Expression and functional analyses of mHAUSP regulating apoptosis of cervical adenocarcinoma cells

Yoo, Kyong-Jai; Lee, Hye-Jin; Lee, Heyjin; Lee, Kwang-Youl; Lee, Sook‐Hwan; Chung, Hyung-Min; Baek, Kwang‐Hyun

doi:10.3892/ijo.27.1.97

Cited by 7 publications

(9 citation statements)

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“…The results showed that the Cys, Asp, and His amino acid residues are highly conserved among all of these enzymes, which include a Gln residue located very close to the catalytic Cys amino acid residue [30]. Even though it has been suggested that this amino acid residue can be part of the oxyanion hole present in the structure of cysteine protease [30,31], the mutation at this site did not inhibit the DUB enzyme activity of HAUSP/USP7 [28], indicating that this amino acid is not required for the enzymatic activity. It is possible that this amino acid residue may cooperate with conserved catalytic amino acid residues (Cys, Asp, and His) even though the Gln in oxyanion hole may not be involved in DUB enzyme activity.…”

Section: Structural Features Of Dub Enzymesmentioning

confidence: 69%

“…A previous study on the crystal structure of an UBP-family deubiquitinating enzyme, HAUSP/USP7 has been suggested that an Asp amino acid residue located between DH-V and DH-VI is a new candidate for one of conserved amino acid residues for the catalytic triad [27]. However, biochemical assays for mutants of this conserved amino acid residue in both HAUSP/USP7 and DUB-2A demonstrated that it is not required for the catalytic activity of these DUB enzymes [28,29]. This is surprising since this result argues the model proposed by Hu and his colleagues [27].…”

Section: Structural Features Of Dub Enzymesmentioning

confidence: 91%

“…These conserved amino acids constitute the proteolytic catalytic triad. Even though a conserved Asp amino acid residue (II) located between DH-V and DH-VI has been suggested as one of conserved amino acid residues for the catalytic triad [27], it is not required for the catalytic activity of HAUSP/USP7 and DUB-2A [28,29].…”

Section: Cytokine-inducible Dub Enzymes In Signaling Pathwaysmentioning

confidence: 98%

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Cytokine-Regulated Protein Degradation by the Ubiquitination System

Baek¹

2006

CPPS

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The ubiquitin-mediated protein degradation pathway exerts a wide spectrum of effects and modulates a variety of biological processes including cell cycle progression, transcriptional regulation, signal transduction, antigen presentation, apoptosis (or programmed cell death), oncogenesis, preimplantation, and DNA repair. Recently, the importance of deubiquitination mechanism has been emerged as an essential regulatory step to control these cellular mechanisms for homeostasis. Even though a number of deubiquitinating enzymes have recently been isolated, relatively little is known about their substrates and biological functions. Identified from yeast to human, deubiquitinating (DUB) enzymes are classified into the ubiquitin C-terminal hydrolase (UCH), the ubiquitin-specific processing proteases (UBP or USP), Jab1/Pad1/MPN domain containing metallo-enzymes (JAMM), Otu domain ubiquitin-aldehyde binding proteins (OTU), and Ataxin-3/Josephin domain containing proteins (Ataxin-3/Josephin). Several members of a novel DUB subfamily induced by cytokines in murine lymphocytes have recently been identified. In addition, human DUB enzyme DUB-3, highly homologous to USP17 and induced by cytokines interleukin (IL)-4 and IL-6, has been recently isolated and showed that it has significant homology to the known murine DUB subfamily members. Interestingly, both murine DUB and human USP17 subfamily members are localized and clustered on murine chromosome 7 and on human chromosomes 4 and 8, respectively. This review introduces the reader to provide a great understanding of cytokine-inducible DUB enzymes in both mouse and human, and new insights into DUB subfamily members.

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Section: Structural Features Of Dub Enzymesmentioning

confidence: 69%

Section: Structural Features Of Dub Enzymesmentioning

confidence: 91%

Section: Cytokine-inducible Dub Enzymes In Signaling Pathwaysmentioning

confidence: 98%

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Cytokine-Regulated Protein Degradation by the Ubiquitination System

Baek¹

2006

CPPS

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“…HAUSP is highly expressed in organs that rely on apoptosis for development and is specifically processed upon dexamethasone and gamma-irradiation-induced cell death [76]. The overexpression of mHAUSP induces apoptosis in cervical adenocarcinoma cells [77]. Recently, inhibitors that were developed for USP7 induced p53-dependent apoptosis in cancer cell lines [78].…”

Section: Usp7 and Usp10mentioning

confidence: 99%

The role of deubiquitinating enzymes in apoptosis

Ramakrishna

Suresh

Baek

2010

Cell. Mol. Life Sci.

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It has become apparent that ubiquitination plays a critical role in cell survival and cell death. In addition, deubiquitinating enzymes (DUBs) have been determined to be highly important regulators of these processes. Cells can be subjected to various stresses and respond in a variety of different ways ranging from activation of survival pathways to the promotion of cell death, which eventually eliminates damaged cells. The regulatory mechanisms of apoptosis depend on the balanced action between ubiquitination and deubiquitination systems. There is a growing recognition that DUBs play essential roles in regulating several binding partners to modulate the process of apoptosis. Thus, the interplay between the timing of DUB activity and the specificity of ubiquitin attachment and removal from its substrates during apoptosis is important to ensure cellular homeostasis. This review discusses the role of a few ubiquitin-specific DUBs that are involved in either promoting or suppressing the process of apoptosis.

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“…(27) A mouse orthologue of herpes virus-associated ubiquitin-specific protease (HAUSP) was reported as a regulator of apoptosis for cervical adenocarcinoma cells. (28) USP2 regulates cell viability and induces apoptosis when overexpressed in 293T cells. (29) USP2a reduces fatty acid (30) USP36 results in reduced rate of cell proliferation in HeLa cells.…”

Section: Discussionmentioning

confidence: 99%

Polyclonal and Monoclonal Antibodies Specific for USP17, a Proapoptotic Deubiquitinating Enzyme

et al. 2010

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USP17, a deubiquitinating enzyme (DUB), belongs to the ubiquitin-specific protease protein family. USP17 has highly conserved Cys, His, and Asp domains responsible for the deubiquitinating activity, and two hyaluronan binding motifs in its sequence. We reported that the presence of hyaluronan binding motifs in USP17 is responsible for the cell viability of cancerous cells. Although many if not all of the DUBs contain hyaluronan binding motifs in its sequence, the actual mechanism of hyaluronan binding motifs regulating signal transduction remains unclear. USP17 also regulates Ras activation and cell proliferation by inhibiting RCE1 activity. Thus USP17 may have a critical role in regulating tumor pathway through its deubiquitinating activity on various tumor-related proteins. This study reports the generation and characterization of polyclonal and six monoclonal antibodies against USP17 through immunoblotting, immunoprecipitation, and immunofluorescence microscopy analyses. These antibodies of USP17 will be useful as tools to investigate the mechanism of hyaluronan-mediated tumor suppression and also to screen interacting oncogenic substrates by immunoprecipitation assay.

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Expression and functional analyses of mHAUSP regulating apoptosis of cervical adenocarcinoma cells

Cited by 7 publications

References 0 publications

Cytokine-Regulated Protein Degradation by the Ubiquitination System

Cytokine-Regulated Protein Degradation by the Ubiquitination System

The role of deubiquitinating enzymes in apoptosis

Polyclonal and Monoclonal Antibodies Specific for USP17, a Proapoptotic Deubiquitinating Enzyme

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