RTG3/YBL103C Literature Guide Help

Other names published for RTG3: YBL103C

RTG3 - Protein-protein Interactions (13)

ReferenceOther Genes Addressed
Ruiz-Roig C, et al.  (2012) The Hog1 SAPK controls the Rtg1/Rtg3 transcriptional complex activity by multiple regulatory mechanisms. Mol Biol Cell 23(21):4286-96
Khoury CM, et al.  (2008) A TSC22-like motif defines a novel antiapoptotic protein family. FEMS Yeast Res 8(4):540-63
Dilova I, et al.  (2004) Tor signaling and nutrient-based signals converge on Mks1p phosphorylation to regulate expression of Rtg1.Rtg3p-dependent target genes. J Biol Chem 279(45):46527-35
Dilova I, et al.  (2002) Mks1 in concert with TOR signaling negatively regulates RTG target gene expression in S. cerevisiae. Curr Biol 12(5):389-95
Georgakopoulos T, et al.  (2001) Functional analysis of the Saccharomyces cerevisiae YFR021w/YGR223c/YPL100w ORF family suggests relations to mitochondrial/peroxisomal functions and amino acid signalling pathways. Yeast 18(12):1155-71
van Hemert MJ, et al.  (2001) Yeast 14-3-3 proteins. Yeast 18(10):889-95
van Heusden GP and Steensma HY  (2001) 14-3-3 Proteins are essential for regulation of RTG3-dependent transcription in Saccharomyces cerevisiae. Yeast 18(16):1479-91
Massari ME and Murre C  (2000) Helix-loop-helix proteins: regulators of transcription in eucaryotic organisms. Mol Cell Biol 20(2):429-40
Robinson KA, et al.  (2000) A network of yeast basic helix-loop-helix interactions. Nucleic Acids Res 28(22):4460-6
Sekito T, et al.  (2000) Mitochondria-to-nuclear signaling is regulated by the subcellular localization of the transcription factors Rtg1p and Rtg3p. Mol Biol Cell 11(6):2103-15
Conlan RS, et al.  (1999) The Tup1-Cyc8 protein complex can shift from a transcriptional co-repressor to a transcriptional co-activator. J Biol Chem 274(1):205-10
Massari ME, et al.  (1999) A conserved motif present in a class of helix-loop-helix proteins activates transcription by direct recruitment of the SAGA complex. Mol Cell 4(1):63-73
Rothermel BA, et al.  (1997) Rtg3p, a basic helix-loop-helix/leucine zipper protein that functions in mitochondrial-induced changes in gene expression, contains independent activation domains. J Biol Chem 272(32):19801-7