ArticleThe Journal of biological chemistry2011
Light chain-dependent self-association of dynein intermediate chain.
Article in The Journal of biological chemistry, 2011. 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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Who cites it
30 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
- Exploration of the interaction between dynein intermediate chain and dynactin p150Protein science : a publication of the Protein Society · 2025Article
- 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
- Linker Length Drives Heterogeneity of Multivalent Complexes of Hub Protein LC8 and Transcription Factor ASCIZ.Biomolecules · 2023Article
- Article
- A Pseudorabies Virus Serine/Threonine Kinase, US3, Promotes Retrograde Transport in Axons via Akt/mToRC1.Journal of virology · 2022Article
- Cellular and Viral Determinants of HSV-1 Entry and Intracellular Transport towards Nucleus of Infected Cells.Journal of virology · 2021Article
- Protein Kinase-Mediated Decision Between the Life and Death.Advances in experimental medicine and biology · 2021Article
- Interplay of Disorder and Sequence Specificity in the Formation of Stable Dynein-Dynactin Complexes.Biophysical journal · 2020Article
- The Generation of Dynein Networks by Multi-Layered Regulation and Their Implication in Cell Division.Frontiers in cell and developmental biology · 2020Review
- The LC8-RavP ensemble Structure Evinces A Role for LC8 in Regulating Lyssavirus Polymerase Functionality.Journal of molecular biology · 2019Article
- Systematic identification of recognition motifs for the hub protein LC8.Life science alliance · 2019Article
- Article
- Dynein light chain regulates adaptive and innate B cell development by distinctive genetic mechanisms.PLoS genetics · 2017Article
- Molecular Basis for the Protein Recognition Specificity of the Dynein Light Chain DYNLT1/Tctex1: CHARACTERIZATION OF THE INTERACTION WITH ACTIVIN RECEPTOR IIB.The Journal of biological chemistry · 2016Article
- Interactions of Yeast Dynein with Dynein Light Chain and Dynactin: GENERAL IMPLICATIONS FOR INTRINSICALLY DISORDERED DUPLEX SCAFFOLDS IN MULTIPROTEIN ASSEMBLIES.The Journal of biological chemistry · 2015Article
- Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds.FEBS letters · 2015Review
- Distinct functional roles of cytoplasmic dynein defined by the intermediate chain isoforms.Experimental cell research · 2015Review
- Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold.The Journal of cell biology · 2015Article
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Authors and funding
2 authors.
Funding
Abstract
Dynein light chains are bivalent dimers that bind two copies of dynein intermediate chain IC to form a cargo attachment subcomplex. The interaction of light chain LC8 with the natively disordered N-terminal domain of IC induces helix formation at distant IC sites in or near a region predicted to form a coiled-coil. This fostered the hypothesis that LC8 binding promotes IC self-association to form a coiled-coil or other interchain helical structure. However, recent studies show that the predicted coiled-coil sequence partially overlaps the light chain LC7 recognition sequence on IC, raising questions about the apparently contradictory effects of LC8 and LC7. Here, we use NMR and fluorescence quenching to localize IC self-association to residues within the predicted coiled-coil that also correspond to helix 1 of the LC7 recognition sequence. LC8 binding promotes IC self-association of helix 1 from each of two IC chains, whereas LC7 binding reverses self-association by incorporating the same residues into two symmetrical, but distant, helices of the LC7-IC complex. Isothermal titration experiments confirm the distinction of LC8 enhancement of IC self-association and LC7 binding effects. When all three light chains are bound, IC self-association is shifted to another region. Such flexibility in association modes may function in maintaining a stable and versatile light chain-intermediate chain assembly under changing cellular conditions.
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