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PP5 (PPP5C) is a phosphatase of Dvl2.
- Source :
-
Scientific reports [Sci Rep] 2018 Feb 09; Vol. 8 (1), pp. 2715. Date of Electronic Publication: 2018 Feb 09. - Publication Year :
- 2018
-
Abstract
- Dishevelled (Dvl) family proteins are key mediators of Wnt signalling and function in both canonical and noncanonical branches. Dvl2, the most studied Dvl protein, is extensively regulated by phosphorylation. Several kinases were found to be critical for Dvl2 localisation, stability control and functional segregation. For example, S143-phosphorylated Dvl2 was detected, together with CK1δ/ε, at the centrosome and basal body of primary cilia and plays pivotal roles during ciliogenesis. However, relatively less is known about Dvl dephosphorylation and the phosphatases involved. Here, we identified PP5 (PPP5C) as a phosphatase of Dvl2. PP5 interacts with and can directly dephosphorylate Dvl2. Knockdown of PP5 caused elevated Dvl2 phosphorylation both at the basal level and upon Wnt stimulation. In the Dvl2 protein, S143, the 10B5 cluster and other sites were dephosphorylated by PP5. Interestingly, comparison of PP5 with PP2A, another known Dvl2 phosphatase, revealed that PP5 and PP2A are not fully redundant in the regulation of Dvl2 phosphorylation status. In hTERT-RPE1 cells, PP5 was found at the basal body of cilia, where S143-phosphorylated Dvl2 also resides. Functional assays revealed modest effects on ciliogenesis after PP5 depletion or over-expression. Taken together, our results provided evidence to suggest PP5 as a new phosphatase for Dvl2.
- Subjects :
- Cells, Cultured
Dishevelled Proteins genetics
HEK293 Cells
HeLa Cells
Humans
MCF-7 Cells
Nuclear Proteins genetics
Phosphoprotein Phosphatases genetics
Phosphorylation
Proteolysis
Retinal Pigment Epithelium cytology
Signal Transduction
Wnt Proteins genetics
Cilia physiology
Dishevelled Proteins metabolism
Nuclear Proteins metabolism
Phosphoprotein Phosphatases metabolism
Retinal Pigment Epithelium metabolism
Wnt Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 8
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 29426949
- Full Text :
- https://doi.org/10.1038/s41598-018-21124-3