Relevant bibliographies by topics / Ubiquitin-Specific Peptidase 1

Academic literature on the topic 'Ubiquitin-Specific Peptidase 1'

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Published: 11 March 2023

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Journal articles on the topic "Ubiquitin-Specific Peptidase 1"

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Raimondi, Marzia, Daniela Cesselli, Carla Di Loreto, Francesco La Marra, Claudio Schneider, and Francesca Demarchi. "USP1 (ubiquitin specific peptidase 1) targets ULK1 and regulates its cellular compartmentalization and autophagy." Autophagy 15, no. 4 (October 29, 2018): 613–30. http://dx.doi.org/10.1080/15548627.2018.1535291.

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Zhang, Jinghui, Chenchang Liu, and Guofeng You. "Ubiquitin-specific peptidase 8 regulates the trafficking and stability of the human organic anion transporter 1." Biochimica et Biophysica Acta (BBA) - General Subjects 1864, no. 12 (December 2020): 129701. http://dx.doi.org/10.1016/j.bbagen.2020.129701.

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Shanmugam, Ilanchezhian, Mohammad Abbas, Farhan Ayoub, Susan Mirabal, Manal Bsaili, Erin K. Caulder, David M. Weinstock, Alan E. Tomkinson, Robert Hromas, and Monte Shaheen. "Ubiquitin-specific Peptidase 20 Regulates Rad17 Stability, Checkpoint Kinase 1 Phosphorylation and DNA Repair by Homologous Recombination." Journal of Biological Chemistry 289, no. 33 (June 12, 2014): 22739–48. http://dx.doi.org/10.1074/jbc.m114.550459.

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Attaix, Didier, Sophie Ventadour, Audrey Codran, Daniel Béchet, Daniel Taillandier, and Lydie Combaret. "The ubiquitin–proteasome system and skeletal muscle wasting." Essays in Biochemistry 41 (October 1, 2005): 173–86. http://dx.doi.org/10.1042/bse0410173.

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The ubiquitin–proteasome system (UPS) is believed to degrade the major contractile skeletal muscle proteins and plays a major role in muscle wasting. Different and multiple events in the ubiquitination, deubiquitination and proteolytic machineries are responsible for the activation of the system and subsequent muscle wasting. However, other proteolytic enzymes act upstream (possibly m-calpain, cathepsin L, and/or caspase 3) and downstream (tripeptidyl-peptidase II and aminopeptidases) of the UPS, for the complete breakdown of the myofibrillar proteins into free amino acids. Recent studies have identified a few critical proteins that seem necessary for muscle wasting {i.e. the MAFbx (muscle atrophy F-box protein, also called atrogin-1) and MuRF-1 [muscle-specific RING (really interesting new gene) finger 1] ubiquitin–protein ligases}. The characterization of their signalling pathways is leading to new pharmacological approaches that can be useful to block or partially prevent muscle wasting in human patients.
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Nakae, Aya, Michiko Kodama, Toru Okamoto, Makoto Tokunaga, Hiroko Shimura, Kae Hashimoto, Kenjiro Sawada, et al. "Ubiquitin specific peptidase 32 acts as an oncogene in epithelial ovarian cancer by deubiquitylating farnesyl-diphosphate farnesyltransferase 1." Biochemical and Biophysical Research Communications 552 (May 2021): 120–27. http://dx.doi.org/10.1016/j.bbrc.2021.03.049.

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Ogawa, Masahiro, Tomoya Kitakaze, Naoki Harada, and Ryoichi Yamaji. "Female-specific regulation of skeletal muscle mass by USP19 in young mice." Journal of Endocrinology 225, no. 3 (April 21, 2015): 135–45. http://dx.doi.org/10.1530/joe-15-0128.

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17β-estradiol (E2) is thought to be responsible for sex-specific differences in skeletal muscle mass. The biological function of E2 is exerted through its binding to estrogen receptor α (ERα). The expression of ubiquitin-specific peptidase 19 (USP19) is upregulated during muscle atrophy and by E2-activated ERα. Here, we investigated the involvement of USP19 in sex difference in muscle mass in young mice. Knockdown of USP19 in hindlimb muscles increased the mass and fiber size in soleus muscle in females but not males. Using Usp19 promoter reporter constructs, a functional half-estrogen response element (hERE) was identified in intron 1 of Usp19. ERα bound to hERE in an E2-dependent manner in C2C12 myoblasts and in soleus muscle in ovariectomized (OVX) female mice. Furthermore, under normal physiological conditions, ERα bound to hERE in soleus muscle only in females. In contrast, administration of E2 resulted in increased Usp19 mRNA expression, decreased muscle mass, and recruitment of ERα to hERE in soleus muscle in males. Knockdown of ERα in hindlimb muscles decreased Usp19 mRNA expression and increased the mass of soleus muscle only in females. Knockdown of USP19 resulted in increased levels of ubiquitin conjugates in soleus muscle in females. OVX increased the levels of ubiquitin conjugates and administration of E2 decreased OVX-induced levels of ubiquitin conjugates. These results demonstrate that in soleus muscle in young female mice under physiological conditions, E2 upregulates USP19 expression through ERα and consequently leads to decreases in ubiquitin conjugates and muscle mass.
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Yu, Zhongxia, Hui Song, Mutian Jia, Jintao Zhang, Wenwen Wang, Qi Li, Lining Zhang, and Wei Zhao. "USP1–UAF1 deubiquitinase complex stabilizes TBK1 and enhances antiviral responses." Journal of Experimental Medicine 214, no. 12 (November 14, 2017): 3553–63. http://dx.doi.org/10.1084/jem.20170180.

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Optimal activation of TANK-binding kinase 1 (TBK1) is crucial for initiation of innate antiviral immunity and maintenance of immune homeostasis. Although several E3 ubiquitin ligases have been reported to regulate TBK1 activation by mediating its polyubiquitination, the functions of deubiquitinase on TBK1 activity remain largely unclear. Here, we identified a deubiquitinase complex, which is formed by ubiquitin specific peptidase 1 (USP1) and USP1-associated factor 1 (UAF1), as a viral infection–induced physiological enhancer of TBK1 expression. USP1–UAF1 complex enhanced TLR3/4 and RIG-I–induced IFN regulatory factor 3 (IRF3) activation and subsequent IFN-β secretion. Mechanistically, USP1 and UAF1 bound to TBK1, removed its K48-linked polyubiquitination, and then reversed the degradation process of TBK1. Furthermore, we found that ML323, a specific USP1–UAF1 inhibitor, attenuated IFN-β expression and enhanced viral replication both in vitro and in vivo. Therefore, our results outline a novel mechanism for the control of TBK1 activity and suggest USP1–UAF1 complex as a potential target for the prevention of viral diseases.
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Hu, Bin, Chunhua Ge, and Chunqing Zhu. "Ubiquitin-specific peptidase 18 negatively regulates and inhibits lipopolysaccharide-induced sepsis by targeting transforming growth factor-β-activated kinase 1 activity." International Immunology 33, no. 9 (June 11, 2021): 461–68. http://dx.doi.org/10.1093/intimm/dxab029.

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Abstract Sepsis is an inflammatory disease with exacerbated inflammation at early stages. Inflammatory cytokines play critical roles in the pathophysiology of sepsis. Ubiquitin-specific peptidase 18 (USP18), a deubiquitinating enzyme, has been shown to modulate transforming growth factor-β-activated kinase 1 (TAK1) activity. However, the precise role of USP18 in sepsis is not clear. Here, we investigated the potential effect of USP18 on inflammation in sepsis. We generated mice with USP18 or/and TAK1 deficiency in macrophages (USP18MKO mice, TAK1MKO mice and USP18MKO-TAK1MKO mice) and established a lipopolysaccharide (LPS)-induced sepsis model in mice. Bone marrow-derived macrophages were isolated from wild-type (WT), USP18MKO or TAK1MKO mice and treated with LPS or CpG, and the expression of cytokines including IL-6, IL-10, IL-1β and tumor necrosis factor α (TNF-α) was measured. The activation of NF-κB, ERK and p38 signaling pathways and ubiquitination of TAK1 were detected. We induced sepsis in WT, USP18MKO, TAK1MKO or USP18MKO-TAK1MKO mice and evaluated the survival rate, lung pathology and inflammatory cytokine levels in serum. Macrophages deficient in USP18 produced significantly increased IL-6, IL-1β and TNF-α post-LPS or -CpG stimulation. Macrophages deficient in USP18 had promoted activation of NF-κB, p38 and ERK, and increased ubiquitination of TAK1. Mice with TAK1 deficiency in macrophages had increased survival rates, decreased immune cell infiltration in lung and decreased pro-inflammatory cytokines in serum. In contrast, mice with USP18 deficiency in macrophages had decreased survival rates, increased cell infiltration in lung and increased pro-inflammatory cytokines in serum. USP18 alleviated LPS-induced sepsis by inhibiting TAK1 activity.
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Yasunaga, J., F. C. Lin, X. Lu, and K. T. Jeang. "Ubiquitin-Specific Peptidase 20 Targets TRAF6 and Human T Cell Leukemia Virus Type 1 Tax To Negatively Regulate NF- B Signaling." Journal of Virology 85, no. 13 (April 27, 2011): 6212–19. http://dx.doi.org/10.1128/jvi.00079-11.

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Jingjing, Wu, Guo Wenzheng, Wen Donghua, Hou Guangyu, Zhou Aiping, and Wu Wenjuan. "Deubiquitination and stabilization of programmed cell death ligand 1 by ubiquitin-specific peptidase 9, X-linked in oral squamous cell carcinoma." Cancer Medicine 7, no. 8 (July 10, 2018): 4004–11. http://dx.doi.org/10.1002/cam4.1675.

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Dissertations / Theses on the topic "Ubiquitin-Specific Peptidase 1"

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Cataldo, Francesca. "Role of calpain in USP1 stability regulation and genome integrity maintenance." Doctoral thesis, Università degli studi di Trieste, 2012. http://hdl.handle.net/10077/7860.

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2010/2011
The calpains are a family of intracellular cysteine proteases, among which the best studied isoforms, micro- (CAPN1) and milli-calpain (CAPN2), are heterodimers consisting of a catalytic subunit and a common regulatory subunit, CAPNS1, required for function. Calpain is involved in many processes important for cancer biology, such as autophagy, indeed in calpain-depleted cells autophagy is impaired, with a subsequent increase in apoptosis sensitivity. Calpain is also important in all the stages of the stress response. A proteomic approach was employed for the identification of novel CAPNS1 interacting proteins. Proteins immunoprecipitating with endogenous CAPNS1 in HT1080 cell lysates were analyzed by Mass Spectrometry. We identified novel partners among which the deubiquitinating enzyme USP1, a key regulator of the DNA damage response and genome integrity maintenance via its specific action on FANCD2, involved in DNA repair and protection from chromosome instability, and PCNA, involved in the regulation of translesion DNA synthesis (TLS), that bypasses DNA lesions with low stringency basepairing requirements. We performed co-IP assays in lysates of 293T cells and confirmed that the interaction was specific. Furhermore, we observed that calpain is able to bind a USP1 C-terminal deleted mutant, suggesting that USP1 first 523 aminoacids were sufficient for the binding. To understand what is the effect exerted by calpain upon USP1, we depleted calpain activity in a series of cell lines, and followed the fate of endogenous USP1. We transfected CAPNS1 specific siRNAs, or treated cells with a specific inhibitor of calpain, and we observed a strong decrease in USP1 protein levels. This effect should be at a post-transcriptional level, since any significant change in USP1 mRNA levels is detected. We also obtained the same result by transfecting a siRNA specific for CAPN1, the gene encoding for the catalytic subunit micro-calpain. Moreover, we studied the role of calpain in the PCNA-mediated switch between high fidelity replication and TLS upon UV irradiation. In mouse embryonic fibroblasts knockout for CAPNS1, USP1 downregulation is coupled to an increase in PCNA monoubiquitination. Moreover, CAPNS1-depleted U2OS cells showed an increase in the percentage of nuclei containing PCNA-induced foci upon UV irradiation. Since we demonstrated that calpain can modulate an important regulator of DNA damage response such as USP1, we investigated if calpain could have a role in genome integrity maintenance. CAPNS1 depleted cells showed a reduced rescue in DNA repair compared to control cells, suggesting that increased levels in PCNA monoubiquitination could lead to an increased amount of errore-prone TLS. Calpain plays an important role in autophagy, so we asked if USP1 degradation in absence of calpain activity could involve autophagic pathways. We first blocked macroautophagy by silencing ATG5, and we observed that USP1 was downregulated, suggesting that the depletion of ATG5 could lead to an increased activity of other degradation pathways. To impaire chaperone-mediated autophagy (CMA), we silenced a protein important for autophagosome formation, LAMP-2A. Also in this case we observed a decrease in USP1 protein levels, thus suggesting that USP1 is alternatively degraded by different pathways. However, we observed that USP1 is stabilized upon inhibition of lysosomal enzymes, suggesting that USP1 may be degraded in the lysosome. To better understand the mechanism by which calpain affect USP1 stability we search for an effect of calpain upon USP1 co-factor and activator UAF1/WDR48. CAPNS1-depleted cells showed WDR48 downregulation, but WDR48 overexpression only partially rescue USP1 protein levels in this cells. Furthermore, we provided evidences that calpain regulation of p35/p25 activator of Cdk5 can affect Cdh1 phosphorylation and thus APC/Cdh1 activity, leading to a regulation of USP1 stabilization. In conclusion, we identified USP1 as a novel interactor of calpain, and we found that calpain is important for USP1 stability, since in its absence USP1 is downregulated. The importance of this novel regulation is strengthened by the recent findings that unveiled a role of USP1 in maintenance of a mesenchymal stem cell program in osteosarcoma, and thus placing calpain in a crucial regulatory position for cancer development.
XXIV Ciclo
1983
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Book chapters on the topic "Ubiquitin-Specific Peptidase 1"

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Békés, Miklós, and Tony T. Huang. "Ubiquitin-specific Peptidase 1." In Handbook of Proteolytic Enzymes, 2079–85. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-382219-2.00468-3.

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Békés, Miklós. "Ubiquitin-Specific Peptidase 10." In Handbook of Proteolytic Enzymes, 2076–79. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-382219-2.00467-1.

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Jones, Amanda, Chao Xu, Jinrong Min, and Hengbin Wang. "Ubiquitin Specific Peptidase 16." In Handbook of Proteolytic Enzymes, 2090–94. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-382219-2.00470-1.

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Conference papers on the topic "Ubiquitin-Specific Peptidase 1"

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Liu, Xi, Yun Lu, Weiguo Hu, Zibo Chen, Lisa M. Mustachio, Jason Roszik, Lin Zheng, et al. "Abstract 2399: Loss of ubiquitin-specific peptidase 18 (USP18) destabilizes the regulator of thermogenesis uncoupling protein-1 (UCP-1) and represses lung cancer growth." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-2399.

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Liu, Xi, Yun Lu, Lin Zheng, David J. Sekula, Sarah J. Freemantle, and Ethan Dmitrovsky. "Abstract 24: Loss of ubiquitin-specific peptidase 18 (USP18) causes cold sensitive mice by destabilizing the critical regulator of thermogenesis: uncoupling protein-1 (UCP-1)." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-24.

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Singh, Mayank, Amy C. Burrows, Andrew Dickson, Komal Komal, Debjani Pal, and Matthew K. Summers. "Abstract 496: Ubiquitin specific peptidases 37 promotes constitutive replication fork movement by stabilizing Chk1 via its deubiquitination." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-496.

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