ArticleThe Journal of biological chemistry2009
Multivalency in the assembly of intrinsically disordered Dynein intermediate chain.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Walking the tightrope: Balancing opposing cooperativities in dynein assembly.The Journal of biological chemistry · 2026Article
- Walking the Tightrope: Balancing Opposing Cooperativities as an Operating Principle in Dynein Assembly.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
- 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
- Molecular mechanism of dynein-dynactin complex assembly by LIS1.Science (New York, N.Y.) · 2024Article
- Review
- 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
- Article
- Continuum dynamics and statistical correction of compositional heterogeneity in multivalent IDP oligomers resolved by single-particle EM.Journal of molecular biology · 2022Article
- The dynein light chain protein Tda2 functions as a dimerization engine to regulate actin capping protein during endocytosis.Molecular biology of the cell · 2021Article
- 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
- The Generation of Dynein Networks by Multi-Layered Regulation and Their Implication in Cell Division.Frontiers in cell and developmental biology · 2020Review
- Article
- Structural atlas of dynein motors at atomic resolution.Biophysical reviews · 2018Review
- Novel linear motif filtering protocol reveals the role of the LC8 dynein light chain in the Hippo pathway.PLoS computational biology · 2017Article
- Novel function of a dynein light chain in actin assembly during clathrin-mediated endocytosis.The Journal of cell biology · 2017Article
- Genetic diversity and selection of three nuclear genes in Schistosoma japonicum populations.Parasites & vectors · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Dynein light chains are thought to increase binding efficiency of dynein intermediate chain to both dynein heavy chain and dynactin, but their exact role is not clear. Isothermal titration calorimetry and x-ray crystallography reported herein indicate that multivalency effects underlie efficient dynein assembly and regulation. For a ternary complex of a 60-amino acid segment of dynein intermediate chain (IC) bound to two homodimeric dynein light chains Tctex1 and LC8, there is a 50-fold affinity enhancement for the second light chain binding. For a designed IC construct containing two LC8 sites, observed the 1000-fold enhancement reflects a remarkably pure entropic chelate effect of a magnitude commensurate with theoretical predictions. The lower enhancement in wild-type IC is attributed to unfavorable free energy changes associated with incremental interactions of IC with Tctex1. Our results show assembled dynein IC as an elongated, flexible polybivalent duplex, and suggest that polybivalency is an important general mechanism for constructing stable yet reversible and functionally versatile complexes.
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