ArticleThe Journal of biological chemistry2010
The crystal structure of dynein intermediate chain-light chain roadblock complex gives new insights into dynein assembly.
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 24 papers.
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Who cites it
24 citing papers in PubMed.
- Review
- Article
- km23-1/DYNLRB1 regulation of MEK/ERK signaling and R-Ras in invasive human colorectal cancer cells.Cell biology international · 2020Article
- The Generation of Dynein Networks by Multi-Layered Regulation and Their Implication in Cell Division.Frontiers in cell and developmental biology · 2020Review
- Emerging mechanisms of dynein transport in the cytoplasm versus the cilium.Biochemical Society transactions · 2018Review
- Article
- 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
- Crystal structure of the Ego1-Ego2-Ego3 complex and its role in promoting Rag GTPase-dependent TORC1 signaling.Cell research · 2015Article
- Structural organization of the dynein-dynactin complex bound to microtubules.Nature structural & molecular biology · 2015Article
- NMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein.Computational and structural biotechnology journal · 2014Review
- The yeast dynein Dyn2-Pac11 complex is a dynein dimerization/processivity factor: structural and single-molecule characterization.Molecular biology of the cell · 2013Article
- Systematic dissection of dynein regulators in mitosis.The Journal of cell biology · 2013Article
- Requirement for protein kinase A in the phosphorylation of the TGFβ receptor-interacting protein km23-1 as a component of TGFβ downstream effects.Experimental cell research · 2013Article
- A dynein motor attachment complex regulates TGFß/Smad3 signaling.International journal of biological sciences · 2013Article
- Decreased tumor progression and invasion by a novel anti-cell motility target for human colorectal carcinoma cells.PloS one · 2013Article
- Native disorder mediates binding of dynein to NudE and dynactin.Biochemical Society transactions · 2012Review
- Intrinsic disorder in dynein intermediate chain modulates its interactions with NudE and dynactin.The Journal of biological chemistry · 2012Article
- Requirement of a dynein light chain in transforming growth factor β signaling in zebrafish ovarian follicle cells.Molecular and cellular endocrinology · 2012Article
- Structural dynamics and multiregion interactions in dynein-dynactin recognition.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The roadblock/LC7 dynein light chain is a ubiquitous component of all dyneins and is essential for many diverse processes including proper axonal transport and dendrite growth. In addition, LC7 functions in non-dynein transcriptional activation of the transforming growth factor-beta complex. Crystal structures of Drosophila melanogaster LC7 in the apo form and in complex with a segment of the disordered N-terminal domain of dynein intermediate chain (IC) provide the first definitive identification of the IC sequence recognized by LC7. The site, confirmed by isothermal titration calorimetry studies, overlaps the IC sequence considered in the literature to be an IC self-association domain. The IC peptide binds as two amphipathic helices that lie along an extensive hydrophobic cleft on LC7 and ends with a polar side-chain interaction network that includes conserved residues from both proteins. The LC7 recognition sequence on IC and its interface with LC7 are well conserved and are, thus, likely representative of all IC x LC7 structures. Interestingly, the position of bound IC in the IC x LC7 complex mimics a helix that is integrated into the primary structure in distantly related LC7 homologs. The IC x LC7 structure further shows that the naturally occurring robl(Z) deletion mutation contains the majority of the IC binding site and suggests that promotion of IC binding by phosphorylation of LC7 is an indirect effect.
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