ArticleCell communication and signaling : CCS2020
Orchestration of signaling by structural disorder in class 1 cytokine receptors.
Article in Cell communication and signaling : CCS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- Accurate conformational ensembles of intrinsically disordered proteins using reweighting based on NMR chemical shifts.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Common gamma chain cytokines-driven optimization of chimeric antigen receptor T cells: Mechanistic insights and future directions.World journal of clinical oncology · 2026Review
- MPL receptor dimerization and the thrombopoietin pathway in primary immune thrombocytopenia: from molecular mechanisms to targeted therapies.Frontiers in medicine · 2026Review
- Beyond Static Tethering at Membrane Contact Sites: Structural Dynamics and Functional Implications of VAP Proteins.Molecules (Basel, Switzerland) · 2025Review
- Refining minimal engineered receptors for specific activation of on-target signaling molecules.Scientific reports · 2024Article
- Prolactin: structure, receptors, and functions.Reviews in endocrine & metabolic disorders · 2024Review
- Hydrodynamic Radii of Intrinsically Disordered Proteins: Fast Prediction by Minimum Dissipation Approximation and Experimental Validation.The journal of physical chemistry letters · 2024Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Diversity of hydrodynamic radii of intrinsically disordered proteins.European biophysics journal : EBJ · 2023Article
- Article
- Assessment of models for calculating the hydrodynamic radius of intrinsically disordered proteins.Biophysical journal · 2023Article
- A context-dependent and disordered ubiquitin-binding motif.Cellular and molecular life sciences : CMLS · 2022Article
- Structures of highly flexible intracellular domain of human α7 nicotinic acetylcholine receptor.Nature communications · 2022Article
- Improved predictions of phase behaviour of intrinsically disordered proteins by tuning the interaction range.Open research Europe · 2022Article
- Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs.Biomolecules · 2021Review
- On the roles of intrinsically disordered proteins and regions in cell communication and signaling.Cell communication and signaling : CCS · 2021Article
- The thrombopoietin receptor: revisiting the master regulator of platelet production.Platelets · 2021Review
- Insight into Calcium-Binding Motifs of Intrinsically Disordered Proteins.Biomolecules · 2021Article
- On the specificity of protein-protein interactions in the context of disorder.The Biochemical journal · 2021Review
- Order and disorder-An integrative structure of the full-length human growth hormone receptor.Science advances · 2021Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundClass 1 cytokine receptors (C1CRs) are single-pass transmembrane proteins responsible for transmitting signals between the outside and the inside of cells. Remarkably, they orchestrate key biological processes such as proliferation, differentiation, immunity and growth through long disordered intracellular domains (ICDs), but without having intrinsic kinase activity. Despite these key roles, their characteristics remain rudimentarily understood.
methodsThe current paper asks the question of why disorder has evolved to govern signaling of C1CRs by reviewing the literature in combination with new sequence and biophysical analyses of chain properties across the family.
resultsWe uncover that the C1CR-ICDs are fully disordered and brimming with SLiMs. Many of these short linear motifs (SLiMs) are overlapping, jointly signifying a complex regulation of interactions, including network rewiring by isoforms. The C1CR-ICDs have unique properties that distinguish them from most IDPs and we forward the perception that the C1CR-ICDs are far from simple strings with constitutively bound kinases. Rather, they carry both organizational and operational features left uncovered within their disorder, including mechanisms and complexities of regulatory functions.
conclusionsCritically, the understanding of the fascinating ability of these long, completely disordered chains to orchestrate complex cellular signaling pathways is still in its infancy, and we urge a perceptional shift away from the current simplistic view towards uncovering their full functionalities and potential. Video abstract.
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