ArticleBiophysical journal2017
Phosphorylation of the IDP KID Modulates Affinity for KIX by Increasing the Lifetime of the Complex.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 27 citations in OpenAlex.
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- Intrinsically Disordered Bacterial Polar Organizing Protein Z, PopZ, Interacts with Protein Binding Partners Through an N-terminal Molecular Recognition Feature.Journal of molecular biology · 2020Article
- Phosphorylation regulates the binding of intrinsically disordered proteins via a flexible conformation selection mechanism.Communications chemistry · 2020Article
- A disordered encounter complex is central to the yeast Abp1p SH3 domain binding pathway.PLoS computational biology · 2020Article
- Reviving Protein-ObservedBiophysical journal · 2020Article
- Measuring and Analyzing Binding Kinetics of Coupled Folding and Binding Reactions Under Pseudo-First-Order Conditions.Methods in molecular biology (Clifton, N.J.) · 2020Article
- IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions-Insights from transcription factors.Protein science : a publication of the Protein Society · 2020Article
- Specificity of MYB interactions relies on motifs in ordered and disordered contexts.Nucleic acids research · 2019Article
- Explicit Characterization of the Free Energy Landscape of pKID-KIX Coupled Folding and Binding.ACS central science · 2019Article
- Coupled Binding and Helix Formation Monitored by Synchrotron-Radiation Circular Dichroism.Biophysical journal · 2019Article
- pKID Binds to KIX via an Unstructured Transition State with Nonnative Interactions.Biophysical journal · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Intrinsically disordered proteins (IDPs) are known to undergo a range of posttranslational modifications, but by what mechanism do such modifications affect the binding of an IDP to its partner protein? We investigate this question using one such IDP, the kinase inducible domain (KID) of the transcription factor CREB, which interacts with the KIX domain of CREB-binding protein upon phosphorylation. As with many other IDPs, KID undergoes coupled folding and binding to form α-helical structure upon interacting with KIX. This single site phosphorylation plays an important role in the control of transcriptional activation in vivo. Here we show that, contrary to expectation, phosphorylation has no effect on association rates-unphosphorylated KID binds just as rapidly as pKID, the phosphorylated form-but rather, acts by increasing the lifetime of the complex. We propose that by controlling the lifetime of the bound complex of pKID:KIX via altering the dissociation rate, phosphorylation can facilitate effective control of transcription regulation.
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