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ProteomicsA proteome-wide screen of Cdc14 interactors in Candida albicans
The Cdc14 phosphatase plays a key role in organising the intricate choreography of mitosis and cell division. In order to understand the role of Cdc14 in the human fungal pathogen Candida albicans we used quantitative proteomics to identify interacting proteins of CaCdc14. We used an orthogonal appr...
ORGANISM(S): Candida albicans (Yeast) 
2019-11-12 | PXD009581 | Pride
Nativesilac Silac Cdc14 Candida albicans 
ProteomicsRe-examining the role of Cdc14 phosphatase in mitotic exit
Given that Cdc14 enzymes are so highly conserved, we questioned whether budding yeast Cdc14 could really have such a different influence on Cdk site dephosphorylation. We used quantitative phosphoproteomics to directly measure the in vivo specificity of budding yeast Cdc14 and found that it very sel...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-07-13 | PXD005237 | Pride
Protein phosphatase Mitosis Cdc14 Cdk Mitotic exit Phosphoproteomics Cyclin-dependent kinase 
ProteomicsMammalian CDC14 control differentiation from pluripotent cells by modulating UTF1 activity on bivalent promoters
CDC14 phosphatases are critical components of the cell cycle machinery that drives exit from mitosis in yeast. However, the two mammalian paralogs, CDC14A and CDC14B, are dispensable for cell cycle progression or exit, and their function remains unclear. By generating a double Cdc14a; Cdc14b-null mo...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2022-10-31 | PXD030296 | Pride
Mescs Utf1 Cdc14 
ProteomicsIdentification of Cdc14 phopho-targets in response to DNA damage
We have previously shown that the Cdc14 phosphatase is essential for an efficient repair of a DNA lesion, however we still missing how the phosphatase exerts this molecular functions and what are its targets during the repair process. To identify Cdc14 phospho-targets in response to DNA damage, we p...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-12-22 | PXD004966 | Pride
Dna damage Saccharomyces cerevisiae Cdc14 
TranscriptomicsCdc14 as transcription regulator of RNA pol-II
In yeast, the phosphatase Cdc14 is required for mitotic exit and for segregation of repetitive regions. Cdc14 is also a subunit of the silencing complex RENT, but no roles in transcription repression have been described. Here we report that Cdc14 promotes silencing at the integenic spacer sequences ...
ORGANISM(S): Saccharomyces cerevisiae 
2011-07-28 | E-GEOD-31020 | biostudies-arrayexpress
ProteomicsGlobal analysis of Cdc14 dephosphorylation sites reveals essential regulatory role in mitosis and cytokinesis
Degradation of the M phase cyclins triggers the exit from M phase. Cdc14 is the major phosphatase required for the exit of the M phase. One of the functions of Cdc14 is to dephosphorylate and activate the Cdh1/APC/C complex, resulting in the degradation of the M phase cyclins. However, other crucial...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2013-12-10 | PXD000375 | Pride
Phosphoproteome Yeast Cdc14 
GenomicsThe Cdc14 phosphatase, Clp1, does not affect genome expression
The Cdc14 phosphatase, Clp1, does not affect genome expression
PRJNA1073561 | ENA
TranscriptomicsCdc14 as transcription regulator of RNA pol-II
In yeast, the phosphatase Cdc14 is required for mitotic exit and for segregation of repetitive regions. Cdc14 is also a subunit of the silencing complex RENT, but no roles in transcription repression have been described. Here we report that Cdc14 promotes silencing at the integenic spacer sequences ...
ORGANISM(S): Saccharomyces cerevisiae 
2011-07-29 | GSE31020 | GEO
GenomicsMammalian CDC14 phosphatases control bivalent promoters and exit from stemness in pluripotent cells [snGEX]
Mammalian CDC14 phosphatases control bivalent promoters and exit from stemness in pluripotent cells [snGEX]
PRJNA803459 | ENA
GenomicsMammalian CDC14 control differentiation from pluripotent cells by modulating UTF1 activity on bivalent promoters
Mammalian CDC14 control differentiation from pluripotent cells by modulating UTF1 activity on bivalent promoters
PRJNA790095 | ENA
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