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Gene Review

ELK4  -  ELK4, ETS-domain protein (SRF accessory...

Homo sapiens

Synonyms: ETS domain-containing protein Elk-4, SAP-1, SAP1, SRF accessory protein 1, Serum response factor accessory protein 1
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Disease relevance of ELK4


Psychiatry related information on ELK4

  • This region can be functionally replaced by fusion of Id proteins to SAP-1, whereby the Id moiety then acts to repress DNA binding in cis [6].

High impact information on ELK4


Biological context of ELK4

  • Secreted aspartyl proteinases (Saps), encoded by a gene family with at least nine members (SAP1 to SAP9), are one of the most discussed virulence factors produced by the human pathogen Candida albicans [11].
  • Here, we have studied the role of HLH motifs in regulating DNA binding and transcription by the TCF protein SAP-1 and how Cdk-mediated phosphorylation affects the inhibitory activity of the Id proteins towards the TCFs [6].
  • These docking domains are found in a range of substrates, including the transcription factors myocyte enhancer factor-2A and SAP-1 [12].
  • The c-fos promoter contains a serum response element (SRE) that mediates ternary complex formation with the Ets proteins SAP-1 or Elk-1 and the MADS-box protein, serum response factor (SRF) [13].
  • Comparison with the published nucleotide sequence for the precursor form of the human activator protein for sulfatide sulfatase (SAP-1) suggested that this activator also has a possibly glycosylated Asn and 6 Cys residues at similar positions, although the remainder of the molecule is somewhat different [14].

Anatomical context of ELK4


Associations of ELK4 with chemical compounds


Physical interactions of ELK4

  • Crystal structure of a ternary SAP-1/SRF/c-fos SRE DNA complex [13].

Other interactions of ELK4

  • Three additional smaller regions show homology to the ELK-1 and SAP-1 genes, a subgroup of the ets gene family that interacts with the serum response factor [23].
  • ELK4 (previously known as SAP-1 [SRF-associated protein-1]) is ubiquitously expressed [24].
  • These data provide further evidence for a crucial role of Sap1 and Sap2 in C. albicans vaginal infections [1].
  • Our results indicate that stratifin markedly increase Elk4/Sap1 mRNA expression in a time-dependent fashion [15].
  • The characters high proteinase and increased virulence were not associated with a single molecular type or category identifiable through DNA fingerprinting or pulsed-field electrophoretic karyotype, and both SAP1 and SAP2 genes were present in both categories of isolates, on the same respective chromosomes [25].

Analytical, diagnostic and therapeutic context of ELK4

  • The genes of two different aspartic proteinases from C. albicans, SAP1 and SAP2, with an overall homology of 77% in their nucleotide sequences, were chosen as targets for PCR [26].
  • Using rabbit antibodies against human SAP-1 it could be visualized in extracts from cultured human skin fibroblasts after sodium dodecylsulfate-polyacrylamide gel electrophoresis, followed by electroblotting to nitrocellulose membrane and immunochemical staining (Western blotting) [21].
  • In the rat extracorporeal circulation system, the hSAP level in the inlet blood to the IAM module decreased to 49% of the initial concentration within 60 min [27].
  • To determine the value of the hSAP in human or rat plasma, we also developed a simple ELISA [27].


  1. The secreted aspartyl proteinases Sap1 and Sap2 cause tissue damage in an in vitro model of vaginal candidiasis based on reconstituted human vaginal epithelium. Schaller, M., Bein, M., Korting, H.C., Baur, S., Hamm, G., Monod, M., Beinhauer, S., Hube, B. Infect. Immun. (2003) [Pubmed]
  2. Additional biochemical findings in a patient and fetal sibling with a genetic defect in the sphingolipid activator protein (SAP) precursor, prosaposin. Evidence for a deficiency in SAP-1 and for a normal lysosomal neuraminidase. Paton, B.C., Schmid, B., Kustermann-Kuhn, B., Poulos, A., Harzer, K. Biochem. J. (1992) [Pubmed]
  3. In vivo analysis of secreted aspartyl proteinase expression in human oral candidiasis. Naglik, J.R., Newport, G., White, T.C., Fernandes-Naglik, L.L., Greenspan, J.S., Greenspan, D., Sweet, S.P., Challacombe, S.J., Agabian, N. Infect. Immun. (1999) [Pubmed]
  4. Invasion of Candida albicans correlates with expression of secreted aspartic proteinases during experimental infection of human epidermis. Schaller, M., Schackert, C., Korting, H.C., Januschke, E., Hube, B. J. Invest. Dermatol. (2000) [Pubmed]
  5. Developmental and liver-specific expression directed by the serum amyloid P component promoter in transgenic mice. Zhao, X., Araki, K., Miyazaki, J., Yamamura, K. J. Biochem. (1992) [Pubmed]
  6. Regulation of TCF ETS-domain transcription factors by helix-loop-helix motifs. Stinson, J., Inoue, T., Yates, P., Clancy, A., Norton, J.D., Sharrocks, A.D. Nucleic Acids Res. (2003) [Pubmed]
  7. Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element. Dalton, S., Treisman, R. Cell (1994) [Pubmed]
  8. Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element. Dalton, S., Treisman, R. Cell (1992) [Pubmed]
  9. Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus. O'Brien, J.S., Kretz, K.A., Dewji, N., Wenger, D.A., Esch, F., Fluharty, A.L. Science (1988) [Pubmed]
  10. The B-box dominates SAP-1-SRF interactions in the structure of the ternary complex. Hassler, M., Richmond, T.J. EMBO J. (2001) [Pubmed]
  11. Disruption of each of the secreted aspartyl proteinase genes SAP1, SAP2, and SAP3 of Candida albicans attenuates virulence. Hube, B., Sanglard, D., Odds, F.C., Hess, D., Monod, M., Schäfer, W., Brown, A.J., Gow, N.A. Infect. Immun. (1997) [Pubmed]
  12. Specificity determinants in MAPK signaling to transcription factors. Barsyte-Lovejoy, D., Galanis, A., Sharrocks, A.D. J. Biol. Chem. (2002) [Pubmed]
  13. Crystal structure of a ternary SAP-1/SRF/c-fos SRE DNA complex. Mo, Y., Ho, W., Johnston, K., Marmorstein, R. J. Mol. Biol. (2001) [Pubmed]
  14. The activator protein for glucosylceramide beta-glucosidase from guinea pig liver. Improved isolation method and complete amino acid sequence. Sano, A., Radin, N.S., Johnson, L.L., Tarr, G.E. J. Biol. Chem. (1988) [Pubmed]
  15. Stratifin-induced matrix metalloproteinase-1 in fibroblast is mediated by c-fos and p38 mitogen-activated protein kinase activation. Lam, E., Kilani, R.T., Li, Y., Tredget, E.E., Ghahary, A. J. Invest. Dermatol. (2005) [Pubmed]
  16. Analysis of SRF, SAP-1 and ELK-1 transcripts and proteins in human cell lines. Magnaghi-Jaulin, L., Masutani, H., Lipinski, M., Harel-Bellan, A. FEBS Lett. (1996) [Pubmed]
  17. Secreted aspartyl proteinases and interactions of Candida albicans with human endothelial cells. Ibrahim, A.S., Filler, S.G., Sanglard, D., Edwards, J.E., Hube, B. Infect. Immun. (1998) [Pubmed]
  18. Altered adherence in strains of Candida albicans harbouring null mutations in secreted aspartic proteinase genes. Watts, H.J., Cheah, F.S., Hube, B., Sanglard, D., Gow, N.A. FEMS Microbiol. Lett. (1998) [Pubmed]
  19. Structure of a filamentous phosphoglycoprotein polymer: the secreted acid phosphatase of Leishmania mexicana. Stierhof, Y.D., Wiese, M., Ilg, T., Overath, P., Häner, M., Aebi, U. J. Mol. Biol. (1998) [Pubmed]
  20. Molecular cloning of Elk-3, a new member of the Ets family expressed during mouse embryogenesis and analysis of its transcriptional repression activity. Nozaki, M., Onishi, Y., Kanno, N., Ono, Y., Fujimura, Y. DNA Cell Biol. (1996) [Pubmed]
  21. The gene coding for a sphingolipid activator protein, SAP-1, is on human chromosome 10. Inui, K., Kao, F.T., Fujibayashi, S., Jones, C., Morse, H.G., Law, M.L., Wenger, D.A. Hum. Genet. (1985) [Pubmed]
  22. Biosynthesis of the sulfatide/GM1 activator protein (SAP-1) in control and mutant cultured skin fibroblasts. Fujibayashi, S., Wenger, D.A. Biochim. Biophys. Acta (1986) [Pubmed]
  23. ERP, a new member of the ets transcription factor/oncoprotein family: cloning, characterization, and differential expression during B-lymphocyte development. Lopez, M., Oettgen, P., Akbarali, Y., Dendorfer, U., Libermann, T.A. Mol. Cell. Biol. (1994) [Pubmed]
  24. Serum response factor binding sites differ in three human cell types. Cooper, S.J., Trinklein, N.D., Nguyen, L., Myers, R.M. Genome Res. (2007) [Pubmed]
  25. Elevated aspartic proteinase secretion and experimental pathogenicity of Candida albicans isolates from oral cavities of subjects infected with human immunodeficiency virus. De Bernardis, F., Chiani, P., Ciccozzi, M., Pellegrini, G., Ceddia, T., D'Offizzi, G., Quinti, I., Sullivan, P.A., Cassone, A. Infect. Immun. (1996) [Pubmed]
  26. A method for recovery of Candida albicans DNA from larger blood samples and its detection by polymerase chain reaction on proteinase genes. Reichard, U., Margraf, S., Hube, B., Rüchel, R. Mycoses (1997) [Pubmed]
  27. Selective removal of human serum amyloid P component from rat blood by use of an immunoaffinity membrane in an extracorporeal circulation system. Adachi, T., Mogi, M., Harada, M., Kojima, K. J. Chromatogr. B, Biomed. Appl. (1996) [Pubmed]
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