ArticleThe Journal of biological chemistry2011
Structural dynamics and multiregion interactions in dynein-dynactin recognition.
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 24 papers.
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Who cites it
24 citing papers in PubMed.
- Exploration of the interaction between dynein intermediate chain and dynactin p150Protein science : a publication of the Protein Society · 2025Article
- Review
- Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.Nature communications · 2023Article
- Article
- Conserved Roles for the Dynein Intermediate Chain and Ndel1 in Assembly and Activation of Dynein.bioRxiv : the preprint server for biology · 2023Article
- Article
- Interplay of Disorder and Sequence Specificity in the Formation of Stable Dynein-Dynactin Complexes.Biophysical journal · 2020Article
- Conformational diversity of dynactin sidearm and domain organization of its subunit p150.Molecular biology of the cell · 2020Article
- Regulation of in vivo dynein force production by CDK5 and 14-3-3ε and KIAA0528.Nature communications · 2019Article
- A conserved interaction of the dynein light intermediate chain with dynein-dynactin effectors necessary for processivity.Nature communications · 2018Article
- Inositol hexakisphosphate kinase 1 (IP6K1) activity is required for cytoplasmic dynein-driven transport.The Biochemical journal · 2016Article
- Multiple Weak Linear Motifs Enhance Recruitment and Processivity in SPOP-Mediated Substrate Ubiquitination.Journal of molecular biology · 2016Article
- Differences in solution dynamics between lens β-crystallin homodimers and heterodimers probed by hydrogen-deuterium exchange and deamidation.Biochimica et biophysica acta · 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
- Polybivalency and disordered proteins in ordering macromolecular assemblies.Seminars in cell & developmental biology · 2015Review
- Autoregulatory mechanism for dynactin control of processive and diffusive dynein transport.Nature cell biology · 2014Article
- Article
- Nudel/NudE and Lis1 promote dynein and dynactin interaction in the context of spindle morphogenesis.Molecular biology of the cell · 2013Article
- Dynactin subunit p150(Glued) is a neuron-specific anti-catastrophe factor.PLoS biology · 2013Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytoplasmic dynein is a 1.2-MDa multisubunit motor protein complex that, together with its activator dynactin, is responsible for the majority of minus end microtubule-based motility. Dynactin targets dynein to specific cellular locations, links dynein to cargo, and increases dynein processivity. These two macromolecular complexes are connected by a direct interaction between dynactin's largest subunit, p150(Glued), and dynein intermediate chain (IC) subunit. Here, we demonstrate using NMR spectroscopy and isothermal titration calorimetry that the binding footprint of p150(Glued) on IC involves two noncontiguous recognition regions, and both are required for full binding affinity. In apo-IC, the helical structure of region 1, the nascent helix of region 2, and the disorder in the rest of the chain are determined from coupling constants, amide-amide sequential NOEs, secondary chemical shifts, and various dynamics measurements. When bound to p150(Glued), different patterns of spectral exchange broadening suggest that region 1 forms a coiled-coil and region 2 a packed stable helix, with the intervening residues remaining disordered. In the 150-kDa complex of p150(Glued), IC, and two light chains, the noninterface segments remain disordered. The multiregion IC binding interface, the partial disorder of region 2 and its potential for post-translational modification, and the modulation of the length of the longer linker by alternative splicing may provide a basis for elegant and multifaceted regulation of binding between IC and p150(Glued). The long disordered linker between the p150(Glued) binding segments and the dynein light chain consensus sequences could also provide an attractive recognition platform for diverse cargoes.
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