Expanding the Paradigm: Intrinsically Disordered Proteins and Allosteric Regulation

• Published in: Journal of molecular biology Vol. 430; no. 16; pp. 2309 - 2320
• Main Authors: Berlow, Rebecca B., Dyson, H. Jane, Wright, Peter E.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 03.08.2018
• Subjects: Allosteric Regulation; allostery; Binding Sites; Gene Expression Regulation; Humans; Intrinsically Disordered Proteins - chemistry; Intrinsically Disordered Proteins - metabolism; Models, Molecular; post-translational modification; Protein Conformation; protein disorder; Protein Folding; protein–protein interaction; Thermodynamics; DBD; protein–protein interaction; post-translational modification; GR; TA; EAM; CBP; N-WASP; ID; IDPs; IDRs; allostery; protein disorder
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/j.jmb.2018.04.003

Allosteric regulatory processes are implicated at all levels of biological function. Recent advances in our understanding of the diverse and functionally significant class of intrinsically disordered proteins have identified a multitude of ways in which disordered proteins function within the confines of the allosteric paradigm. Allostery within or mediated by intrinsically disordered proteins ensures robust and efficient signal integration through mechanisms that would be extremely unfavorable or even impossible for globular protein interaction partners. Here, we highlight recent examples that indicate the breadth of biological outcomes that can be achieved through allosteric regulation by intrinsically disordered proteins. Ongoing and future work in this rapidly evolving area of research will expand our appreciation of the central role of intrinsically disordered proteins in ensuring the fidelity and efficiency of cellular regulation. [Display omitted] •Intrinsically disordered proteins are important for cellular signaling and regulation.•Recent studies highlight the many roles of intrinsically disordered proteins in allosteric processes.