase