The Deubiquitinating Enzyme USP24 Is a Regulator of the UV Damage Response

Zhang, Ling; Nemzow, Leah; Chen, Hua; Lubin, Abigail; Rong, Xi; Sun, Zhongyi; Harris, Thomas K.; Gong, Feng

doi:10.1016/j.celrep.2014.12.024

Cited by 48 publications

(44 citation statements)

References 34 publications

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“…In multiple cell lines, USP24 protein was found to be induced at 3 hours after UV. [53]. This UV-induced upregulation of USP24 was blocked by ATM inhibitor Ku55933 and siRNA knockdown of ATM, suggesting that upregulation of USP24 is ATM-dependent.…”

Section: Deubiquitinating Ner Proteins: the Dubs Involvedmentioning

confidence: 99%

“…USP24 is a 2,620-amino acid ubiquitin-specific protease, containing a UBA domain (ubiquitin-associated domain), a UBL domain (ubiquitin-like domain), and a USP domain (ubiquitin-specific protease domain) [53]. In a yeast-two hybrid screen, USP24 was identified as an interaction partner of DDB2 [54].…”

Section: Deubiquitinating Ner Proteins: the Dubs Involvedmentioning

confidence: 99%

“…This UV-induced upregulation of USP24 was blocked by ATM inhibitor Ku55933 and siRNA knockdown of ATM, suggesting that upregulation of USP24 is ATM-dependent. USP24 is found to deubiquitinate p53 both in vitro and in vivo [53]. p53 is stabilized in response to cellular stress, such as ultraviolet (UV), due to decreased degradation.…”

Section: Deubiquitinating Ner Proteins: the Dubs Involvedmentioning

confidence: 99%

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The emerging role of deubiquitination in nucleotide excision repair

Zhang

Gong

2016

DNA Repair

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Nucleotide excision repair (NER) protects genome stability by eliminating DNA helix distorting lesions, such as those induced by UV radiation. The addition and removal of ubiquitin, namely, ubiquitination and deubiquitination, have recently been demonstrated as general mechanisms to regulate protein functions. Accumulating evidence shows that several NER factors are subjected to extensive regulation by ubiquitination and deubiquitination. Thus, the balance between E3 ligases and deubiquitinating enzyme activities can dynamically alter the ubiquitin landscape at DNA damage sites, thereby regulating NER efficiency. Current knowledge about XPC ubiquitination by different ubiquitin E3 ligases highlights the importance of ubiquitin linkage types in regulating XPC binding and release from damaged DNA. Here, we discuss the emerging roles of deubiquitinating enzymes and their ubiquitin linkage specificities in NER.

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Section: Deubiquitinating Ner Proteins: the Dubs Involvedmentioning

confidence: 99%

Section: Deubiquitinating Ner Proteins: the Dubs Involvedmentioning

confidence: 99%

Section: Deubiquitinating Ner Proteins: the Dubs Involvedmentioning

confidence: 99%

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The emerging role of deubiquitination in nucleotide excision repair

Zhang

Gong

2016

DNA Repair

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“…USP24 binds to, deubiquitinates, and stabilizes the DDB2 component of CUL4 E3 ligase (212). As CUL4-DDB2 is known to polyubiquitinate XPC, whether USP24 influences the XPC polyubiquitination or overall TC-NER is not known, although USP24 depletion increases the UV sensitivity of cells (213).…”

Section: Dubs That Regulate Removal Of Bulky Adducts On Dnamentioning

confidence: 99%

Role of Deubiquitinating Enzymes in DNA Repair

Kee

Huang

2016

Molecular and Cellular Biology

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Both proteolytic and nonproteolytic functions of ubiquitination are essential regulatory mechanisms for promoting DNA repair and the DNA damage response in mammalian cells. Deubiquitinating enzymes (DUBs) have emerged as key players in the maintenance of genome stability. In this minireview, we discuss the recent findings on human DUBs that participate in genome maintenance, with a focus on the role of DUBs in the modulation of DNA repair and DNA damage signaling. DEUBIQUITINATING ENZYMES Safeguarding the genome from genotoxic stress is critical for cell survival and for preventing various human diseases, including cancer. DNA repair or DNA damage responses are under exquisite control and must be accurately and rapidly executed when genome integrity is challenged. Understanding the molecular mechanisms and regulation of critical DNA repair and damage response factors in mammalian cells will provide insight into the pathogenesis of human diseases and aid in the development of therapeutics. Ubiquitination is a posttranslational modification event that allows for rapid and dynamic changes in a protein fate or function. The ubiquitin-proteasome system (UPS) is an essential posttranslational regulatory mechanism that permeates into diverse biological processes, including the DNA repair and damage response pathways. While the role of ubiquitin in mediating controlled degradation/proteolysis of specific proteins is well established, nonproteolytic functions of ubiquitination have also emerged as important players in signaling pathways that often exist in parallel with the UPS. Deubiquitinating enzymes (DUBs), responsible for reversing the ubiquitination reaction by removing covalently attached ubiquitin molecules from substrates or polyubiquitinated chains, have recently exploded onto the ubiquitin field as key regulators of both the UPS and of the nonproteolytic functions of ubiquitination. Thus, DUBs exert profound influence on many cellular pathways, including one of the best-studied biological processes involving DNA repair and damage response in mammalian cells.There are approximately 95 DUBs encoded by the human genome, which fall into one of the five subclasses: ubiquitin C-terminal hydrolases (UCHs), ubiquitin-specific proteases (USPs), Machado-Joseph domain-containing proteins (MJDs), Otubain domain-containing proteases (OTUs), and JAMM (JAB1/MPN/ Mov34) proteases (1, 2). Ubiquitin has seven internal lysine residues (Lys6,, each providing sites for the generation of an isopeptide bond with the carboxy terminus of another ubiquitin to form ubiquitin polymers, otherwise known as polyubiquitination. Linear ubiquitin chains can also be generated when the amino-terminal methionine (Met) of ubiquitin (Met1) forms a peptide bond with the carboxy-terminal glycine (Gly) of ubiquitin. As different types of polyubiquitin polymers adopt different conformations (3), it is not surprising that many DUBs show some degree of specificity toward differentially linked polyubiquitination, each of which results in a different physi...

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“…Az USP24 (Ubiquitin specific peptidase 24) DUB elhasítja az ubiquitin és a P53 fehérje között lévő peptidkötést, amivel hozzájárul a P53 stabilitásának és aktivitásának fenntartásához. Az USP24 DNS károsodást követő aktivációja ATM-függő (Ataxia telangiectasia mutated) -az USP24 ATM kináz általi foszforilációja vezet a P53 fehérje UV sugárzás hatására bekövetkező stabilizálódásához (123).…”

Section: A P53 Proteoszómális éS Proteoszóma-független Bontásaunclassified

A humán P53 fehérje transzkripció elongációban betöltött, eddig nem azonosított szerepének jellemzése

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The Deubiquitinating Enzyme USP24 Is a Regulator of the UV Damage Response

Cited by 48 publications

References 34 publications

The emerging role of deubiquitination in nucleotide excision repair

The emerging role of deubiquitination in nucleotide excision repair

Role of Deubiquitinating Enzymes in DNA Repair

A humán P53 fehérje transzkripció elongációban betöltött, eddig nem azonosított szerepének jellemzése

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