Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications.

Alaji Bah, Julie D Forman-Kay

Journal: The Journal of biological chemistry 2016;291(13):6696-705

PMID: 26851279

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Abstract

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.

Address: From the Program in Molecular Structure & Function, The Hospital for Sick Children, Toronto, Ontario M5G 0A4 and the Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada [email protected].; From the Program in Molecular Structure & Function, The Hospital for Sick Children, Toronto, Ontario M5G 0A4 and the Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada [email protected].

DOI: 10.1074/jbc.R115.695056

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MeSH Terms: Amino Acids, Chromatin, Eukaryotic Initiation Factors, Factor IX, Histones, Humans, Hydrophobic and Hydrophilic Interactions, Intrinsically Disordered Proteins, Phosphorylation, Protein Binding, Protein Folding, Protein Interaction Domains and Motifs, Protein Processing, Post-Translational, Protein Structure, Secondary, Static Electricity, Thermodynamics