DEK

Official Full Name

DEK proto-oncogene

Organism

Homo sapiens

Gene ID

7913

Background

This gene encodes a protein with one SAP domain. This protein binds to cruciform and superhelical DNA and induces positive supercoils into closed circular DNA, and is also involved in splice site selection during mRNA processing. Chromosomal aberrations involving this region, increased expression of this gene, and the presence of antibodies against this protein are all associated with various diseases. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2008]

Synonyms

D6S231E

Cat.No.	Product Name	Price
CSC-DC004207	Panoply™ Human DEK Knockdown Stable Cell Line	Inquiry
CSC-SC004207	Panoply™ Human DEK Over-expressing Stable Cell Line	Inquiry
CLKO-0895	DEK KO Cell Lysate-HEK293T	Inquiry

Cat.No.	Product Name	Price
AD04771Z	Human DEK adenoviral particles	Inquiry
LV10584L	human DEK (NM_001134709) lentivirus particles	Inquiry
LV10585L	human DEK (NM_003472) lentivirus particles	Inquiry

Cat.No.	Product Name	Price
SHH001153	shRNA set against Rat Dek(NM_001004255.1)	Inquiry
SHH001171	shRNA set against Human DEK(NM_003472.3)	Inquiry
SHH276981	shRNA set against Human DEK (NM_003472.3)	Inquiry
SHH276985	shRNA set against Mouse DEK (NM_025900.2)	Inquiry
SHH276989	shRNA set against Rat DEK (NM_001004255.1)	Inquiry
SHW000874	shRNA set against Chicken DEK (NM_001012560)	Inquiry
SHW010159	shRNA set against Danio rerio DEK (NM_001045276)	Inquiry

Cat.No.	Product Name	Price
CDFH004976	Human DEK cDNA Clone(NM_001134709.1)	Inquiry
CDFR001402	Rat Dek cDNA Clone(NM_001004255.1)	Inquiry
MiUTR1H-02768	DEK miRNA 3'UTR clone	Inquiry
MiUTR1R-01464	DEK miRNA 3'UTR clone	Inquiry
MiUTR3H-00642	DEK miRNA 3'UTR clone	Inquiry
SKO0427	DEK Validated sgRNA vector	Inquiry
CDCB158682	Human DEK ORF clone (BC035259)	Inquiry
CDCB162349	Chicken DEK ORF Clone (NM_001012560)	Inquiry
CDCB171634	Danio rerio DEK ORF Clone (NM_001045276)	Inquiry
CDCB193307	Rabbit DEK ORF clone (XM_002720860.2)	Inquiry
CDCR054876	Human DEK ORF clone (NM_001134709.1)	Inquiry
CDCR257809	Mouse Dek ORF Clone(NM_025900.2)	Inquiry
CDCR285688	Human DEK ORF Clone(NM_003472.3)	Inquiry
CDCR368453	Rat Dek ORF Clone(NM_001004255.1)	Inquiry
CDCS408020	Human DEK ORF Clone (BC035259)	Inquiry

Detailed Information

DEK is a strongly conserved nuclear factor and the only member of its class of proteins expressed primarily in proliferatively active and pernicious cells, with up to 4-6 million copies of DEK per cell nucleus. DEK was originally described as a target of recurrent translocations in patients with acute myeloid leukemia (AML). Subsequently, DEK has been shown to promote tumorigenesis in a variety of cancer cell types, at least in part because it disrupts cell division or DNA repair, inhibits cell differentiation, senescence, and apoptosis, and cooperates with transforming oncogenes.

Structure and Function of DEK

The majority of DEK binds to chromatin, mainly in the euchromatin region of chromatin, but can also be found in the nuclear matrix or in clusters of interchromatin granules. Although DEK exhibits some sequence-specific DNA binding, it seems to recognize mainly structural features (cruciform and super helical DNA). DEK has two major structural domains responsible for interaction with DNA. Residues 87 to 187 are homologous to the structural domain of the scaffold attachment factor box (SAF-box) found in several nuclear proteins. The second domain, composed of residues 270 to 350 in the carboxy-terminal region of the DEK protein, is also responsible for multimerization. Although the most well-known oncogenic property of DEK is related to DNA binding, a portion of DEK (about 10%) is associated with RNA and regulates RNA processing. Thus, DEK can influence the recognition of the 3' splice site by the splicing factor U2AF. In addition, DEK interacts with SR (serine/arginine-rich) proteins and other factors involved in the exon-exon junction complex, but the functional relevance of these interactions in cancer remains to be clarified.

Role of DEK in Tumor Progression and Drug Response

DEK has been implicated in tumor development. In malignant myeloid cells, DEK-NUP214 exposure is associated with a generalized activation of protein synthesis and increased phosphorylation of eIF4E, a key factor in transmission initiation and a marker of translational activity. In conclusion, the DEK-NUP214 fusion protein was found to be impaired in its ability to bind to histones and its translational activity in 293T cells was also affected. ability to bind to histones and to be phosphorylated by CK2α and CK2β.

DEK Works as A Drug Target

DEK is an abundant polymitotic factor that binds to large swaths of chromatin. Interfering with DEK function can cause intolerable side effects in normal cells. However, the fact that DEK-deficient mice survive and DEK-deficient tumor cells go into senescence or apoptosis is evidence of a DEK-dependent "carcinogenic addiction." The feasibility and efficacy of sustained down-regulation of DEK in physiologically relevant tumor models or clinical settings remains to be demonstrated. However，the development of new siRNA delivery strategies and the realization that normal cells may be less sensitive to DEK downregulation are less sensitive to DEK downregulation than their hyperproliferative counterparts, providing a window for therapeutic intervention. The fact that DEK controls the tolerance of tumor cells to genotoxic drugs may also serve as a guide for rational compound selection. better synergize with DEK inhibitors. The observation that DEK is released from apoptotic cells and produces autoantibodies may also provide an alternative approach to assessing drug efficacy in pharmacodynamics. Alternative methods for assessing drug efficacy in pharmacokinetic or pharmacodynamic studies of proapoptotic agents.

References:

Riveiro-Falkenbach E, Soengas MS. Control of tumorigenesis and chemoresistance by the DEK oncogene. Clin Cancer Res. 2010;16(11):2932-2938. doi:10.1158/1078-0432.CCR-09-2330
Sandén C, Gullberg U. The DEK oncoprotein and its emerging roles in gene regulation. Leukemia. 2015;29(8):1632-1636. doi:10.1038/leu.2015.72

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