Plk4 Is a Novel Substrate of Protein Phosphatase 5

The conserved Ser/Thr protein phosphatase 5 (PP5) is involved in the regulation of key cellular processes, including DNA damage repair and cell division in eukaryotes. As a co-chaperone of Hsp90, PP5 has been shown to modulate the maturation and activity of numerous oncogenic kinases. Here, we ident...

Teljes leírás

Elmentve itt :
Bibliográfiai részletek
Szerzők: Ábrahám Edit
Réthi-Nagy Zsuzsánna
Vilmos Péter
Sinka Rita
Lipinszki Zoltán
Dokumentumtípus: Cikk
Megjelent: 2023
Sorozat:INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES 24 No. 3
Tárgyszavak:
doi:10.3390/ijms24032033

mtmt:33723350
Online Access:http://publicatio.bibl.u-szeged.hu/34612
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520 3 |a The conserved Ser/Thr protein phosphatase 5 (PP5) is involved in the regulation of key cellular processes, including DNA damage repair and cell division in eukaryotes. As a co-chaperone of Hsp90, PP5 has been shown to modulate the maturation and activity of numerous oncogenic kinases. Here, we identify a novel substrate of PP5, the Polo-like kinase 4 (Plk4), which is the master regulator of centriole duplication in animal cells. We show that PP5 specifically interacts with Plk4, and is able to dephosphorylate the kinase in vitro and in vivo, which affects the interaction of Plk4 with its partner proteins. In addition, we provide evidence that PP5 and Plk4 co-localize to the centrosomes in Drosophila embryos and cultured cells. We demonstrate that PP5 is not essential; the null mutant flies are viable without a severe mitotic phenotype; however, its loss significantly reduces the fertility of the animals. Our results suggest that PP5 is a novel regulator of the Plk4 kinase in Drosophila. 
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700 0 2 |a Vilmos Péter  |e aut 
700 0 2 |a Sinka Rita  |e aut 
700 0 2 |a Lipinszki Zoltán  |e aut 
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