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Gene Review

HLH106  -  Helix loop helix protein 106

Drosophila melanogaster

Synonyms: CG8522, Dmel\CG8522, HlH106, SREBP, Srebp, ...
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Disease relevance of HLH106

  • Results of an earlier study showed that efficient activation of transcription from the LDL receptor promoter required domain C of Sp1; however, this domain is not crucial for activation of the simian virus 40 promoter, where synergistic activation occurs through multiple Sp1 binding sites and does not require SREBP [1].

High impact information on HLH106

  • Transport is blocked by cholesterol, which triggers SCAP, the SREBP escort protein, to bind to Insigs, which are ER retention proteins [2].
  • Importantly, sterol regulation of all promoters studied thus far is mediated by SREBP binding only to SREs [3].
  • This nuclear form, which may correspond to proteolytically activated HLH106, is abundant in the blood cell line mbn-2 [4].
  • In contrast to the rat homolog, HLH106 transcripts are not more abundant in adipose tissue than in other tissues [4].
  • HLH106, a Drosophila transcription factor with similarity to the vertebrate sterol responsive element binding protein [4].

Biological context of HLH106

  • HLH106 binds to both palindromic E-boxes and direct repeat sterol regulatory elements (SREs) efficiently, suggesting that it has a dual DNA binding specificity similar to the mammalian proteins [5].
  • These findings suggest that the ancestral SREBP pathway functions to maintain membrane integrity rather than to control cholesterol homeostasis [6].
  • SREBP-dependent transcriptional activation from all promoters examined thus far is dependent on the presence of an additional binding site for a ubiquitous coactivator [1].

Anatomical context of HLH106


Associations of HLH106 with chemical compounds


Other interactions of HLH106

  • Consistent with this model, a synthetic construct containing three tandem copies of the native LDL receptor SREBP site linked to a single Sp1 site was also significantly activated in a buttonhead-independent fashion [1].

Analytical, diagnostic and therapeutic context of HLH106

  • We describe experiments that evaluate the functional equivalence of mammalian SREBPs and the insect homologue of SREBP-1a, HLH106, in both mammalian and insect cell culture systems [5].


  1. Promoter selective transcriptional synergy mediated by sterol regulatory element binding protein and Sp1: a critical role for the Btd domain of Sp1. Athanikar, J.N., Sanchez, H.B., Osborne, T.F. Mol. Cell. Biol. (1997) [Pubmed]
  2. Direct binding of cholesterol to the purified membrane region of SCAP: mechanism for a sterol-sensing domain. Radhakrishnan, A., Sun, L.P., Kwon, H.J., Brown, M.S., Goldstein, J.L. Mol. Cell (2004) [Pubmed]
  3. Specificity in cholesterol regulation of gene expression by coevolution of sterol regulatory DNA element and its binding protein. Athanikar, J.N., Osborne, T.F. Proc. Natl. Acad. Sci. U.S.A. (1998) [Pubmed]
  4. HLH106, a Drosophila transcription factor with similarity to the vertebrate sterol responsive element binding protein. Theopold, U., Ekengren, S., Hultmark, D. Proc. Natl. Acad. Sci. U.S.A. (1996) [Pubmed]
  5. HLH106, a Drosophila sterol regulatory element-binding protein in a natural cholesterol auxotroph. Rosenfeld, J.M., Osborne, T.F. J. Biol. Chem. (1998) [Pubmed]
  6. The SREBP pathway in Drosophila: regulation by palmitate, not sterols. Seegmiller, A.C., Dobrosotskaya, I., Goldstein, J.L., Ho, Y.K., Brown, M.S., Rawson, R.B. Dev. Cell (2002) [Pubmed]
  7. Regulation of SREBP processing and membrane lipid production by phospholipids in Drosophila. Dobrosotskaya, I.Y., Seegmiller, A.C., Brown, M.S., Goldstein, J.L., Rawson, R.B. Science (2002) [Pubmed]
  8. Fatty acid auxotrophy in Drosophila larvae lacking SREBP. Kunte, A.S., Matthews, K.A., Rawson, R.B. Cell metabolism. (2006) [Pubmed]
  9. Reconstitution of sterol-regulated endoplasmic reticulum-to-Golgi transport of SREBP-2 in insect cells by co-expression of mammalian SCAP and Insigs. Dobrosotskaya, I.Y., Goldstein, J.L., Brown, M.S., Rawson, R.B. J. Biol. Chem. (2003) [Pubmed]
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