Il n’y a pas de produits dans votre liste de comparaison.
Votre panier est vide.
Afficher tous les synonymes
Sélectionnez vos espèces d'intérêt
Nonphosphorylated Asl binds Plk4 and stimulates its kinase activity, but after Asl is phosphorylated, a negative-feedback mechanism suppresses Plk4 activity. This dual regulatory effect by Asl-A may limit Plk4 to bursts of activity that modulate centriole duplication.
Plk4 phosphorylates Cep135 to properly position the essential centriole component Asterless.
Plk4 phosphorylates Ana2 at S38 and STAN motif and promotes Ana2 recruitment to the centriole.
When Asl reduction is attenuated by Asl overexpression, plk4 mutations, Plk4 RNAi, or Slimb overexpression, Asl levels are higher in spermatozoa, resulting in embryos with reduced viability.
Drosophila Plk4 phosphorylates four conserved serines in the STAN motif of the core centriole protein Ana2 to enable it to bind and recruit its Sas6 partner.
Plk4 directly generates its own phosphodegron.Phosphorylation of only S293 of the Slimb-recognition motif is required for Slimb binding to Plk4.
Regulation of autophosphorylation controls PLK4 self-destruction and centriole number.PLK4 protein levels are controlled by Slimb.
Data indicate that interphase centrioles are closely associated with Sas-4, Spd-2, Polo kinase, Pericentrin-like protein (Dplp), Asterless (Asl), Plk4 kinase, Centrosomin (Cnn) and gamma-tubulin.
SAK/PLK4 is required for centriole duplication and flagella development.
MiRNA-126/PLK-4 axis is critical for tumorigenesis and progression of HCC.
Study showed that the mRNA level of PLK4 was significantly associated with glioma grade and inversely correlated with overall survival and temozolomide sensitivity.
PLK4 phosphorylates CEP131 at Ser-78 to maintain centriolar satellite integrity.
blocking of PLK4 or STIL functions leads to centrosome loss followed by both p53-dependent and -independent defects, including prolonged cell divisions, upregulation of p53, chromosome instability, and, importantly, reduction of pluripotency markers and induction of differentiation.
Elevated PLK4 expression was observed in high grade glioblastoma (GBM) patients and was associated with poor prognosis. PLK4 expression was markedly elevated by the exogenous overexpression of ATAD2 in GBM cells. Results suggested that the ATAD2dependent transcriptional regulation of PLK4 promoted cell proliferation and tumorigenesis.
Study demonstrated that PLK4 has an ability to phase-separate into condensates via an intrinsically disordered linker and that the condensation properties of PLK4 are regulated by autophosphorylation. Consistently, the dissociation dynamics of centriolar PLK4 are controlled by autophosphorylation.
Study shows that Cep63 and Cep152 cooperatively generate a heterotetrameric alpha-helical bundle that functions in conjunction with its neighboring hydrophobic motifs to self-assemble into a higher-order cylindrical architecture capable of recruiting downstream components, including Plk4, a key regulator for centriole duplication. Mutations disrupting the self-assembly abrogate Plk4-mediated centriole duplication.
Pololike kinase 4 (PLK4) has been identified as an oncogene, which is overexpressed in various types of human cancer
Plk4 functions as a homeostatic clock, establishing an inverse relationship between growth rate and period to ensure that daughter centrioles grow to the correct size.
Plk4 first phosphorylates the extreme N terminus of Ana2, which is critical for subsequent STAN domain modification. Phosphorylation of the central region then breaks the Plk4-Ana2 interaction. This phosphorylation pattern is important for centriole assembly and integrity.
our data support tripolar chromosome segregation as a key mechanism generating complex aneuploidy in cleavage-stage embryos and implicate maternal genotype at a quantitative trait locus spanning PLK4 as a factor influencing its occurrence.
Study found that organization of acto-myosin force modulates specifically S-G2 phase length of the cell cycle, PLK4 recruitment at the centrosome and the fidelity of centriole duplication.
Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly.
KAT2A/2B acetylation of PLK4 prevents centrosome amplification
PLK4 played important roles in regulating cell cycle- and DNA replication-related pathways. E2F could upregulate the expression levels of PLK4 by deregulating the methylations of their promoters to promote the relapse of Acute Lymphoblastic Leukemia.
PLK4 specifically phosphorylates CP110 at the S98 position and is an essential step for centriole assembly.
These data show that complementary mechanisms, such as mother-daughter centriole proximity and CDK1-CyclinB interaction with centriolar components, ensure that centriole biogenesis occurs once and only once per cell cycle, raising parallels to the cell-cycle regulation of DNA replication and centromere formation.
Homozygous splicing acceptor site transition (c.31-3 A>G) in PLK4 was identified in a family with Seckel syndrome. PLK4 is essential for centriole biogenesis and DNA damage response.
the interaction between Cep78 and the N-terminal catalytic domain of Plk4 is a new and important element in the centrosome overduplication process.
Our results validate Plk4 as a therapeutic target in cancer patients
Aurora A and Plk4 are rate-limiting factors contributing to microtubule growth as the acentriolar oocyte resumes meiosis.
that aneuploidy induced by transient centrosome amplification can accelerate tumorigenesis in p53-deficient cells
Transient knockdown of KLF14 is sufficient to induce Plk4-directed centrosome amplification.
PLK4 is essential for meiotic resumption but may not influence spindle formation in mouse oocytes during meiotic maturation
p53-Dependent and cell specific epigenetic regulation of the polo-like kinases under oxidative stress.
The Plk4-Cep152 complex has an unexpected role in promoting microtubule nucleation in the vicinity of chromosomes to mediate bipolar spindle formation in the absence of centrioles.
Loss of Plk4 is associated with centrosome amplification causing microcephaly.
PP2A (Protein Phosphatase 2A(Twins)) counteracts Plk4 autophosphorylation, thus stabilizing Plk4 and promoting centriole duplication
the I242N heterozygous mutation in PLK4 is causative for patchy germ cell loss beginning at P10, suggesting a role for PLK4 during the initiation of spermatogenesis.
Aberrant Plk methylation is correlated with the development of hepatocellular carcinoma in mice.
Plk4 is required for cytokinesis and maintenance of chromosomal stability
We propose that kinase-mediated, autoregulated instability of Plk4 self-limits Plk4 activity so as to prevent centrosome amplification.
2.0 A crystal structure of a novel domain composed of the polo box motif of murine Sak
polo-like kinase Plk4 (also called Sak) is required for late mitotic progression, cell survival and postgastrulation embryonic development
Study shows that polo-like kinase Plk4 mediate the nucleolar release of Hand1 for its dimerization and biological function.
Plk4 haploinsufficiency leads to changes in the levels of RNA accumulation for a number of key cellular genes as well as changes in protein levels for several important cell cycle/DNA damage proteins
These results indicated that PLK4 plays crucial roles in bovine oocyte meiotic maturation and subsequent early embryo development.
results provide the first steps in defining a new role for plk4 in organogenesis and implies a role in planar cell polarity, segmentation, and in recently described PLK4 mutations in human
This gene encodes a member of the polo family of serine/threonine protein kinases. The protein localizes to centrioles, complex microtubule-based structures found in centrosomes, and regulates centriole duplication during the cell cycle. Three alternatively spliced transcript variants that encode different protein isoforms have been found for this gene.
, Snk akin kinase
, serine/threonine kinase 18
, serine/threonine protein kinase SAK
, serine/threonine-protein kinase 18
, serine/threonine-protein kinase PLK4
, serine/threonine-protein kinase Sak