ArticleThe Journal of biological chemistry2013
Structural analysis of the regulation of the DYNLL/LC8 binding to Nek9 by phosphorylation.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Residual flexibility in the topologically constrained multivalent complex between the GKAP scaffold and LC8 hub proteins.The FEBS journal · 2026Article
- NIMA-related kinase family at the nexus of skeletal development and congenital arthrogryposis: coordinated regulation of cell cycle and ciliary dynamics.Frontiers in genetics · 2026Review
- 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
- Article
- Crystal structure of human LC8 bound to a peptide from Ebola virus VP35.Journal of microbiology (Seoul, Korea) · 2021Article
- Molecular principles of Piwi-mediated cotranscriptional silencing through the dimeric SFiNX complex.Genes & development · 2021Article
- Modeling beta-sheet peptide-protein interactions: Rosetta FlexPepDock in CAPRI rounds 38-45.Proteins · 2020Article
- Physiological and Pathological Roles of Mammalian NEK7.Frontiers in physiology · 2020Review
- APC2 controls dendrite development by promoting microtubule dynamics.Nature communications · 2018Article
- Structural atlas of dynein motors at atomic resolution.Biophysical reviews · 2018Review
- The established and the predicted roles of dynein light chain in the regulation of mitochondrial apoptosis.Cell cycle (Georgetown, Tex.) · 2018Article
- Structural insights into a 20.8-kDa tegumental-allergen-like (TAL) protein from Clonorchis sinensis.Scientific reports · 2017Article
- Mitotic Regulation by NEK Kinase Networks.Frontiers in cell and developmental biology · 2017Review
- Fasciola hepatica calcium-binding protein FhCaBP2: structure of the dynein light chain-like domain.Parasitology research · 2016Article
- The Anchored Flexibility Model in LC8 Motif Recognition: Insights from the Chica Complex.Biochemistry · 2016Article
- Dynein Light Chain LC8 Is Required for RNA Polymerase I-Mediated Transcription in Trypanosoma brucei, Facilitating Assembly and Promoter Binding of Class I Transcription Factor A.Molecular and cellular biology · 2016Article
- Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization.Nature communications · 2015Article
- Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds.FEBS letters · 2015Review
- The mechanism of dynein light chain LC8-mediated oligomerization of the Ana2 centriole duplication factor.The Journal of biological chemistry · 2014Article
- Developments in optics and performance at BL13-XALOC, the macromolecular crystallography beamline at the ALBA synchrotron.Journal of synchrotron radiation · 2014Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The NIMA family protein kinases Nek9/Nercc1, Nek6, and Nek7 constitute a signaling module activated in early mitosis involved in the control of spindle organization. DYNLL/LC8 (dynein light chain 8) was originally described as a component of the dynein complex, but the recent discovery of multiple interaction partners for LC8 has suggested that it has a general role as a dimerization hub that organizes different protein partners. Recent experiments suggested that LC8 binding to Nek9 was regulated by Nek9 autophosphorylation on Ser(944), a residue immediately located N-terminal to the LC8 conserved (K/R)xTQT binding motif, and that this was crucial for the control of signal transduction through the Nek/Nek6/7 module. In the present work, we present two crystal structures of LC8 with a peptide corresponding to the Nek9 binding region with and without a phosphorylation on Ser(944). Structural analysis of LC8 with both Nek9 peptides, together with different biophysical experiments, explains the observed diminished binding affinity of Nek9 to LC8 upon phosphorylation on Ser(944) within the Nek9 sequence, thus shedding light into a novel phosphorylation regulatory mechanism that interferes with LC8 protein · protein complex formation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.