ArticleThe Journal of biological chemistry2013
Multiple recognition motifs in nucleoporin Nup159 provide a stable and rigid Nup159-Dyn2 assembly.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 45 citations in OpenAlex.
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- Cooperative multivalency converts disorder into rods, resolving a paradox in cellular architecture.bioRxiv : the preprint server for biology · 2026Article
- Residual flexibility in the topologically constrained multivalent complex between the GKAP scaffold and LC8 hub proteins.The FEBS journal · 2026Article
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- Dynamic interactions of dimeric hub proteins underlie their diverse functions and structures: A comparative analysis of 14-3-3 and LC8.The Journal of biological chemistry · 2025Review
- Successful prediction of LC8 binding to intrinsically disordered proteins sheds light on AlphaFold's black box.Frontiers in molecular biosciences · 2025Article
- Quantifying cooperative multisite binding in the hub protein LC8 through Bayesian inference.PLoS computational biology · 2023Article
- Linker Length Drives Heterogeneity of Multivalent Complexes of Hub Protein LC8 and Transcription Factor ASCIZ.Biomolecules · 2023Article
- Multivalent binding of the hub protein LC8 at a newly discovered site in 53BP1.Biophysical journal · 2022Article
- Continuum dynamics and statistical correction of compositional heterogeneity in multivalent IDP oligomers resolved by single-particle EM.Journal of molecular biology · 2022Article
- Assessing Protein Interactions for Clustering of Mitochondrial Urea Cycle Enzymes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Dimerisation of the PICTS complex via LC8/Cut-up drives co-transcriptional transposon silencing ineLife · 2021Article
- The dynein light chain 8 (LC8) binds predominantly "in-register" to a multivalent intrinsically disordered partner.The Journal of biological chemistry · 2020Article
- Systematic identification of recognition motifs for the hub protein LC8.Life science alliance · 2019Article
- Computational Prediction of MoRFs, Short Disorder-to-order Transitioning Protein Binding Regions.Computational and structural biotechnology journal · 2019Review
- The Structural Properties in Solution of the Intrinsically Mixed Folded Protein Ataxin-3.Biophysical journal · 2018Article
- Article
- IDPs in macromolecular complexes: the roles of multivalent interactions in diverse assemblies.Current opinion in structural biology · 2018Review
- Dynein light chain DLC-1 promotes localization and function of the PUF protein FBF-2 in germline progenitor cells.Development (Cambridge, England) · 2016Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Dyn2 is the yeast ortholog of the molecular hub LC8, which binds disordered proteins and promotes their self-association and higher order assembly. Dyn2 is proposed to dimerize and stabilize the Nup82-Nsp1-Nup159 complex of the nuclear pore assembly through its interaction with nucleoporin Nup159. Nup159 has six LC8 recognition motifs separated by short linkers. NMR experiments reported here show that the Dyn2 binding domain of Nup159 is intrinsically disordered and that binding of one equivalent of Dyn2 dimer aligns two Nup159 chains along the full Dyn2 binding domain to form a bivalent scaffold that promotes binding of other Dyn2 dimers. Isothermal titration calorimetry of Dyn2 binding to Nup constructs of increasing lengths determine that the third LC8 recognition motifs does not bind Dyn2. A new approach to identifying active LC8 recognition motifs based on NMR-detected β-sheet propensities is presented. Isothermal titration calorimetry experiments also show that, due to unfavorable entropy changes, a Nup-Dyn2 complex with three Dyn2 dimers is more stable than the wild-type complex with five Dyn2 dimers. The calorimetric results argue that, from a thermodynamics perspective, only three Dyn2 dimers are needed for optimal stability and suggest that the evolutionary adaptation of multiple tandem LC8 recognition motifs imparts to the complex other properties such as rigidity and a kink in the rod-like structure. These findings extend the repertoire of functions of intrinsically disordered protein to fine-tuning and versatile assembly of higher order macromolecular complexes.
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