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Ubiquitin specific peptidase 14

This gene encodes a member of the ubiquitin-specific processing (UBP) family of proteases that is a deubiquitinating enzyme (DUB) with His and Cys domains. This protein is located in the cytoplasm and cleaves the ubiquitin moiety from ubiquitin-fused precursors and ubiquitinylated proteins. Mice with a mutation that results in reduced expression of the ortholog of this protein are retarded for growth, develop severe tremors by 2 to 3 weeks of age followed by hindlimb paralysis and death by 6 to 10 weeks of age. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, CAN, V1a, UCH37, PrP
Papers on USP14
Downregulation of ubiquitin-specific protease 14 (USP14) inhibits breast cancer cell proliferation and metastasis, but promotes apoptosis.
Wang et al., Nantong, China. In J Mol Histol, Feb 2016
Previously, evidence suggested that ubiquitin-specific protease 14 (USP14) was associated with various signal transduction pathways and tumourigenesis.
The tumor suppressor role of miR-4782-3p in hepatocellular carcinoma.
Liu et al., Chengdu, China. In Oncol Rep, Feb 2016
We confirmed that USP14 was targeted by miR-4782-3p in HCC cells.
The role of Ubiquitin-specific protease 14 (USP14) in cell adhesion-mediated drug resistance(CAM-DR) of multiple myeloma cells.
He et al., Nantong, China. In Eur J Haematol, Jan 2016
Ubiquitin-specific protease 14 (USP14) is down-regulated in the apoptotic model and up-regulated in the adhesive model of MM.
A new ER-specific photosensitizer unravels (1)O2-driven protein oxidation and inhibition of deubiquitinases as a generic mechanism for cancer PDT.
Feron et al., Brussels, Belgium. In Oncogene, Jan 2016
This new class of PS unraveled an unsuspected common mechanism of action for PS that involves the combined inhibition of the mammalian target of rapamycin (mTOR) signaling pathway and proteasomal deubiquitinases (DUBs) USP14 and UCH37.
Reversible ubiquitination shapes NLRC5 function and modulates NF-κB activation switch.
Cui et al., Guangzhou, China. In J Cell Biol, Jan 2016
Meanwhile, we found USP14 specifically removes the polyubiquitin chains from NLRC5 to enhance NLRC5-mediated inhibition of NF-κB signaling.
Deubiquitinases Modulate Platelet Proteome Ubiquitination, Aggregation, and Thrombosis.
McIntyre et al., Cleveland, United States. In Arterioscler Thromb Vasc Biol, Dec 2015
Platelets express the proteasome-associated deubiquitinases USP14 and UCHL5, and selective inhibition of these enzymes by b-AP15 reproduced the inhibitory effect of the general deubiquitinase inhibitors on ex vivo platelet function.
Inhibition of proteasome deubiquitinase activity: a strategy to overcome resistance to conventional proteasome inhibitors?
D'Arcy et al., Linköping, Sweden. In Drug Resist Updat, Jul 2015
In particular, pharmacological inhibition of the proteasomal cysteine DUBs (i.e., USP14 and UCHL5) has been shown to be particularly cytotoxic to cancer cells and inhibit tumour growth in several in vivo models.
Deubiquitinase inhibition as a cancer therapeutic strategy.
Linder et al., Linköping, Sweden. In Pharmacol Ther, Mar 2015
USP14 and UCHL5) can be predicted to be particularly cytotoxic to cancer cells as it leads to blocking of proteasome function and accumulation of proteasomal substrates.
Phosphorylation and activation of ubiquitin-specific protease-14 by Akt regulates the ubiquitin-proteasome system.
Yuan et al., Shanghai, China. In Elife, 2014
Here we show that USP14, a major deubiquitinating enzyme that regulates the UPS, is a substrate of Akt, a serine/threonine-specific protein kinase critical in mediating intracellular signaling transducer for growth factors.
Inhibition of 19S proteasome-associated deubiquitinases by metal-containing compounds.
Liu et al., Guangzhou, China. In Oncoscience, 2014
Recently, we have reported that the anti-cancer activity of copper (II) pyrithione CuPT and gold (I) complex auranofin is associated with targeting the 19S proteasome-associated deubiquitinases (DUBs), UCHL5 and USP14.
Deubiquitinases in skeletal muscle atrophy.
Wing, Canada. In Int J Biochem Cell Biol, 2013
Instead several deubiquitinases are induced in atrophying muscle, in particular USP19 and USP14.
Proteasome deubiquitinases as novel targets for cancer therapy.
Linder et al., Stockholm, Sweden. In Int J Biochem Cell Biol, 2012
b-AP15 inhibits two proteasome-associated DUBs, USP14 and UCHL5, resulting in a rapid accumulation of high molecular weight ubiquitin conjugates and a functional proteasome shutdown.
Inhibition of proteasome deubiquitinating activity as a new cancer therapy.
Linder et al., Stockholm, Sweden. In Nat Med, 2011
b-AP15 inhibited the activity of two 19S regulatory-particle-associated deubiquitinases, ubiquitin C-terminal hydrolase 5 (UCHL5) and ubiquitin-specific peptidase 14 (USP14), resulting in accumulation of polyubiquitin.
Ubiquitin-specific protease 14 expression associated with intrahepatic cholangiocarcinoma cell differentiation.
Petmitr et al., Lang Suan, Thailand. In Asian Pac J Cancer Prev, 2010
High Ubiquitin-specific protease 14 expression associated with intrahepatic cholangiocarcinoma cell differentiation.
Enhancement of proteasome activity by a small-molecule inhibitor of USP14.
Finley et al., Boston, United States. In Nature, 2010
Here we show that USP14, a proteasome-associated deubiquitinating enzyme, can inhibit the degradation of ubiquitin-protein conjugates both in vitro and in cells.
The proteasome-associated deubiquitinating enzyme Usp14 is essential for the maintenance of synaptic ubiquitin levels and the development of neuromuscular junctions.
Wilson et al., Birmingham, United States. In J Neurosci, 2009
Data from transgenic mice define a critical role for Usp14 at mammalian synapses and suggest a requirement for local ubiquitin recycling by the proteasome to control the development and function of neuromuscular junctions.
The ataxia (axJ) mutation causes abnormal GABAA receptor turnover in mice.
Kneussel et al., Hamburg, Germany. In Plos Genet, 2009
A mutated axJ gene locus, encoding the ubiquitin-specific protease 14 (Usp14), negatively influences GABAA receptor turnover.
USP14 inhibits ER-associated degradation via interaction with IRE1alpha.
Ichijo et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2009
These findings suggest that USP14 is a novel player in the unfolded protein response by serving as a physiological inhibitor of ER-associated degradation under the non-stressed condition.
Differential effects of Usp14 and Uch-L1 on the ubiquitin proteasome system and synaptic activity.
Wilson et al., Birmingham, United States. In Mol Cell Neurosci, 2008
Results suggest that Uch-L1 and Usp14 may differentially affect the ubiquitin proteasome system and synaptic activity by regulating different pools of ubiquitin in the cell.
Synaptic defects in ataxia mice result from a mutation in Usp14, encoding a ubiquitin-specific protease.
Jenkins et al., Frederick, United States. In Nat Genet, 2002
USP14 has a role in regulating synaptic activity in mammals
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