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Dataset Information


Identification of mitotic substrates of phospho-regulated USP9X

ABSTRACT: We previously identified the deubiquitylase USP9X as a G2/M-specific CDC14B interactor (PXD012732) and subsequently identified USP9X as a specific CDC14B target (PXD012733). To investigate relevant mitotic substrates of phospho-regulated USP9X, we next performed a Stable isotope labeling by amino acids in cell culture (SILAC)-based screen in which ubiquitylated proteins were purified from control or USP9X depleted HEK 293T cells that were either asynchronous or synchronized in mitosis. Stable expression of recombinant His-tagged ubiquitin has been used for selective enrichment of ubiquitinylated proteins in both conditions.


ORGANISM(S): Homo sapiens  

TISSUE(S): Cell Culture

DISEASE(S): Not Available

SUBMITTER: Johannes Gloeckner  

LAB HEAD: Christian Johannes Gloeckner

PROVIDER: PXD012734 | Pride | 2020-03-25


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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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