Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 13, Pages 6696-6705Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R115.695056
Keywords
intrinsically disordered protein; post-translational modification (PTM); protein conformation; protein-DNA interaction; protein-protein interaction; regulation
Categories
Funding
- Canadian Institutes of Health Research (CIHR)
- Canadian Cancer Society
- Cystic Fibrosis Canada
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Post-translational modifications (PTMs) produce significant changes in the structural properties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes. PTMs can induce a range of effects, from local stabilization or destabilization of transient secondary structure to global disorder-to-order transitions, potentially driving complete state changes between intrinsically disordered and folded states or dispersed monomeric and phase-separated states. Here, we discuss diverse biological processes that are dependent on PTM regulation of IDPs. We also present recent tools for generating homogenously modified IDPs for studies of PTM-mediated IDP regulatory mechanisms.
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