ArticleEMBO reports2003
Trithorax interacts with type 1 serine/threonine protein phosphatase in Drosophila.
Article in EMBO reports, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 23 citations in OpenAlex.
- Trithorax regulates systemic signaling during Drosophila imaginal disc regeneration.Development (Cambridge, England) · 2015Article
- PNUTS/PP1 regulates RNAPII-mediated gene expression and is necessary for developmental growth.PLoS genetics · 2013Article
- Polycomb purification by in vivo biotinylation tagging reveals cohesin and Trithorax group proteins as interaction partners.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Article
- Ikaros stability and pericentromeric localization are regulated by protein phosphatase 1.The Journal of biological chemistry · 2009Article
- Drosophila Uri, a PP1alpha binding protein, is essential for viability, maintenance of DNA integrity and normal transcriptional activity.BMC molecular biology · 2008Article
- G1/S transcriptional networks modulated by the HOX11/TLX1 oncogene of T-cell acute lymphoblastic leukemia.Oncogene · 2005Article
- The essential role of PP1beta in Drosophila is to regulate nonmuscle myosin.Molecular biology of the cell · 2004Article
- SIPP1, a novel pre-mRNA splicing factor and interactor of protein phosphatase-1.The Biochemical journal · 2004Article
- Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The catalytic subunit of type 1 serine/threonine protein phosphatase (PP1c) was shown to bind trithorax (TRX) in the yeast two-hybrid system. Interaction between PP1c and TRX was confirmed in vivo by co-immunoprecipitation from Drosophila extracts. An amino-terminal fragment of TRX, containing a putative PP1c-binding motif, was shown to be sufficient for binding to PP1c by in vitro glutathione S-transferase pull-down assays using recombinant protein and fly extracts expressing epitope tagged PP1c. Disruption of the PP1c-binding motif abolished binding, indicating that this motif is necessary for interaction with PP1. On polytene chromosomes, PP1c is found at many discrete bands, which are widely distributed along the chromosomes. Many of the sites that stain strongly for PP1c correspond to sites of TRX, consistent with a physical association of PP1c with chromatin-bound TRX. Homeotic transformations of haltere to wing in flies mutant for trx are dominantly suppressed by PP1c mutants, indicating that PP1c not only binds TRX, but is a physiologically relevant regulator of TRX function in vivo.
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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.