Serine/threonine protein phosphatases in DNA damage response

Liu, Bo; Xu, Xingzhi

doi:10.1007/s11434-011-4679-5

Cited by 8 publications

(8 citation statements)

References 134 publications

(166 reference statements)

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“…7 ), including phosphorylation by PIKK family kinases and dephosphorylation by protein phosphatases including PP2A, PP4, PP6 and WIP1. Protein phosphatase 2A (PP2A) was the first γH2AX dephosphorylating agent to be identified [30,31], and inhibition or silencing of PP2A leads to γH2AX foci persistence and defects in DNA repair. PP2A is a member of a family of protein phosphatases composed of multiple catalytic subunits and regulatory subunits [31].…”

Section: Discussionmentioning

confidence: 99%

γH2AX foci formation in the absence of DNA damage: Mitotic H2AX phosphorylation is mediated by the DNA‐PKcs/CHK2 pathway

et al. 2013

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Edited by Varda RotterKeywords: cH2AX CHK2 DNA-PKcs DNA damage Mitosis a b s t r a c t Phosphorylated H2AX is considered to be a biomarker for DNA double-strand breaks (DSB), but recent evidence suggests that cH2AX does not always indicate the presence of DSB. Here we demonstrate the bimodal dynamic of H2AX phosphorylation induced by ionizing radiation, with the second peak appearing when G2/M arrest is induced. An increased level of cH2AX occurred in mitotic cells, and this increase was attenuated by DNA-PKcs inactivation or Chk2 depletion, but not by ATM inhibition. The phosphorylation-mimic CHK2-T68D abrogated the attenuation of mitotic cH2AX induced by DNA-PKcs inactivation. Thus, the DNA-PKcs/CHK2 pathway mediates the mitotic phosphorylation of H2AX in the absence of DNA damage.

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Section: Discussionmentioning

confidence: 99%

γH2AX foci formation in the absence of DNA damage: Mitotic H2AX phosphorylation is mediated by the DNA‐PKcs/CHK2 pathway

et al. 2013

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“…Many Ser/Thr phosphatases are highly conserved from yeast to human beings [27]. The high conservation of PP5 among species (at the level of amino acids) suggests that the functions of PP5 may be universal [27].…”

Section: Discussionmentioning

confidence: 99%

“…The high conservation of PP5 among species (at the level of amino acids) suggests that the functions of PP5 may be universal [27]. Mammalian protein phosphatase 5 (PP5) and its S. cerevisiae homolog Ppt1 contain a PP2Ac catalytic domain and unique TPR repeats that are not found in other phosphatases.…”

Section: Discussionmentioning

confidence: 99%

“…For instance, reactive oxygen species (ROS) derived from normal cellular metabolism could oxidize bases and make DNA breaks [27]. In addition to DNA damage stress, other stress conditions, such as salt stress, are frequently encountered by all species [28]; therefore, the ability to adapt to external and internal stresses is important for the survival and proliferation of C. albicans in the human host.…”

Section: Discussionmentioning

confidence: 99%

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Role of Ppt1 in multiple stress responses in Candida albicans

Gao

et al. 2014

Chin. Sci. Bull.

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To study the function of CaPpt1, we deleted PPT1 gene from the Candida albicans genome by sequentially replacing the entire coding region with the selectable markers ARG4 and HIS1. The results showed that the deletion of Ppt1 did not affect the hyphal formation of C. albicans under serum induction and caused enhanced sensitivity to DNA damage, Calcofluor white and saltinduced stress. We also found that Ppt1 was not required for the phenotypic response of cells treated with the genotoxins, methylmethane sulfonate and hydroxyurea. Flow cytometric analyses indicated that ppt1D cells and wild-type cells showed similar G 2 /M arrest profiles when exposed to DNA damage stress. Ppt1 was not required for the activation of the DNA damage response pathway, as indicated by normal phosphorylation of Rad53 and Rfa2 in ppt1D cells under DNA damage stress. We suggest that Ppt1 plays important roles in response to various stress conditions in C. albicans.

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“…A balance between phosphorylation and dephosphorylation is very important to maintain the proper activity of these DDR proteins. Liu and Xu [4] provide cutting-edge information on serine/threonine protein phosphatases involved in the DNA damage response. They propose that in situ dephosphorylation of phosphoproteins by protein phosphatases, instead of proteasome-mediated degradation, is the primary cellular mechanism.…”

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confidence: 99%

DNA damage, signaling and repair: Protecting genomic integrity and reducing the risk of human disease

Zhou

2011

Chin. Sci. Bull.

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DNA Damage, Signaling and Repair: Protecting genomic integrity and reducing the risk of human diseaseDNA is the genetic material that contains the "instructions" to not only guide the continuation of life but also govern the development, metabolism and functioning of living organisms. DNA damage occurs daily due to various exogenous (environmental) genotoxic agents and normal metabolic processes within cells. Even under normal growth and metabolic conditions, DNA damage occurs at a rate of approximately 10000 lesions per cell per hour in mammalian cells. DNA damage that is not properly and promptly repaired can lead to genomic instability, an increased likelihood of gene mutation or even cell death. Cells cannot function normally if DNA damage corrupts the integrity and accessibility of the essential information in the genome, which in turn has a harmful effect on health, such as carcinogenesis, tissue-degeneration or functional failure and accelerated aging. In this special topic, Chinese Science Bulletin presents a series of research articles and reviews covering some of the critical aspects of the molecular mechanisms of DNA damage signaling, repair and cellular responses.DNA repair and the cell cycle checkpoint are two fundamental mechanisms governing genome integrity, and both are tightly interconnected in their signaling pathways, sharing some signaling molecules. Depending on the lesion inflicted on the DNA double helical structure, multiple repair pathways have evolved to replace the lost information and recover genomic integrity. The mechanistic pathways of repairing the damage occurring at one of the two helical domains of DNA include: (1) Direct reversal of the damage, which is the specialized mechanism for reversing a specific type of damage; for example, methyl guanine methyl transferase (MGMT) specifically removes a methyl group from DNA bases. (2) Excision repair, in which the damaged nucleotide is removed and the normal DNA structure is recovered using information from the undamaged strand. Excision repair mechanisms include base excision repair that repairs simple damage due to alkylation or deamination, and nucleotide excision repair that repairs bulky, complex or helix-distorting damage. In eukaryotic cells, there are two subpathways of nucleotide excision repair: global-genome nucleotide excision repair and transcription-coupled repair. Transcription-coupled repair can remove bulky DNA lesions located on the transcribed strand of an active gene more rapidly than those on the non-transcribed strand or in the general genomic DNA. And (3) mismatch repair, which corrects errors of DNA replication, recombination and induced mismatched bases. Obviously, DNA double-strand breakage (DSB) is a particularly hazardous type of DNA damage to dividing cells as it involves a break to both strands nearby in the double helix. There are two interconnected and collaborative pathways to repair this damage: homologous recombination and non-homologous endjoining.Evoking the cell cycle checkpoints is one of the cel...

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Serine/threonine protein phosphatases in DNA damage response

Cited by 8 publications

References 134 publications

γH2AX foci formation in the absence of DNA damage: Mitotic H2AX phosphorylation is mediated by the DNA‐PKcs/CHK2 pathway

γH2AX foci formation in the absence of DNA damage: Mitotic H2AX phosphorylation is mediated by the DNA‐PKcs/CHK2 pathway

Role of Ppt1 in multiple stress responses in Candida albicans

DNA damage, signaling and repair: Protecting genomic integrity and reducing the risk of human disease

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