ArticleeLife2019
Comprehensive substrate specificity profiling of the human Nek kinome reveals unexpected signaling outputs.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
34 citing papers in PubMed.
- A divergent Plasmodium NEK4 acts as a key regulator driving the early events of meiosis.Nature communications · 2026Article
- NEK7 phosphorylation of cortactin modulates the migratory capacity of cells expressing EML4-ALK V3.Scientific reports · 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
- NEK Family Kinases: Structure, Function, and Role in Disease.Biomolecules · 2025Review
- CETSA-MS unveils novel targets engaged by rigosertib to promote anti-tumor activity and inflammatory responses.iScience · 2025Article
- Structural Identification of Major Molecular Determinants for Phosphotyrosine Recognition in Tyrosine Kinases Reveals Tumour Promoting and Suppressive Functions.bioRxiv : the preprint server for biology · 2025Article
- NEK8, a NIMA-family protein kinase at the core of the ciliary INV complex.Cell communication and signaling : CCS · 2025Review
- Review
- The kinase NEK6 positively regulates LSD1 activity and accumulation in local chromatin sub-compartments.Communications biology · 2024Article
- Requirement of Nek2a and cyclin A2 for Wapl-dependent removal of cohesin from prophase chromatin.The EMBO journal · 2024Article
- NEKL-4 regulates microtubule stability and mitochondrial health in ciliated neurons.The Journal of cell biology · 2024Article
- β-catenin turnover is regulated by Nek10-mediated tyrosine phosphorylation in A549 lung adenocarcinoma cells.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Bifunctional Inhibitor Reveals NEK2 as a Therapeutic Target and Regulator of Oncogenic Pathways in Lymphoma.Molecular cancer therapeutics · 2024Article
- Involvement of NEK2 and NEK9 in LPS - induced endothelial barrier dysfunction.Microvascular research · 2024Article
- Loss of function of the ALS-associated NEK1 kinase disrupts microtubule homeostasis and nuclear import.Science advances · 2023Article
- Functional characterization of C21ORF2 association with the NEK1 kinase mutated in human in diseases.Life science alliance · 2023Article
- NEK1-Mediated Phosphorylation of YAP1 Is Key to Prostate Cancer Progression.Biomedicines · 2023Article
- Identification of biological pathways and processes regulated by NEK5 in breast epithelial cells via an integrated proteomic approach.Cell communication and signaling : CCS · 2022Article
- NEK7: a new target for the treatment of multiple tumors and chronic inflammatory diseases.Inflammopharmacology · 2022Review
Corrections and comments
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Authors and funding
11 authors.
Funding
Abstract
Human NimA-related kinases (Neks) have multiple mitotic and non-mitotic functions, but few substrates are known. We systematically determined the phosphorylation-site motifs for the entire Nek kinase family, except for Nek11. While all Nek kinases strongly select for hydrophobic residues in the -3 position, the family separates into four distinct groups based on specificity for a serine versus threonine phospho-acceptor, and preference for basic or acidic residues in other positions. Unlike Nek1-Nek9, Nek10 is a dual-specificity kinase that efficiently phosphorylates itself and peptide substrates on serine and tyrosine, and its activity is enhanced by tyrosine auto-phosphorylation. Nek10 dual-specificity depends on residues in the HRD+2 and APE-4 positions that are uncommon in either serine/threonine or tyrosine kinases. Finally, we show that the phosphorylation-site motifs for the mitotic kinases Nek6, Nek7 and Nek9 are essentially identical to that of their upstream activator Plk1, suggesting that Nek6/7/9 function as phospho-motif amplifiers of Plk1 signaling.
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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.