Cited by 156Protein Structure and DynamicsProtein Interaction Studies and Fluorescence Analysis14-3-3 protein interactions

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Interactions by Disorder – A Matter of Context

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Bugge, Katrine, Brakti, Inna, Fernandes, Catarina B., Dreier, Jesper E., Lundsgaard, Jeppe E., Olsen, Johan G., Skriver, Karen, Kragelund, Birthe B.·2020·Frontiers in Molecular Biosciences

DOI 10.3389/fmolb.2020.00110PMC PMC7308724

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Abstract

Living organisms depend on timely and organized interactions between proteins linked in interactomes of high complexity. The recent increased precision by which protein interactions can be studied, and the enclosure of intrinsic structural disorder, suggest that it is time to zoom out and embrace protein interactions beyond the most central points of physical encounter. The present paper discusses protein-protein interactions in the view of structural disorder with an emphasis on flanking regions and contexts of disorder-based interactions. Context constitutes an overarching concept being of physicochemical, biomolecular, and physiological nature, but it also includes the immediate molecular context of the interaction. For intrinsically disordered proteins, which often function by exploiting short linear motifs, context contributes in highly regulatory and decisive manners and constitute a yet largely unrecognized source of interaction potential in a multitude of biological processes. Through selected examples, this review emphasizes how multivalency, charges and charge clusters, hydrophobic patches, dynamics, energetic frustration, and ensemble redistribution of flanking regions or disordered contexts are emerging as important contributors to allosteric regulation, positive and negative cooperativity, feedback regulation and negative selection in binding. The review emphasizes that understanding context, and in particular the role the molecular disordered context and flanking regions take on in protein interactions, constitute an untapped well of energetic modulation potential, also of relevance to drug discovery and development.

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Authors: Bugge, K., Brakti, I., Fernandes, C. B., Dreier, J. E., Lundsgaard, J. E., Olsen, J. G., Skriver, K., & Kragelund, B. B.
Affiliations: University of Copenhagen (DK)
Corresponding author: Skriver, Karen
Kragelund, Birthe B.
ORCID: Bugge, Katrine
Brakti, Inna
Fernandes, Catarina B.
Dreier, Jesper E.
Olsen, Johan G.
Skriver, Karen
Kragelund, Birthe B.
Venue: Frontiers in Molecular Biosciences
Publisher: Frontiers Media SA
Published: 2020-06-16
Volume: 7
Pages: 110-110
ISSN: 2296-889X (ISSN-L)
DOI: 10.3389/fmolb.2020.00110
PMC: PMC7308724
OpenAlex: W3036355682
Cited by: 155
References: 159
Citations by year: 2026: 16 · 2025: 21 · 2024: 20 · 2023: 31 · 2022: 34 · 2021: 24 · 2020: 9
FWCI: 2.35
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Frontiers in Molecular Biosciences (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: Novo Nordisk Fonden
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 14-3-3 protein interactions
Keywords: protein-protein interaction, intrinsically disordered proteins, structural disorder, flanking regions, context-dependent interactions, short linear motifs, multivalency, charge clusters, hydrophobic patch, allosteric regulation, feedback regulation, protein-protein interaction network, drug discovery

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Interactions by Disorder – A Matter of Context

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