ArticlePLoS biology2015
The Structure of an NDR/LATS Kinase-Mob Complex Reveals a Novel Kinase-Coactivator System and Substrate Docking Mechanism.
Article in PLoS biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 51 citations in OpenAlex.
- NDR kinase SAX-1 controls dendrite branch-specific elimination during neuronal remodeling in C. elegans.The EMBO journal · 2026Article
- LATS kinase activity and tumor suppressor function are regulated by a second autophosphorylation site.The Journal of biological chemistry · 2026Article
- The OsMOB1A-OsSTK38 kinase complex phosphorylates CYCLIN C, controlling grain size and weight in rice.The Plant cell · 2024Article
- Microautophagy regulated by STK38 and GABARAPs is essential to repair lysosomes and prevent aging.EMBO reports · 2023Article
- TOR complex 1 negatively regulates NDR kinase Cbk1 to control cell separation in budding yeast.PLoS biology · 2023Article
- Proteome-wide screening for mitogen-activated protein kinase docking motifs and interactors.Science signaling · 2023Article
- Yeast Ssd1 is a non-enzymatic member of the RNase II family with an alternative RNA recognition site.Nucleic acids research · 2022Article
- Repeated Evolution of Inactive Pseudonucleases in a Fungal Branch of the Dis3/RNase II Family of Nucleases.Molecular biology and evolution · 2021Article
- Article
- Ndr/Lats Kinases Bind Specific Mob-Family Coactivators through a Conserved and Modular Interface.Biochemistry · 2020Article
- Mob Family Proteins: Regulatory Partners in Hippo and Hippo-Like Intracellular Signaling Pathways.Frontiers in cell and developmental biology · 2020Review
- Ssd1 and the cell wall integrity pathway promote entry, maintenance, and recovery from quiescence in budding yeast.Molecular biology of the cell · 2019Article
- Review
- Identification and characterization of differentially expressed miRNAs in HepG2 cells under normoxic and hypoxic conditions.RSC advances · 2019Article
- Disordered Protein Kinase Regions in Regulation of Kinase Domain Cores.Trends in biochemical sciences · 2019Review
- Comprehensive profiling of the STE20 kinase family defines features essential for selective substrate targeting and signaling output.PLoS biology · 2019Article
- Two Antagonistic Hippo Signaling Circuits Set the Division Plane at the Medial Position in the CiliateGenetics · 2019Article
- A cell separation checkpoint that enforces the proper order of late cytokinetic events.The Journal of cell biology · 2019Article
- Activation mechanisms of the Hippo kinase signaling cascade.Bioscience reports · 2018Review
- Structural Basis for Auto-Inhibition of the NDR1 Kinase Domain by an Atypically Long Activation Segment.Structure (London, England : 1993) · 2018Article
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Authors and funding
9 authors at 5 institutions in 3 countries.
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Abstract
Eukaryotic cells commonly use protein kinases in signaling systems that relay information and control a wide range of processes. These enzymes have a fundamentally similar structure, but achieve functional diversity through variable regions that determine how the catalytic core is activated and recruited to phosphorylation targets. "Hippo" pathways are ancient protein kinase signaling systems that control cell proliferation and morphogenesis; the NDR/LATS family protein kinases, which associate with "Mob" coactivator proteins, are central but incompletely understood components of these pathways. Here we describe the crystal structure of budding yeast Cbk1-Mob2, to our knowledge the first of an NDR/LATS kinase-Mob complex. It shows a novel coactivator-organized activation region that may be unique to NDR/LATS kinases, in which a key regulatory motif apparently shifts from an inactive binding mode to an active one upon phosphorylation. We also provide a structural basis for a substrate docking mechanism previously unknown in AGC family kinases, and show that docking interaction provides robustness to Cbk1's regulation of its two known in vivo substrates. Co-evolution of docking motifs and phosphorylation consensus sites strongly indicates that a protein is an in vivo regulatory target of this hippo pathway, and predicts a new group of high-confidence Cbk1 substrates that function at sites of cytokinesis and cell growth. Moreover, docking peptides arise in unstructured regions of proteins that are probably already kinase substrates, suggesting a broad sequential model for adaptive acquisition of kinase docking in rapidly evolving intrinsically disordered polypeptides.
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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.