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

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.

SUBMITTER: Bah A

PROVIDER: S-EPMC4807257 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature

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

Bah Alaji A Forman-Kay Julie D JD

The Journal of biological chemistry 20160205 13

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 diver ...[more]

PMID: 26851279

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