ArticleStructure (London, England : 1993)2018
Structural Basis for Auto-Inhibition of the NDR1 Kinase Domain by an Atypically Long Activation Segment.
Article in Structure (London, England : 1993), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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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
15 citing papers in PubMed, 22 citations in OpenAlex.
- Homer condensates orchestrate YAP-Wnt signaling crosstalk downstream of the Crumbs polarity complex.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Species-specific regulation of necroptosis by STK38-dependent RIPK1 phosphorylation.Cell death and differentiation · 2026Article
- LATS kinase activity and tumor suppressor function are regulated by a second autophosphorylation site.The Journal of biological chemistry · 2026Article
- Interplay of RAP2 GTPase and the cytoskeleton in Hippo pathway regulation.The Journal of biological chemistry · 2024Article
- NDR kinase tricornered genetically interacts with Ccm3 and metabolic enzymes in Drosophila melanogaster tracheal development.G3 (Bethesda, Md.) · 2023Article
- Kinetic Regulation of the Mammalian Sterile 20-like Kinase 2 (MST2).Biochemistry · 2022Article
- Furry is required for cell movements during gastrulation and functionally interacts with NDR1.Scientific reports · 2021Article
- The STK38-XPO1 axis, a new actor in physiology and cancer.Cellular and molecular life sciences : CMLS · 2021Review
- A census of pathway maps in cancer systems biology.Nature reviews. Cancer · 2020Review
- Furry protein suppresses nuclear localization of yes-associated protein (YAP) by activating NDR kinase and binding to YAP.The Journal of biological chemistry · 2020Article
- Mob Family Proteins: Regulatory Partners in Hippo and Hippo-Like Intracellular Signaling Pathways.Frontiers in cell and developmental biology · 2020Review
- A Structurally-Validated Multiple Sequence Alignment of 497 Human Protein Kinase Domains.Scientific reports · 2019Article
- Review
- Insights into evolutionary interaction patterns of the 'Phosphorylation Activation Segment' in kinase.Bioinformation · 2019Article
- Lighting the way: Recent insights into the structure and regulation of phototropin blue light receptors.The Journal of biological chemistryReview
Corrections and comments
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Authors and funding
12 authors at 5 institutions in 3 countries.
Funding
Abstract
The human NDR family kinases control diverse aspects of cell growth, and are regulated through phosphorylation and association with scaffolds such as MOB1. Here, we report the crystal structure of the human NDR1 kinase domain in its non-phosphorylated state, revealing a fully resolved atypically long activation segment that blocks substrate binding and stabilizes a non-productive position of helix αC. Consistent with an auto-inhibitory function, mutations within the activation segment of NDR1 dramatically enhance in vitro kinase activity. Interestingly, NDR1 catalytic activity is further potentiated by MOB1 binding, suggesting that regulation through modulation of the activation segment and by MOB1 binding are mechanistically distinct. Lastly, deleting the auto-inhibitory activation segment of NDR1 causes a marked increase in the association with upstream Hippo pathway components and the Furry scaffold. These findings provide a point of departure for future efforts to explore the cellular functions and the mechanism of NDR1.
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Registered trials
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.