ArticleThe Journal of biological chemistry2012
Intrinsic disorder in dynein intermediate chain modulates its interactions with NudE and dynactin.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 54 citations in OpenAlex.
- Nde1 promotes Lis1 binding to full-length autoinhibited human dynein 1.Nature chemical biology · 2026Article
- Exploration of the interaction between dynein intermediate chain and dynactin p150Protein science : a publication of the Protein Society · 2025Article
- CCSer2 gates dynein activity at the cell periphery.The Journal of cell biology · 2025Article
- Nde1 Promotes Lis1 Binding to Full-Length Autoinhibited Human Dynein-1.bioRxiv : the preprint server for biology · 2025Article
- Molecular mechanism of dynein-dynactin complex assembly by LIS1.Science (New York, N.Y.) · 2024Article
- Review
- Nde1 promotes Lis1-mediated activation of dynein.Nature communications · 2023Article
- Conserved roles for the dynein intermediate chain and Ndel1 in assembly and activation of dynein.Nature communications · 2023Article
- Nde1 Promotes Lis1-Mediated Activation of Dynein.bioRxiv : the preprint server for biology · 2023Article
- Ndel1 disfavors dynein-dynactin-adaptor complex formation in two distinct ways.The Journal of biological chemistry · 2023Article
- Quantifying cooperative multisite binding in the hub protein LC8 through Bayesian inference.PLoS computational biology · 2023Article
- Ndel1 modulates dynein activation in two distinct ways.bioRxiv : the preprint server for biology · 2023Article
- Conserved Roles for the Dynein Intermediate Chain and Ndel1 in Assembly and Activation of Dynein.bioRxiv : the preprint server for biology · 2023Article
- Aurora A phosphorylates Ndel1 to reduce the levels of Mad1 and NuMA at spindle poles.Molecular biology of the cell · 2023Article
- Article
- Nde1 and Ndel1: Outstanding Mysteries in Dynein-Mediated Transport.Frontiers in cell and developmental biology · 2022Review
- Assessing Protein Interactions for Clustering of Mitochondrial Urea Cycle Enzymes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Phosphorylation and Pin1 binding to the LIC1 subunit selectively regulate mitotic dynein functions.The Journal of cell biology · 2021Article
- Article
- Cargo-Mediated Activation of Cytoplasmic DyneinFrontiers in cell and developmental biology · 2020Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The functional diversity of cytoplasmic dynein is in part attributed to multiple interactions between noncatalytic dynein subunits and an array of regulatory proteins. This study focuses on the interaction between the dynein intermediate chain subunit (IC) and a dynein regulator protein (NudE). We use isothermal titration calorimetry and NMR spectroscopy to map their interacting sections to their respective N-terminal domains, which are predicted to form dimeric coiled-coils. Interestingly, the specific residues within IC that interact with NudE are a subset of the bi-segmental binding region reported for p150(Glued), a subunit of the dynein activator protein dynactin. Although the IC binding domains of both NudE and p150(Glued) form dimeric coiled-coils and bind IC at a common site, we observe distinct binding modes for each regulatory protein: 1) NudE binds region 1 of the bi-segmental binding footprint of p150(Glued), whereas p150(Glued) requires regions 1 and 2 to match the binding affinity of NudE with region 1 alone. 2) Compared with unbound IC, NudE-bound IC shows a slight increase in flexibility in region 2, in contrast to the increase in ordered structure observed for p150(Glued)-bound IC (Morgan, J. L., Song, Y., and Barbar, E. (2011) J. Biol. Chem. 286, 39349-39359). 3) Although NudE has a higher affinity for the common binding segment on IC, when all three proteins are in solution, IC preferentially binds p150(Glued). These results underscore the importance of a bi-segmental binding region of IC and disorder in region 2 and flanking linkers in selecting which regulatory protein binds IC.
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