Disease relevance of tgo

• Expression of DmagARNT in ARNT-lacking mouse Hepa-c4 cells resulted in the compensation for the loss of hypoxia response, suggesting the formation of a dimer with mouse HIF-1alpha and that the resulting heterodimer binds to the hypoxia-responsive elements (HRE), leading to transcription of the downstream luciferase gene [1].

High impact information on tgo

• In its control of dendritic diversity among da neurons, ss likely acts independently of its known cofactor tango and through a regulatory program distinct from those involving cut and abrupt [2].
• period and timeless tango: a dance of two clock genes [3].
• PAS is an acronym formed from the names of the Drosophila period clock protein (PER), vertebrate aryl hydrocarbon receptor nuclear translocator (ARNT), and Drosophila single-minded protein (SIM) [4].
• We show that both HIF-1 subunits are basic-helix-loop-helix proteins containing a PAS domain, defined by its presence in the Drosophila Per and Sim proteins and in the mammalian ARNT and AHR proteins [5].
• The Dysfusion protein functions as a heterodimer with the Tango bHLH-PAS protein in vivo to form a putative DNA-binding complex [6].

Biological context of tgo

• Lastly, expression of a C-terminal truncated tgo transgene specifically in the CNS midline and trachea resulted in reductions in the number of breathless-expressing cells [7].
• Analysis of the transcriptional activation domain of the Drosophila tango bHLH-PAS transcription factor [7].
• Drosophila tango is orthologous to mammalian Arnt and acts as a common dimerization partner for bHLH-PAS proteins during embryogenesis [7].
• A transient transfection assay using Drosophila S2 tissue culture cells and wild-type and mutant Drosophila tango cDNAs was used to localize the activation domain of the Tango protein [7].
• Expression of both single-minded and trachealess is highly restricted to their respective cell lineages, however tango is broadly expressed [8].

Anatomical context of tgo

• In contrast, nuclear localization of Tango is developmentally regulated; it is localized to the cytoplasm in most cells except the CNS midline, salivary duct, and tracheal cells where it accumulates in nuclei [8].
• Expression of D. magna ARNT was evident at the middle to late stages of embryonic development (about 25 h to 48 h after ovulation) in several tissues, including a pair of the 1st antenna, 2nd antenna, 2nd maxilla, five pairs of the thoracic limbs, the central nerve system, anus, dorsal organ, maxillary gland, and carapace [1].

Associations of tgo with chemical compounds

• Dioxin and other aryl hydrocarbons bind to the PAS domain of Ahr, causing Ahr to translocate to the nucleus, where it dimerizes with another bHLH-PAS protein, the aryl hydrocarbon receptor nuclear translocator (Arnt) [9].
• The ta5 enhancer was comprised of a basal enhancer required for driving Bar expression and a negative regulatory motif serving as a binding site for the heterodimer of Spineless and Tango, homologs of the mammalian dioxin receptor and aryl hydrocarbon nuclear translocator, respectively [10].

Other interactions of tgo

• The spineless-aristapedia and tango bHLH-PAS proteins interact to control antennal and tarsal development in Drosophila [9].
• Co-expression assays of trachealess and tgo in the developing eye imaginal disc showed a requirement for the C-terminal transactivation domain of TGO for a cellular response [7].
• Transcriptional activation of the fibroblast growth factor receptor (breathless) gene required an intact TGO C-terminus, in vitro [7].
• We show that the bHLH-PAS proteins Similar (Sima) and Tango (Tgo) function as HIF-alpha and HIF-beta homologues, respectively, and demonstrate a conserved mode of regulation for Sima by oxygen [11].
• Drosophila cyclin D/Cdk4 requires Hif-1 prolyl hydroxylase to drive cell growth [12].

Analytical, diagnostic and therapeutic context of tgo

• Immunoprecipitation experiments with recombinant proteins indicate that mSIM-2 associates with the arnt gene product [13].

References