The Cdc14B phosphatase displays oncogenic activity mediated by the Ras-Mek signaling pathway

Chiesa, Massimo; Guillamot, María; Bueno, María José Sánchez; Malumbres, Marcos

doi:10.4161/cc.10.10.15566

Cited by 16 publications

(10 citation statements)

References 35 publications

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“…, 2011). Cdc14B seems to be involved in many functions during the cell cycle (Mocciaro and Schiebel, 2010) and is able to promote malignant transformation in vitro (Chiesa et al. , 2011).…”

Section: Introductionmentioning

confidence: 99%

Human Cdc14A regulates Wee1 stability by counteracting CDK-mediated phosphorylation

Ovejero

Ayala

Bueno

et al. 2012

MBoC

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“…, 2011). Cdc14B seems to be involved in many functions during the cell cycle (Mocciaro and Schiebel, 2010) and is able to promote malignant transformation in vitro (Chiesa et al. , 2011).…”

Section: Introductionmentioning

confidence: 99%

Human Cdc14A regulates Wee1 stability by counteracting CDK-mediated phosphorylation

Ovejero

Ayala

Bueno

et al. 2012

MBoC

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“…Gene Set Enrichment Analysis (GSEA) was carried out using limma moderated t statistic for gene ranking28. The effect of overexpression of Cdc14 or the phosphatase-dead (PD) form of Cdc14b was analyzed as reported previously10.…”

Section: Methodsmentioning

confidence: 99%

“…Cdc14a specifically regulates centrosome function and prevents premature Cdk1 activation8 whereas Cdc14b has been proposed to play multiple functions during the cell cycle9. Cdc14b is able to induce malignant transformation in vitro although this activity has no clear links to direct cell cycle regulation10. Recent knockout studies in established cell lines have shown not obvious mitotic defects in the absence of these proteins, although mammalian Cdc14 phosphatases have been suggested to be required for efficient DNA repair1112.…”

mentioning

confidence: 99%

Cdc14b regulates mammalian RNA polymerase II and represses cell cycle transcription

Guillamot

Manchado

Chiesa

et al. 2011

Sci Rep

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Cdc14 is an essential phosphatase in yeast but its role in the mammalian cell cycle remains obscure. We report here that Cdc14b-knockout cells display unscheduled induction of multiple cell cycle regulators resulting in early entry into DNA replication and mitosis from quiescence. Cdc14b dephosphorylates Ser5 at the C-terminal domain (CTD) of RNA polymerase II, a major substrate of cyclin-dependent kinases. Lack of Cdc14b results in increased CTD-Ser5 phosphorylation, epigenetic modifications that mark active chromatin, and transcriptional induction of cell cycle regulators. These data suggest a function for mammalian Cdc14 phosphatases in the control of transcription during the cell cycle.

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“…This could define Ptpcd2 as an unidentified tumor suppressor phosphatase, which might be mutated in a subset of cancer cells. Interestingly, Cdc14 B has been proved to be of oncogenic potential which is an unusual feature for mammalian phosphatases (Chiesa et al, 2011;Wei and Zhang, 2011). Furtherly, Cdc14 down regulation has been proved to suppress glioblastoma growth (Galeano et al, 2013).…”

Section: Discussionmentioning

confidence: 99%

Cloning and Functional Characterization of Ptpcd2 as a Novel Cell Cycle Related Protein Tyrosine Phosphatase that Regulates Mitotic Exit

Zineldeen

Wagih²,

Nakanishi³

2013

Asian Pacific Journal of Cancer Prevention

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Faithful transmission of genetic information depends on accurate chromosome segregation as cells exit from mitosis, and errors in chromosomal segregation are catastrophic and may lead to aneuploidy which is the hallmark of cancer. In eukaryotes, an elaborate molecular control system ensures proper orchestration of events at mitotic exit. Phosphorylation of specific tyrosyl residues is a major control mechanism for cellular proliferation and the activities of protein tyrosine kinases and phosphatases must be integrated. Although mitotic kinases are well characterized, phosphatases involved in mitosis remain largely elusive. Here we identify a novel variant of mouse protein tyrosine phosphatase containing domain 1 (Ptpcd1), that we named Ptpcd2. Ptpcd1 is a Cdc14 related centrosomal phosphatase. Our newly identified Ptpcd2 shared a significant homology to yeast Cdc14p (34.1%) and other Cdc14 family of phosphatases. By subcellular fractionation Ptpcd2 was found to be enriched in the cytoplasm and nuclear pellets with catalytic phosphatase activity. By means of immunofluorescence, Ptpcd2 was spatiotemporally regulated in a cell cycle dependent manner with cytoplasmic abundance during mitosis, followed by nuclear localization during interphase. Overexpression of Ptpcd2 induced mitotic exit with decreased levels of some mitotic markers. Moreover, Ptpcd2 failed to colocalize with the centrosomal marker γ-tubulin, suggesting it as a non-centrosomal protein. Taken together, Ptpcd2 phosphatase appears a non-centrosomal variant of Ptpcd1 with probable mitotic functions. The identification of this new phosphatase suggests the existence of an interacting phosphatase network that controls mammalian mitosis and provides new drug targets for anticancer modalities.

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The Cdc14B phosphatase displays oncogenic activity mediated by the Ras-Mek signaling pathway

Cited by 16 publications

References 35 publications

Human Cdc14A regulates Wee1 stability by counteracting CDK-mediated phosphorylation

Human Cdc14A regulates Wee1 stability by counteracting CDK-mediated phosphorylation

Cdc14b regulates mammalian RNA polymerase II and represses cell cycle transcription

Cloning and Functional Characterization of Ptpcd2 as a Novel Cell Cycle Related Protein Tyrosine Phosphatase that Regulates Mitotic Exit

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