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Ubiquitin specific peptidase 28

USP28
The ubiquitin-dependent protein degradation pathway is essential for proteolysis of intracellular proteins and peptides. Enzymes that remove ubiquitin from ubiquitin-conjugated peptides, like USP28, affect the fate and degradation of intracellular proteins and are essential for maintenance of cell-free ubiquitin pools (Valero et al., 2001).[supplied by OMIM, Mar 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, c-Myc, CAN, Cdc4, V1a
Papers using USP28 antibodies
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs.
Supplier
Marfany Gemma et al., In Genome Biology, 1996
... USP28 cDNA cloningTo screen cDNA libraries from human fetal brain, placenta and kidney (Clontech), specific primers of the ...
Papers on USP28
BRAF inhibitor resistance enhances vulnerability to arginine deprivation in melanoma.
New
Savaraj et al., Miami, United States. In Oncotarget, Feb 2016
Furthermore, our study uncovers that downregulation of deubiquitinase USP28 which results in more active c-Myc degradation via ubiquitin-proteasome machinery is the primary mechanism for inability to re-express ASS1 upon arginine deprivation in BR cells.
Deubiquitinating c-Myc: USP36 steps up in the nucleolus.
New
Dai et al., Portland, United States. In Cell Cycle, Jan 2016
An early study showed that USP28 deubiquitinates c-Myc via interacting with Fbw7α whereas a recent study reveals that USP37 deubiquitinates c-Myc independently of Fbw7 and c-Myc phosphorylation.
The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights.
New
Zhang et al., Shanghai, China. In Biochem J, Nov 2015
The deubiquitinase ubiquitin-specific protease 28 (Usp28) contains a ubiquitin-binding region (UBR) composed of one ubiquitin-associated domain (UBA) and one ubiquitin-interacting motif (UIM) at its N-terminus.
Fbw7 and its counteracting forces in stem cells and cancer: Oncoproteins in the balance.
Review
New
Behrens et al., London, United Kingdom. In Semin Cancer Biol, Oct 2015
We discuss mechanisms that regulate ubiquitination by Fbw7, including ubiquitin-specific proteases such as USP28 that counteract Fbw7 activity and thereby stabilise oncoproteins.
Ubiquitin-specific protease 28 is overexpressed in human glioblastomas and contributes to glioma tumorigenicity by regulating MYC expression.
New
Qin et al., Weifang, China. In Exp Biol Med (maywood), Aug 2015
Deubiquitinase ubiquitin-specific protease 28 (USP28) stabilizes oncogenic factors, including MYC.
Usp28 counteracts Fbw7 in intestinal homeostasis and cancer.
New
Behrens et al., London, United Kingdom. In Cancer Res, May 2015
This activity is antagonized by the deubiquitinase Usp28, which is highly expressed in murine and human intestinal cancers.
Overexpression of deubiquitinating enzyme USP28 promoted non-small cell lung cancer growth.
New
Qian et al., Nanjing, China. In J Cell Mol Med, Apr 2015
However, the role of USP28 in NSCLC is unknown.
Regulation of USP28 deubiquitinating activity by SUMO conjugation.
Reverter et al., Barcelona, Spain. In J Biol Chem, 2015
USP28 (ubiquitin-specific protease 28) is a deubiquitinating enzyme that has been implicated in the DNA damage response, the regulation of Myc signaling, and cancer progression.
Dual regulation of Fbw7 function and oncogenic transformation by Usp28.
Popov et al., Würzburg, Germany. In Cell Rep, 2014
Fbw7-dependent substrate ubiquitination is antagonized by the Usp28 deubiquitinase.
The deubiquitinase USP28 controls intestinal homeostasis and promotes colorectal cancer.
Behrens et al., In J Clin Invest, 2014
The deubiquitinase USP28 stabilizes oncogenic factors, including c-MYC; however, the contribution of USP28 in tumorigenesis, particularly in the intestine, is unknown.
GSK-3β regulates cell growth, migration, and angiogenesis via Fbw7 and USP28-dependent degradation of HIF-1α.
GeneRIF
Kietzmann et al., Oulu, Finland. In Blood, 2012
A new pathway that could be targeted at the level of GSK-3, Fbw7, or USP28 to influence HIF-1alpha-dependent processes like angiogenesis and metastasis.
Emerging roles of deubiquitinases in cancer-associated pathways.
Review
Urbé et al., Liverpool, United Kingdom. In Iubmb Life, 2010
They may regulate the stability of key oncogenes, exemplified by USP28 stabilisation of c-Myc.
Mutational evolution in a lobular breast tumour profiled at single nucleotide resolution.
Impact
Aparicio et al., Vancouver, Canada. In Nature, 2009
Five of the 32 mutations (in ABCB11, HAUS3, SLC24A4, SNX4 and PALB2) were prevalent in the DNA of the primary tumour removed at diagnosis 9 years earlier, six (in KIF1C, USP28, MYH8, MORC1, KIAA1468 and RNASEH2A) were present at lower frequencies (1-13%), 19 were not detected in the primary tumour, and two were undetermined.
The Cdc14B-Cdh1-Plk1 axis controls the G2 DNA-damage-response checkpoint.
Impact
Pagano et al., New York City, United States. In Cell, 2008
However, this process is counteracted by the deubiquitylating enzyme Usp28 to permit Claspin-mediated activation of Chk1 in response to DNA damage.
Fbw7 and Usp28 regulate myc protein stability in response to DNA damage.
GeneRIF
Eilers et al., Marburg an der Lahn, Germany. In Cell Cycle, 2007
Usp28 dissociates from Fbw7alpha in response to UV irradiation, providing a mechanism how Fbw7-mediated degradation of Myc is enhanced upon DNA damage.
The ubiquitin-specific protease USP28 is required for MYC stability.
Impact
GeneRIF
Eilers et al., Marburg an der Lahn, Germany. In Nat Cell Biol, 2007
High expression levels of USP28 are found in colon and breast carcinomas, and stabilization of MYC by USP28 is essential for tumour-cell proliferation.
A role for the deubiquitinating enzyme USP28 in control of the DNA-damage response.
Impact
GeneRIF
Elledge et al., Boston, United States. In Cell, 2006
Using a human cell line that faithfully recapitulated the Chk2-p53-PUMA pathway, we show that USP28 is required to stabilize Chk2 and 53BP1 in response to DNA damage.
Characterization of alternatively spliced products and tissue-specific isoforms of USP28 and USP25.
GeneRIF
Marfany et al., Barcelona, Spain. In Genome Biol, 2000
molecular cloning of USP28 & characterization of alternatively spliced products and tissue-specific isoforms
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