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Gene Review

qkr58E-3  -  quaking related 58E-3

Drosophila melanogaster

Synonyms: CG3584, Dmel\CG3584, KEP1, QKR58E-3, kep1, ...
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Disease relevance of qkr58E-3


High impact information on qkr58E-3

  • We found that Kep1 bound dredd RNA in vitro, and that extracts prepared from kep1 mutant ovaries had markedly reduced proteolytic cleavage activity toward the caspase-8 target substrate IETD-7-amino-4-trifluoromethyl coumarin [1].
  • We have previously shown that kep1 can induce apoptosis when transfected into different cell lines [1].
  • The Drosophila kep1 gene encodes an RNA binding protein related to the murine QUAKING apoptotic inducer [1].
  • Here we report the identification of two novel Drosophila KH domain proteins, which we termed KEP1 (KH encompassing protein) and SAM [2].
  • The identification of KEP1 and SAM implies that a large GSG domain protein family exists and helps redefine the boundaries of the GSG domain [2].

Biological context of qkr58E-3

  • Taken together, our data suggest that KEP1 and SAM may play a role in the activation or regulation of apoptosis and further implicate the GSG domain in RNA binding and oligomerization [2].
  • Mutations in the Drosophila kep1 gene, encoding a single maxi KH (K homology) domain-containing RNA-binding protein, result in a reduction of fertility in part due to the disruption of the apoptotic programme during oogenesis [3].
  • This modulation in splicing was not observed in the parental NIH 3T3 cell line in which we obtained 7.5% exon 5 inclusion following kep1 transfection [3].
  • Using a CD44v5 alternative splicing reporter construct, we observed 99% inclusion of the alternatively spliced exon 5 following kep1 transfection in a cell line that constitutively expresses activated Src [3].

Regulatory relationships of qkr58E-3

  • Taken together, our results suggest that Kep1 regulates apoptosis by influencing the processing of dredd RNA [1].

Other interactions of qkr58E-3

  • KEP1 and Who/How were nuclear and SAM was cytoplasmic [2].
  • We observed increased levels of the beta isoform of dredd mRNA in kep1 mutants as compared with wild-type [1].


  1. Kep1 interacts genetically with dredd/caspase-8, and kep1 mutants alter the balance of dredd isoforms. Di Fruscio, M., Styhler, S., Wikholm, E., Boulanger, M.C., Lasko, P., Richard, S. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  2. The identification of two Drosophila K homology domain proteins. Kep1 and SAM are members of the Sam68 family of GSG domain proteins. Di Fruscio, M., Chen, T., Bonyadi, S., Lasko, P., Richard, S. J. Biol. Chem. (1998) [Pubmed]
  3. Phosphorylation status of the Kep1 protein alters its affinity for its protein binding partner alternative splicing factor ASF/SF2. Robard, C., Daviau, A., Di Fruscio, M. Biochem. J. (2006) [Pubmed]
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