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Ubiquitin specific peptidase 15

USP15, ubiquitin specific peptidase-15, deubiquitinating enzyme USP15
This gene encodes a member of the ubiquitin specific protease (USP) family of deubiquitinating enzymes. USP enzymes play critical roles in ubiquitin-dependent processes through polyubiquitin chain disassembly and hydrolysis of ubiquitin-substrate bonds. The encoded protein associates with the COP9 signalosome, and also plays a role in transforming growth factor beta signalling through deubiquitination of receptor-activated SMAD transcription factors. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and a pseudogene of this gene is located on the long arm of chromosome 2. [provided by RefSeq, Nov 2011] (from NCBI)
Top mentioned proteins: Ubiquitin, CAN, Unp, V1a, Cullin
Papers on USP15
T Cell Intrinsic USP15 Deficiency Promotes Excessive IFN-γ Production and an Immunosuppressive Tumor Microenvironment in MCA-Induced Fibrosarcoma.
Sun et al., Shanghai, China. In Cell Rep, Jan 2016
USP15 is a deubiquitinase that negatively regulates activation of naive CD4(+) T cells and generation of IFN-γ-producing T helper 1 (Th1) cells.
Unravelling the mechanism of action of enzyme replacement therapy in Fabry disease.
Lee et al., Seoul, South Korea. In J Hum Genet, Nov 2015
Especially the catabolic process-related genes, including USP15 and ERUN1, showed direct increasing after ERT in vivo in male patients.
CHMP5 controls bone turnover rates by dampening NF-κB activity in osteoclasts.
Shim et al., Seoul, South Korea. In J Exp Med, Aug 2015
Biochemical analysis demonstrated that CHMP5 cooperates with the PDB genetic risk factor valosin-containing protein (VCP/p97) to stabilize the inhibitor of NF-κBα (IκBα), down-regulating ubiquitination of IκBα via the deubiquitinating enzyme USP15.
[Research progress on ubiquitin-specific protease in antiviral immunity].
Wei-Lin et al., Hangzhou, China. In Zhejiang Da Xue Xue Bao Yi Xue Ban, Jun 2015
USP2b, USP3, USP18, USP25, UL36USP and HAUSP play a role of antivirus; while USP4, USP13, USP15 and USP17 negatively regulate antiviral immune response.
The three 'P's of mitophagy: PARKIN, PINK1, and post-translational modifications.
Fon et al., Montréal, Canada. In Genes Dev, Jun 2015
Moreover, these modifications are reversible and can be disassembled by deubiquitinating enzymes (DUBs), including Ub-specific protease 8 (USP8), USP15, and USP30.
Tissue-specific Gene Expression in Rat Hearts and Aortas in a Model of Vascular Nitrate Tolerance.
Ferdinandy et al., Szeged, Hungary. In J Cardiovasc Pharmacol, May 2015
Of 7742 genes analyzed by DNA microarray, we found that although the expression of 25 genes changed significantly in the heart (increased: Tas2r119, Map6, Cd59, Kcnh2, Kcnh3, Senp6, Mcpt1, Tshb, Haus1, Vipr1, Lrn3, Lifr; decreased: Ihh, Fgfr1, Cryge, Krt9, Agrn, C4bpb, Fcer1a, Csf3, Hsd17b11, Hsd11b2, Ctnnbl1, Prpg1, Hsf1), only 14 genes were altered in the aorta (increased: Tas2r119, Ihh, Rrad, Npm1, Snai1; decreased: Tubb2b, Usp15, Sema6c, Wfdc2, Rps21, Ramp2, Galr1, Atxn1, Lhx1) in vascular nitrate tolerance.
Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis.
Komander et al., Cambridge, United Kingdom. In Embo J, Mar 2015
While Lys63-linked poly-phosphoUb is recognized by the TAB2 NZF Ub binding domain (UBD), 10 out of 12 deubiquitinases (DUBs), including USP8, USP15 and USP30, are impaired in hydrolyzing phosphoUb chains.
Evolution of the highly networked deubiquitinating enzymes USP4, USP15, and USP11.
Gray et al., Ottawa, Canada. In Bmc Evol Biol, 2014
BACKGROUND: USP4, USP15 and USP11 are paralogous deubiquitinating enzymes as evidenced by structural organization and sequence similarity.
USP15 regulates SMURF2 kinetics through C-lobe mediated deubiquitination.
Eichhorn et al., Singapore, Singapore. In Sci Rep, 2014
Here, we demonstrate that apart from targeting the TβR complex directly, USP15 also deubiquitinates SMURF2 resulting in enhanced TβR stability and downstream pathway activation.
Ubiquitin-specific Protease 15 Negatively Regulates Virus-induced Type I Interferon Signaling via Catalytically-dependent and -independent Mechanisms.
Xiao et al., Wuhan, China. In Sci Rep, 2014
Knockdown of endogenous USP15 augmented cellular antiviral responses.
Several fusion genes identified by whole transcriptome sequencing in a spindle cell sarcoma with rearrangements of chromosome arm 12q and MDM2 amplification.
Heim et al., Oslo, Norway. In Int J Oncol, 2014
RNA-Seq of the primary tumor identified four fusion genes, PTGES3-PTPRB, HMGA2-DYRK2, TMBIM4-MSRB3 and USP15-CNTN1, in which all the partner genes map to the q arm of chromosome 12.
USP15 stabilizes MDM2 to mediate cancer-cell survival and inhibit antitumor T cell responses.
Sun et al., Houston, United States. In Nat Immunol, 2014
Here we identified the DUB USP15 as a crucial negative regulator of T cell activation.
Ubiquitin removal in the TGF-β pathway.
Massagué et al., New York City, United States. In Nat Cell Biol, 2012
Both ubiquitin-specific peptidase-4 (USP4) and -15 (USP15) extend the life of activated receptors against the negative pressure of receptor-ubiquitinating complexes, but through distinct modes of action.
USP15 stabilizes TGF-β receptor I and promotes oncogenesis through the activation of TGF-β signaling in glioblastoma.
Seoane et al., Barcelona, Spain. In Nat Med, 2012
Our results show that USP15 regulates the TGF-beta pathway and is a key factor in glioblastoma pathogenesis
Structural variability of the ubiquitin specific protease DUSP-UBL double domains.
Barsukov et al., Liverpool, United Kingdom. In Febs Lett, 2011
structure of the double domain from USP15
USP15 is a deubiquitylating enzyme for receptor-activated SMADs.
Piccolo et al., Padova, Italy. In Nat Cell Biol, 2011
USP15 is critical for the occupancy of endogenous target promoters by the SMAD complex.
Structure of the USP15 N-terminal domains: a β-hairpin mediates close association between the DUSP and UBL domains.
Dreveny et al., Nottingham, United Kingdom. In Biochemistry, 2011
A 1.5 A resolution crystal structure of the human USP15 N-terminal domain revealed a 80 A elongated arrangement with the domains aligned in tandem.
Transgenic overexpression of USP15 in the heart induces cardiac remodeling in mice.
Nakajima et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2011
These results indicate that USP15 is involved in the regulation of hypertrophic responses in cardiac muscle through transcriptional and post-translational modulation of SLIM1.
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