PLK4 Antibody

1. Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly. PMID: 29712910
2. KAT2A/2B acetylation of PLK4 prevents centrosome amplification PMID: 27796307
3. 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. PMID: 29768346
4. PLK4 specifically phosphorylates CP110 at the S98 position and is an essential step for centriole assembly. PMID: 28562169
5. 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. PMID: 27112295
6. 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. PMID: 28832566
7. the interaction between Cep78 and the N-terminal catalytic domain of Plk4 is a new and important element in the centrosome overduplication process. PMID: 27246242
8. Our results validate Plk4 as a therapeutic target in cancer patients PMID: 27872092
9. Heterozygous missense mutation in PLK4 identified in a patient with microcephaly and chorioretinopathy. Aberrant spindle formation was observed in a LCL derived from this patient. Mutant PLK4 proteins demonstrated altered mobility pattern on a western blot suggesting alterations in post-translation modification. PMID: 27650967
10. Studies indicate that depletion of any one of the protein kinase polo-like kinase 4 (PLK4) and the two proteins STIL and SAS-6 blocks centriole duplication, and, conversely, overexpression causes centriole amplification. PMID: 27911707
11. Common PLK4 variant rs2305957 is associated with blastocyst formation and early recurrent miscarriage in Chinese women. PMID: 28238495
12. Mutations in human PLK4, the protein of which plays critical role in centriole duplication and normal nuclear formation, could be associated with abnormal spermatogenesis leading to Sertoli cell-only syndrome. Aberrant forms of PLK4 might also cause other types of oligozoospermia or sperm fl agellar abnormalities. PMID: 26452337
13. Plk4 directly binds PCM1 and phosphorylates S372. Plk4 depletion leads to the dispersal of centriolar satellites. PMID: 26755742
14. Decreased PLK4 protein expression due to promoter hypermethylation was negatively correlated with JAK2 overexpression, a common occurrence in hematological malignancies. PMID: 25347426
15. KLF14 transcription is significantly downregulated, whereas Plk4 transcription is upregulated in multiple types of cancers, and there exists an inverse correlation between KLF14 and Plk4 protein expression in human breast and colon cancers. PMID: 26439168
16. The s suggest that the STIL-coiled-coil region/PLK4 interaction mediates PLK4 activation as well as stabilization of centriolar PLK4 and plays a key role in centriole duplication. PMID: 26188084
17. We demonstrate that centrioles promote PLK4 activation through its recruitment and local accumulation. Though centriole removal reduces the proportion of active PLK4, this is rescued by concentrating PLK4 to the peroxisome lumen PMID: 26481051
18. these results identify the interaction between Mib1 and Plk4 as a new and important element in the control of centriole homeostasis. PMID: 25795303
19. PLK4 functions downstream of ROCK2 to drive centrosome amplification in arrested cells. PMID: 25590559
20. PLK4 overexpression induces centrosome amplification and chromosome instability and causes the suppression of primary cilia formation. PMID: 24981932
21. Negative feedback by centriolar STIL regulates bimodal centriolar distribution of Plk4 and seemingly restricts occurrence of procentriole formation to one site on each parental centriole. PMID: 25342035
22. An unexpected activity of Plk4 that promotes cell migration and may underlie an association between increased Plk4 expression, cancer progression and death from metastasis in solid tumor patients. PMID: 25174401
23. Plk4 activity promotes the recruitment of STIL to the centriole and primes the direct binding of STIL to the C terminus of SAS6. PMID: 26101219
24. Mutation in PLK4, encoding a master regulator of centriole formation, defines a novel locus for primordial dwarfism. PMID: 25320347
25. Data suggest polo-like kinase 4 (PLK4) inhibitors as a clinical candidate for cancer therapy. PMID: 25723005
26. Studies indicate that overexpression of polo-like kinase 4 (PLK4) is found in several cancer and suggest the PLK4 inhibitors as anticancer therapeutics. PMID: 24867403
27. identified association between aneuploidy of putative mitotic origin and linked genetic variants on chromosome 4 of maternal genomes; associated region contains candidate gene,PLK4, that plays a role in centriole duplication and can alter mitotic fidelity upon minor dysregulation PMID: 25859044
28. different levels of impaired PLK4 activity result in growth and cilia phenotypes, providing a mechanism by which microcephaly disorders can occur with or without ciliopathic features PMID: 25344692
29. Results demonstrated that Plk4 is under the direct control of the E2F activators in breast cancer cells. PMID: 24797070
30. p53-Dependent and cell specific epigenetic regulation of the polo-like kinases under oxidative stress. PMID: 24498222
31. Breast cancer cell viability is dependent on PLK4 expression. PMID: 25043604
32. Plk4 is intricately regulated in time and space through ordered interactions with two distinct scaffolds, Cep192 and Cep152, and a failure in this process may lead to human cancer. PMID: 24997597
33. it appears that Nek2 and Plk4 might synergize to promote breast tumorigenesis and may also be involved in tamoxifen and trastuzumab resistance PMID: 24389189
34. PLK4 is a new NFkappaB target gene, providing a direct link between NFkappaB activity and centrosome duplication, with implications for the role of these transcription factors in tumorigenesis. PMID: 23974100
35. Plk4 dynamically localizes to distinct subcentrosomal regions by interacting with two hierarchically regulated scaffolds, Cep192 and Cep152. PMID: 24277814
36. Studies indicate that autophosphorylation of Nek7 and Plk4 occurred through an intermolecular mechanism, the kinases Aurora-A and Chk2 followed an intramolecular mechanism. PMID: 23821772
37. cooperation between Cep192 and Cep152 is crucial for centriole recruitment of Plk4 and centriole duplication during the cell cycle. PMID: 23641073
38. If both p53 and the SAPKK MKK4 are simultaneously inactivated, persistent polo-like kinase 4 activity combined with the lack of SAPK-mediated inhibition of centrosome duplication conspire to induce supernumerary centrosomes under stress. PMID: 23653187
39. Preventing Plk4 autoregulation causes centrosome amplification, stabilization of p53, and loss of cell proliferation PMID: 23249732
40. CAND1 promotes PLK4-mediated centriole overduplication and is frequently disrupted in prostate cancer. PMID: 23019411
41. Study demonstrated that PLK4 was remarkably downregulated in HCC and could be served as a potential prognostic marker for patients with this deadly disease. PMID: 22829937
42. STIL cooperates with SAS-6 and PLK4 in the control of centriole number and represents a key centriole duplication factor in human cells. PMID: 22349698
43. Plk4 is a centriole-localized kinase that does not directly regulate cytokinesis. PMID: 22456511
44. The activity of SCF-FBXW5 is negatively regulated by Polo-like kinase 4 (PLK4), which phosphorylates FBXW5 at Ser 151 to suppress its ability to ubiquitylate HsSAS-6. PMID: 21725316
45. These results highlight the critical role of PLK4 transcriptional deregulation in centriole multiplication in HPV-16 E7-expressing cells. PMID: 21609466
46. CDK11(p58), which accumulates only in the vicinity of mitotic centrosomes, directly interacts with the centriole-associated protein kinase Plk4 that regulates centriole number in cells. PMID: 21297952
47. Results suggest that Cep152 recruits Plk4 and CPAP to the centrosome to ensure a faithful centrosome duplication process. PMID: 21059844
48. Data show that Cep152 can be phosphorylated by Plk4 in vitro, suggesting that Cep152 acts with Plk4 to initiate centriole formation. PMID: 21059850
49. Data suggest that active Plk4 promotes its own degradation by catalyzing betaTrCP binding through trans-autophosphorylation (phosphorylation by the other kinase in the dimer) within homodimers. PMID: 20516151
50. Data suggest that polo-like kinase 4 activity is restricted to the centrosome to prevent aberrant centriole assembly and sustained kinase activity is required for centriole duplication. PMID: 20032307

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HGNC: 11397

OMIM: 605031

KEGG: hsa:10733

STRING: 9606.ENSP00000270861

UniGene: Hs.172052