ArticleThe Journal of biological chemistry2011
DYNLL/LC8 protein controls signal transduction through the Nek9/Nek6 signaling module by regulating Nek6 binding to Nek9.
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 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- The interaction between LC8 and LCA5 reveals a novel oligomerization function of LC8 in the ciliary-centrosome system.Scientific reports · 2022Article
- Continuum dynamics and statistical correction of compositional heterogeneity in multivalent IDP oligomers resolved by single-particle EM.Journal of molecular biology · 2022Article
- In Mitosis You Are Not: The NIMA Family of Kinases inInternational journal of molecular sciences · 2022Review
- Structures and functions of the inflammasome engine.The Journal of allergy and clinical immunology · 2021Review
- EML4-ALK V3 oncogenic fusion proteins promote microtubule stabilization and accelerated migration through NEK9 and NEK7.Journal of cell science · 2020Article
- Physiological and Pathological Roles of Mammalian NEK7.Frontiers in physiology · 2020Review
- The Tousled-like kinases regulate genome and epigenome stability: implications in development and disease.Cellular and molecular life sciences : CMLS · 2019Review
- Oridonin is a covalent NLRP3 inhibitor with strong anti-inflammasome activity.Nature communications · 2018Article
- The established and the predicted roles of dynein light chain in the regulation of mitochondrial apoptosis.Cell cycle (Georgetown, Tex.) · 2018Article
- Genetic variants associated with mosaic Y chromosome loss highlight cell cycle genes and overlap with cancer susceptibility.Nature genetics · 2017Article
- Mitotic Regulation by NEK Kinase Networks.Frontiers in cell and developmental biology · 2017Review
- The Dual Nature of Nek9 in Adenovirus Replication.Journal of virology · 2016Article
- Mitotic kinase cascades orchestrating timely disjunction and movement of centrosomes maintain chromosomal stability and prevent cancer.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2016Review
- Mechanistic basis of Nek7 activation through Nek9 binding and induced dimerization.Nature communications · 2015Article
- Separate to operate: control of centrosome positioning and separation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2014Review
- "Stop Ne(c)king around": How interactomics contributes to functionally characterize Nek family kinases.World journal of biological chemistry · 2014Review
- NMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein.Computational and structural biotechnology journal · 2014Review
- Structural analysis of the regulation of the DYNLL/LC8 binding to Nek9 by phosphorylation.The Journal of biological chemistry · 2013Article
- On the molecular mechanisms of mitotic kinase activation.Open biology · 2012Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The NIMA family protein kinases Nek9/Nercc1 and the highly similar Nek6 and Nek7 form a signaling module activated in mitosis, when they are involved in the control of spindle organization and function. Here we report that Nek9, the module upstream kinase, binds to DYNLL/LC8, a highly conserved protein originally described as a component of the dynein complex. LC8 is a dimer that interacts with different proteins and has been suggested to act as a dimerization hub promoting the organization and oligomerization of partially disorganized partners. We find that the interaction of LC8 with Nek9 depends on a (K/R)XTQT motif adjacent to the Nek9 C-terminal coiled coil motif, results in Nek9 multimerization, and increases the rate of Nek9 autoactivation. LC8 binding to Nek9 is regulated by Nek9 activity through the autophosphorylation of Ser(944), a residue immediately N-terminal to the (K/R)XTQT motif. Remarkably, LC8 binding interferes with the interaction of Nek9 with its downstream partner Nek6 as well as with Nek6 activation, thus controlling both processes. Our work sheds light into the control of signal transduction through the module formed by Nek9 and Nek6/7 and uncovers a novel manner in which LC8 can regulate partner physiology by interfering with protein complex formation. We suggest that this and other LC8 functions can be specifically regulated by partner phosphorylation.
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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.