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Transcriptional Activity of GLI1 Is Negatively Regulated by Protein Kinase A
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Susanne Kaesler
Published/Copyright:
June 1, 2005
Abstract
The transcription factor GLI1 is one of three vertebrate members of the GLI family, which is characterized by a highly conserved DNAbinding domain of five zinc fingers. We have analyzed whether human GLI1 is a target of PKA regulation. It was found that PKA inhibits GLI1 transcriptional activity. However, no evidence for proteolytic processing or for alteration in the subcellular distribution of GLI1 was obtained. The responsive PKA site (aa333-336) was localized to the second zinc finger of GLI1. Mutation of Ser336 revealed that PKA could also stimulate GLI1 transcriptional activity. Thus, our data demonstrate both negative and positive regulation of human GLI1 by PKA.
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Published Online: 2005-06-01
Published in Print: 2000-07-04
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Characterization of Regulatory Elements in the 5'-Flanking Region of the GM2 Activator Gene
- Transcriptional Activity of GLI1 Is Negatively Regulated by Protein Kinase A
- Peptide Bond Synthesis: Function of the efp Gene Product
- Molecular Cloning, Expression and Purification of Muscle Fructose-1,6-Bisphosphatase from Zaocys dhumnades: the Role of the N-Terminal Sequence in AMP Activation at Alkaline pH
- The pH-Dependent Interaction of Cinnamomin with Lipid Membranes Investigated by Fluorescence Methods
- Nitric Oxide Detection and Visualization in Biological Systems. Applications of the FNOCT Method
- Processing of V-ATPase Subunit B of Mesembryanthemum crystallinum L. Is Mediated in Vitro by a Protease and/or Reactive Oxygen Species
- The Thioredoxin Boxes of Thyroglobulin: Possible Implications for Intermolecular Disulfide Bond Formation in the Follicle Lumen
- New Bivalent Thrombin Inhibitors with N? (Methyl)Arginine at the P1-Position
- Multiple Promoters Direct the Tissue-Specific Expression of Rat Mitochondrial Glycerol-3-Phosphate Dehydrogenase
- Characterization of SNP, a Novel Tissue- and Phase-Specific Nuclear Protein Expressed during the Proliferative Phase in the Oviduct of the Lizard Podarcis sicula Raf.
- Association of Betaine-Homocysteine S-Methyltransferase with Microtubules
- Re-Evaluation of Amino Acid Sequence and Structural Consensus Rules for Cysteine-Nitric Oxide Reactivity
- Expression of Human Tissue Kallikrein in Differentiated HL-60 Cells
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