ArticleMolecular and cellular biology2000
Magnitude of the CREB-dependent transcriptional response is determined by the strength of the interaction between the kinase-inducible domain of CREB and the KIX domain of CREB-binding protein.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 80 citations in OpenAlex.
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- Characterization of the Crustacean Methyl Farnesoate Transcriptional Signaling Genes.International journal of molecular sciences · 2026Article
- Molecular and functional characterization of an evolutionarily conserved CREB-binding protein in the Lymnaea CNS.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
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- Phosphorylation regulates the binding of intrinsically disordered proteins via a flexible conformation selection mechanism.Communications chemistry · 2020Article
- HIV-1 Tat protein promotes neuronal dysregulation by inhibiting E2F transcription factor 3 (E2F3).The Journal of biological chemistry · 2019Article
- Finding gene regulatory network candidates using the gene expression knowledge base.BMC bioinformatics · 2014Article
- Combinatorial regulation of a signal-dependent activator by phosphorylation and acetylation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Bioinformatics study of cancer-related mutations within p53 phosphorylation site motifs.International journal of molecular sciences · 2014Article
- Cyclin-dependent kinase 1-dependent phosphorylation of cAMP response element-binding protein decreases chromatin occupancy.The Journal of biological chemistry · 2013Article
- Metalloprotein-based MRI probes.FEBS letters · 2013Review
- On the importance of polar interactions for complexes containing intrinsically disordered proteins.PLoS computational biology · 2013Article
- Multiple transcription factor families regulate axon growth and regeneration.Developmental neurobiology · 2011Review
- CREB and the CRTC co-activators: sensors for hormonal and metabolic signals.Nature reviews. Molecular cell biology · 2011Review
- Dual role of protein phosphorylation in DNA activator/coactivator binding.Biophysical journal · 2011Article
- Regulation of brain-derived neurotrophic factor exon IV transcription through calcium responsive elements in cortical neurons.PloS one · 2011Article
- Article
- Conserved and distinct modes of CREB/ATF transcription factor regulation by PP2A/B56gamma and genotoxic stress.PloS one · 2010Article
- A functional analysis of the CREB signaling pathway using HaloCHIP-chip and high throughput reporter assays.BMC genomics · 2009Article
- Multitasking C2H2 zinc fingers link Zac DNA binding to coordinated regulation of p300-histone acetyltransferase activity.Molecular and cellular biology · 2006Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The activity of the transcription factor CREB is regulated by extracellular stimuli that result in its phosphorylation at a critical serine residue, Ser133. Phosphorylation of Ser133 is believed to promote CREB-dependent transcription by allowing CREB to interact with the transcriptional coactivator CREB-binding protein (CBP). Previous studies have established that the domain encompassing Ser133 on CREB, known as the kinase-inducible domain (KID), interacts specifically with a short domain in CBP termed the KIX domain and that this interaction depends on the phosphorylation of Ser133. In this study, we adapted a recently described Escherichia coli-based two-hybrid system for the examination of phosphorylation-dependent protein-protein interactions, and we used this system to study the kinase-induced interaction between the KID and the KIX domain. We identified residues of the KID and the KIX domain that are critical for their interaction as well as two pairs of oppositely charged residues that apparently interact at the KID-KIX interface. We then isolated a mutant form of the KIX domain that interacts more tightly with wild-type and mutant forms of the KID than does the wild-type KIX domain. We show that in the context of full-length CBP, the corresponding amino acid substitution resulted in an enhanced ability of CBP to stimulate CREB-dependent transcription in mammalian cells. Conversely, an amino acid substitution in the KIX domain that weakens its interaction with the KID resulted in a decreased ability of full-length CBP to stimulate CREB-dependent transcription. These findings demonstrate that the magnitude of CREB-dependent transcription in mammalian cells depends on the strength of the KID-KIX interaction and suggest that the level of transcription induced by coactivator-dependent transcriptional activators can be specified by the strength of the activator-coactivator interaction.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.