Jump to content

DDX3X

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Rjwilmsi (talk | contribs) at 09:05, 5 March 2018 (Journal cites:,). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

DDX3X
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesDDX3X, DBX, DDX14, DDX3, HLP2, CAP-Rf, MRX102, DEAD-box helicase 3, X-linked, DEAD-box helicase 3 X-linked, MRXSSB
External IDsOMIM: 300160; MGI: 103064; HomoloGene: 3425; GeneCards: DDX3X; OMA:DDX3X - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001193416
NM_001193417
NM_001356
NM_024005
NM_001363819

NM_010028
NM_008015

RefSeq (protein)

NP_001180345
NP_001180346
NP_001347
NP_001350748

NP_034158

Location (UCSC)Chr X: 41.33 – 41.36 MbChr X: 13.15 – 13.16 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

ATP-dependent RNA helicase DDX3X is an enzyme that in humans is encoded by the DDX3X gene.[5][6][7]

Function

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which interacts specifically with hepatitis C virus core protein resulting a change in intracellular location. This gene has a homolog located in the nonrecombining region of the Y chromosome. The protein sequence is 91% identical between this gene and the Y-linked homolog.[7]

Role in cancer

DDX3X is involved in many different types of cancer. For example, it is abnormally expressed in breast epithelial cancer cells in which its expression is activated by HIF1A during hypoxia.[8] Increased expression of DDX3X by HIF1A in hypoxia is initiated by the direct binding of HIF1A to the HIF1A response element,[8] as verified with chromatin immunoprecipitation and luciferase reporter assay. Since the expression of DDX3X is affected by the activity of HIF1A, the co-localization of these proteins has also been demonstrated in MDA-MB-231 xenograft tumor samples.[8]

In HeLa cells DDX3X is reported to control cell cycle progression through Cyclin E1.[9] More specifically, DDX3X was shown to directly bind to the 5´ UTR of Cyclin E1 and thereby facilitating the translation of the protein. Increased protein levels of Cyclin E1 was demonstrated to mediate the transition of S phase entry.[9]

Clinical significance

Mutations of the DDX3X gene are also associated with medulloblastoma.[10][11][12]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000215301Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000000787Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Lahn BT, Page DC (October 1997). "Functional coherence of the human Y chromosome". Science. 278 (5338): 675–80. doi:10.1126/science.278.5338.675. PMID 9381176.
  6. ^ Park SH, Lee SG, Kim Y, Song K (Oct 1998). "Assignment of a human putative RNA helicase gene, DDX3, to human X chromosome bands p11.3→p11.23". Cytogenetics and Cell Genetics. 81 (3–4): 178–9. doi:10.1159/000015022. PMID 9730595.
  7. ^ a b "Entrez Gene: DDX3X DEAD (Asp-Glu-Ala-Asp) box polypeptide 3, X-linked".
  8. ^ a b c Botlagunta M, Krishnamachary B, Vesuna F, Winnard PT, Bol GM, Patel AH, Raman V (March 2011). "Expression of DDX3 is directly modulated by hypoxia inducible factor-1 alpha in breast epithelial cells". PLOS One. 6 (3). PLOS One: e17563. doi:10.1371/journal.pone.0017563. PMC 3063174. PMID 21448281.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  9. ^ a b Lai MC, Chang WC, Shieh SY, Tarn WY (November 2010). "DDX3 regulates cell growth through translational control of cyclin E1". Molecular and Cellular Biology. 30 (22). Molecular and Cellular Biology: 5444–53. doi:10.1128/MCB.00560-10. PMC 2976371. PMID 20837705.
  10. ^ Robinson G, Parker M, Kranenburg TA, Lu C, Chen X, Ding L, et al. (August 2012). "Novel mutations target distinct subgroups of medulloblastoma". Nature. 488 (7409): 43–8. doi:10.1038/nature11213. PMC 3412905. PMID 22722829.
  11. ^ Jones DT, Jäger N, Kool M, Zichner T, Hutter B, Sultan M, et al. (August 2012). "Dissecting the genomic complexity underlying medulloblastoma". Nature. 488 (7409): 100–5. doi:10.1038/nature11284. PMC 3662966. PMID 22832583.
  12. ^ Pugh TJ, Weeraratne SD, Archer TC, Pomeranz Krummel DA, Auclair D, Bochicchio J, et al. (August 2012). "Medulloblastoma exome sequencing uncovers subtype-specific somatic mutations". Nature. 488 (7409): 106–10. doi:10.1038/nature11329. PMC 3413789. PMID 22820256.

Further reading