Proteomics

Dataset Information

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CDC14B interactome - The proteomic approach aimed at the identification of interaction partners for the human dual phosphatase and tumor suppressor CDC14B by Co-inmunoprecipitation (Co-IP) experiments. In this approach, CDC14B interactomes from unsynchronized and G2/M enriched cells were compared semi-quantitatively based on spectral counting. This approach yielded the deubiquitylase USP9X as a G2/M-specific CDC14B interactor which has been confirmed by Western-blot (WB).


ABSTRACT: The proteomic approach aimed at the identification of interaction partners for the human dual phosphatase and tumor suppressor CDC14B by Co-inmunoprecipitation (Co-IP) experiments. In this approach, CDC14B interactomes from unsynchronized and G2/M enriched cells were compared semi-quantitatively based on spectral counting. This approach yielded the deubiquitylase USP9X as a G2/M-specific CDC14B interactor which has been confirmed by Western-blot (WB).

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Johannes Gloeckner  

LAB HEAD: Christian Johannes Gloeckner

PROVIDER: PXD012732 | Pride | 2020-03-25

REPOSITORIES: pride

Dataset's files

Source:
Action DRS
GLO2216A2MA2-40-29070.RAW Raw
GLO2216A3MA2-40-29072.RAW Raw
GLO2216A4MA2-40-29074.RAW Raw
GLO2216_rev1.sf3 Other
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Publications


Regulation of mitosis secures cellular integrity and its failure critically contributes to the development, maintenance, and treatment resistance of cancer. In yeast, the dual phosphatase Cdc14 controls mitotic progression by antagonizing Cdk1-mediated protein phosphorylation. By contrast, specific mitotic functions of the mammalian Cdc14 orthologue CDC14B have remained largely elusive. Here, we find that CDC14B antagonizes CDK1-mediated activating mitotic phosphorylation of the deubiquitinase U  ...[more]

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