Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications

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 globa...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 2016-03, Vol.291 (13), p.6696-6705
Main Authors: Bah, Alaji, Forman-Kay, Julie D.
Format: Article
Language:English
Subjects:
Amino Acids - chemistry
Amino Acids - metabolism
Chromatin
Eukaryotic Initiation Factors - chemistry
Eukaryotic Initiation Factors - genetics
Eukaryotic Initiation Factors - metabolism
Factor IX - chemistry
Factor IX - genetics
Factor IX - metabolism
Histones
Humans
Hydrophobic and Hydrophilic Interactions
intrinsically disordered protein
Intrinsically Disordered Proteins - chemistry
Intrinsically Disordered Proteins - genetics
Intrinsically Disordered Proteins - metabolism
Minireviews
Phosphorylation
post-translational modification (PTM)
Protein Binding
protein conformation
Protein Folding
Protein Interaction Domains and Motifs
Protein Processing, Post-Translational
Protein Structure, Secondary
protein-DNA interaction
protein-protein interaction
regulation
Static Electricity
Thermodynamics
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.R115.695056