ArticleThe Journal of biological chemistry2010
Affinity, avidity, and kinetics of target sequence binding to LC8 dynein light chain isoforms.
Article in The Journal of biological chemistry, 2010. 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, 37 citations in OpenAlex.
- Residual flexibility in the topologically constrained multivalent complex between the GKAP scaffold and LC8 hub proteins.The FEBS journal · 2026Article
- To be, or not to be cleaved: Directed evolution of a canonical serine protease inhibitor against active and inactive protease pair identifies binding loop residue critical for prevention of proteolytic cleavage.Protein science : a publication of the Protein Society · 2025Article
- The interaction between LC8 and LCA5 reveals a novel oligomerization function of LC8 in the ciliary-centrosome system.Scientific reports · 2022Article
- Binding Revisited-Avidity in Cellular Function and Signaling.Frontiers in molecular biosciences · 2020Review
- The LC8-RavP ensemble Structure Evinces A Role for LC8 in Regulating Lyssavirus Polymerase Functionality.Journal of molecular biology · 2019Article
- Nanoparticles engineered to bind cellular motors for efficient delivery.Journal of nanobiotechnology · 2018Article
- The established and the predicted roles of dynein light chain in the regulation of mitochondrial apoptosis.Cell cycle (Georgetown, Tex.) · 2018Article
- Novel linear motif filtering protocol reveals the role of the LC8 dynein light chain in the Hippo pathway.PLoS computational biology · 2017Article
- Binding Site Geometry and Subdomain Valency Control Effects of Neutralizing Lectins on HIV-1 Viral Particles.ACS infectious diseases · 2016Article
- Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies.The Journal of biological chemistry · 2016Review
- The yeast dynein Dyn2-Pac11 complex is a dynein dimerization/processivity factor: structural and single-molecule characterization.Molecular biology of the cell · 2013Article
- Structural analysis of the regulation of the DYNLL/LC8 binding to Nek9 by phosphorylation.The Journal of biological chemistry · 2013Article
- Structural basis for kinesin-1:cargo recognition.Science (New York, N.Y.) · 2013Article
- Mechanisms controlling the temporal degradation of Nek2A and Kif18A by the APC/C-Cdc20 complex.The EMBO journal · 2013Article
- Structure of a yeast Dyn2-Nup159 complex and molecular basis for dynein light chain-nuclear pore interaction.The Journal of biological chemistry · 2012Article
- Myosin Va plays a key role in nitrergic neurotransmission by transporting nNOSα to enteric varicosity membrane.American journal of physiology. Gastrointestinal and liver physiology · 2011Article
- The association of viral proteins with host cell dynein components during virus infection.The FEBS journal · 2011Review
- Coupling viruses to dynein and kinesin-1.The EMBO journal · 2011Review
- Aplysqualenol A binds to the light chain of dynein type 1 (DYNLL1).Angewandte Chemie (International ed. in English) · 2011Article
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LC8 dynein light chain (DYNLL) is a highly conserved eukaryotic hub protein with dozens of binding partners and various functions beyond being a subunit of dynein and myosin Va motor proteins. Here, we compared the kinetic and thermodynamic parameters of binding of both mammalian isoforms, DYNLL1 and DYNLL2, to two putative consensus binding motifs (KXTQTX and XG(I/V)QVD) and report only subtle differences. Peptides containing either of the above motifs bind to DYNLL2 with micromolar affinity, whereas a myosin Va peptide (lacking the conserved Gln) and the noncanonical Pak1 peptide bind with K(d) values of 9 and 40 μM, respectively. Binding of the KXTQTX motif is enthalpy-driven, although that of all other peptides is both enthalpy- and entropy-driven. Moreover, the KXTQTX motif shows strikingly slower off-rate constant than the other motifs. As most DYNLL partners are homodimeric, we also assessed the binding of bivalent ligands to DYNLL2. Compared with monovalent ligands, a significant avidity effect was found as follows: K(d) values of 37 and 3.5 nM for a dimeric myosin Va fragment and a Leu zipper dimerized KXTQTX motif, respectively. Ligand binding kinetics of DYNLL can best be described by a conformational selection model consisting of a slow isomerization and a rapid binding step. We also studied the binding of the phosphomimetic S88E mutant of DYNLL2 to the dimeric myosin Va fragment, and we found a significantly lower apparent K(d) value (3 μM). We conclude that the thermodynamic and kinetic fine-tuning of binding of various ligands to DYNLL could have physiological relevance in its interaction network.
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