ArticleStructure (London, England : 1993)2018
KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive.
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 37 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
37 citing papers in PubMed, 53 citations in OpenAlex.
- Article
- A protein phosphatase 1 specificProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Meiosis-specific functions of kinetochore protein SPC105R required for chromosome segregation inMolecular biology of the cell · 2024Article
- Meiosis-specific functions of kinetochore protein SPC105R required for chromosome segregation inbioRxiv : the preprint server for biology · 2024Article
- Multimerization of a disordered kinetochore protein promotes accurate chromosome segregation by localizing a core dynein module.The Journal of cell biology · 2024Article
- Phosphatase specificity principles uncovered by MRBLE:Dephos and global substrate identification.Molecular systems biology · 2023Article
- Modeling specific aneuploidies: from karyotype manipulations to biological insights.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2023Review
- Substrate and phosphorylation site selection by phosphoprotein phosphatases.Trends in biochemical sciences · 2023Review
- Article
- Inhibitor-3 inhibits Protein Phosphatase 1 via a metal binding dynamic protein-protein interaction.Nature communications · 2023Article
- KNL1 is a prognostic and diagnostic biomarker related to immune infiltration in patients with uterine corpus endometrial carcinoma.Frontiers in oncology · 2023Article
- The ribosomal RNA processing 1B:protein phosphatase 1 holoenzyme reveals non-canonical PP1 interaction motifs.Cell reports · 2022Article
- Molecular architecture of the glycogen- committed PP1/PTG holoenzyme.Nature communications · 2022Article
- Highway to hell-thy meiotic divisions: Chromosome passenger complex functions driven by microtubules: CPC interactions with both the chromosomes and microtubules are important for spindle assembly and function: CPC interactions with both the chromosomes and microtubules are important for spindle assembly and function.BioEssays : news and reviews in molecular, cellular and developmental biology · 2022Article
- The microtubule- and PP1-binding activities ofMolecular biology of the cell · 2022Article
- The Role of Mitotic Kinases and the RZZ Complex in Kinetochore-Microtubule Attachments: Doing the Right Link.Frontiers in cell and developmental biology · 2022Review
- Kinetochore Architecture Employs Diverse Linker Strategies Across Evolution.Frontiers in cell and developmental biology · 2022Review
- On the Regulation of Mitosis by the Kinetochore, a Macromolecular Complex and Organising Hub of Eukaryotic Organisms.Sub-cellular biochemistry · 2022Article
- Counteraction between Astrin-PP1 and Cyclin-B-CDK1 pathways protects chromosome-microtubule attachments independent of biorientation.Nature communications · 2021Article
- Kinetochore life histories reveal an Aurora-B-dependent error correction mechanism in anaphase.Developmental cell · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
The kinetochore scaffold 1 (KNL1) protein coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules. Recently, microtubules and protein phosphatase 1 (PP1), which both bind the N-terminal domain of KNL1, have emerged as regulators of the SAC; however, how these proteins interact to contribute to SAC signaling is unknown. Here, we use X-ray crystallography, nuclear magnetic resonance spectroscopy, and biochemical assays to show how KNL1 binds both PP1 and microtubules. Unexpectedly, we discovered that PP1 and microtubules bind KNL1 via overlapping binding sites. Further, we showed that Aurora B kinase phosphorylation results in distinct patterns of KNL1 complex disruption. Finally, combining this data with co-sedimentation assays unequivocally demonstrated that microtubules and PP1 binding to KNL1 is mutually exclusive, with preferential formation of the KNL1:PP1 holoenzyme in the presence of PP1.
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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.