Cdc14A and Cdc14B Redundantly Regulate DNA Double-Strand Break Repair

Han, Lin; Ha, Kyungsoo; Lu, Gui-Fu; Xiao, Fang; Cheng, Ranran; Zuo, Qiuhong; Zhang, Pumin

doi:10.1128/mcb.00233-15

Cited by 27 publications

(31 citation statements)

References 52 publications

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“…Supporting these results, CDC14B-deficient mouse embryonic fibroblasts exposed to genotoxic stress also develop high levels of endogenous DNA damage and trigger senescence without any interference with the DNA damage checkpoint machinery [96]. It is important to remark that MEFs cells lacking CDC14B present defects in repairing IR-induced DSBs only at late passages, when CDC14A levels are low [128], suggesting that both phosphatase isoforms might collaborate in DNA repair by sharing similar functions.…”

Section: Cdc14mentioning

confidence: 57%

Cell Cycle and DNA Repair Regulation in the Damage Response: Protein Phosphatases Take Over the Reins

Campos

Clemente‐Blanco

2020

IJMS

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Cells are constantly suffering genotoxic stresses that affect the integrity of our genetic material. Genotoxic insults must be repaired to avoid the loss or inappropriate transmission of the genetic information, a situation that could lead to the appearance of developmental abnormalities and tumorigenesis. To combat this threat, eukaryotic cells have evolved a set of sophisticated molecular mechanisms that are collectively known as the DNA damage response (DDR). This surveillance system controls several aspects of the cellular response, including the detection of lesions, a temporary cell cycle arrest, and the repair of the broken DNA. While the regulation of the DDR by numerous kinases has been well documented over the last decade, the complex roles of protein dephosphorylation have only recently begun to be investigated. Here, we review recent progress in the characterization of DDR-related protein phosphatases during the response to a DNA lesion, focusing mainly on their ability to modulate the DNA damage checkpoint and the repair of the damaged DNA. We also discuss their protein composition and structure, target specificity, and biochemical regulation along the different stages encompassed in the DDR. The compilation of this information will allow us to better comprehend the physiological significance of protein dephosphorylation in the maintenance of genome integrity and cell viability in response to genotoxic stress.

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Section: Cdc14mentioning

confidence: 57%

Cell Cycle and DNA Repair Regulation in the Damage Response: Protein Phosphatases Take Over the Reins

Campos

Clemente‐Blanco

2020

IJMS

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“…We showed recently that this E3 ligase helps HDR repair by protecting K-63 linked ubiquitin chains essential for the recruitment of BRCA1 at DSBs [17]. In addition, our work also implicated APC Cdh1 in NHEJ repair [17,18], but how exactly the E3 ligase is involved in NHEJ repair remained unclear. Here we report that APC Cdh1 regulates the expression of RNF8 in G1 and keeps RNF8 level in check at DSBs to prevent premature turnover of Ku80.…”

Section: Introductionmentioning

confidence: 74%

The anaphase promoting complex promotes NHEJ repair through stabilizing Ku80 at DNA damage sites

Kim

et al. 2018

Cell Cycle

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Double-strand breaks (DSBs) are repaired through two major pathways, homology-directed recombination (HDR) and non-homologous end joining (NHEJ). The choice between these two pathways is largely influenced by cell cycle phases. HDR can occur only in S/G2 when sister chromatid can provide homologous templates, whereas NHEJ can take place in all phases of the cell cycle except mitosis. Central to NHEJ repair is the Ku70/80 heterodimer which forms a ring structure that binds DSB ends and serves as a platform to recruit factors involved in NHEJ. Upon completion of NHEJ repair, DNA double strand-encircling Ku dimers have to be removed. The removal depends on ubiquitylation and proteasomal degradation of Ku80 by the ubiquitin E3 ligases RNF8. Here we report that RNF8 is a substrate of APC and the latter keeps RNF8 level in check at DSBs to prevent premature turnover of Ku80.

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“…However, whether this Cdc14B contributes to the G2 checkpoint activity or DNA repair functions of APC/C Cdh1 is unclear and could be influenced by cell type [110][111][112].…”

Section: Crls and Apc/c In Dna Damage Checkpoint Responses 41 The Gmentioning

confidence: 99%

The Roles of Cullin RING Ligases and the Anaphase Promoting Complex/Cyclosome in the Regulation of DNA Double Strand Break Repair

Pal¹,

Summers²

2018

Ubiquitination Governing DNA Repair - Implications in Health and Disease

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Historically, genome maintenance has been viewed as the largely independent activities of (1) ubiquitin ligases driving unidirectional cell cycle progression and, (2) the activity of cellular checkpoints that monitor DNA integrity and DNA replication. It is well established that the DNA damage response (DDR) checkpoint machinery promotes the activation of repair mechanisms in addition to opening a window for repair. Emerging evidence demonstrates an integrated network of the central cell cycle driving E3 ubiquitin ligases and the checkpoint machinery, as well as deubiquitinating enzymes, which intermittently cooperate and antagonize one another to define windows of checkpoint and repair activities to optimize genome stability and cellular health. A growing number of components of the ubiquitin machinery are involved in the DDR. Herein, we focus on the regulation of cell cycle checkpoints and the DNA repair mechanisms for double strand breaks (DSBs) by the coordinated activities of Cullin RING ligases (CRLs) and the anaphase promoting complex/cyclosome (APC/C).

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Cdc14A and Cdc14B Redundantly Regulate DNA Double-Strand Break Repair

Cited by 27 publications

References 52 publications

Cell Cycle and DNA Repair Regulation in the Damage Response: Protein Phosphatases Take Over the Reins

Cell Cycle and DNA Repair Regulation in the Damage Response: Protein Phosphatases Take Over the Reins

The anaphase promoting complex promotes NHEJ repair through stabilizing Ku80 at DNA damage sites

The Roles of Cullin RING Ligases and the Anaphase Promoting Complex/Cyclosome in the Regulation of DNA Double Strand Break Repair

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