ArticleCell cycle (Georgetown, Tex.)2014
Regulation of Greatwall kinase by protein stabilization and nuclear localization.
Article in Cell cycle (Georgetown, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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
9 citing papers in PubMed, 16 citations in OpenAlex.
- γ-tubulin mediates DNA double-strand break repair.Journal of cell science · 2025Article
- Article
- The ATM-E6AP-MASTL axis mediates DNA damage checkpoint recovery.bioRxiv : the preprint server for biology · 2023Article
- Spatiotemporal coordination of Greatwall-Endos-PP2A promotes mitotic progression.The Journal of cell biology · 2021Article
- Greatwall-Endosulfine: A Molecular Switch that Regulates PP2A/B55 Protein Phosphatase Activity in Dividing and Quiescent Cells.International journal of molecular sciences · 2019Review
- PP1 initiates the dephosphorylation of MASTL, triggering mitotic exit and bistability in human cells.Journal of cell science · 2016Article
- MASTL(Greatwall) regulates DNA damage responses by coordinating mitotic entry after checkpoint recovery and APC/C activation.Scientific reports · 2016Article
- Spatial regulation of greatwall by Cdk1 and PP2A-Tws in the cell cycle.Cell cycle (Georgetown, Tex.) · 2016Article
- Regulating Greatwall for mitosis.Cell cycle (Georgetown, Tex.) · 2015Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Greatwall (Gwl) functions as an essential mitotic kinase by antagonizing protein phosphatase 2A. In this study we identified Hsp90, Cdc37 and members of the importin α and β families as the major binding partners of Gwl. Both Hsp90/Cdc37 chaperone and importin complexes associated with the N-terminal kinase domain of Gwl, whereas an intact glycine-rich loop at the N-terminus of Gwl was essential for binding of Hsp90/Cdc37 but not importins. We found that Hsp90 inhibition led to destabilization of Gwl, a mechanism that may partially contribute to the emerging role of Hsp90 in cell cycle progression and the anti-proliferative potential of Hsp90 inhibition. Moreover, in agreement with its importin association, Gwl exhibited nuclear localization in interphase Xenopus S3 cells, and dynamic nucleocytoplasmic distribution during mitosis. We identified KR456/457 as the locus of importin binding and the functional NLS of Gwl. Mutation of this site resulted in exclusion of Gwl from the nucleus. Finally, we showed that the Gwl nuclear localization is indispensable for the biochemical function of Gwl in promoting mitotic entry.
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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.