ArticleThe Biochemical journal2002
Functional interaction between nuclear inhibitor of protein phosphatase type 1 (NIPP1) and protein phosphatase type 1 (PP1) in Drosophila: consequences of over-expression of NIPP1 in flies and suppression by co-expression of PP1.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- Sut-6/NIPP1 modulates tau toxicity.Human molecular genetics · 2023Article
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- Hormonal control of motivational circuitry orchestrates the transition to sexuality inScience advances · 2021Article
- Protein phosphatase 1 activity controls a balance between collective and single cell modes of migration.eLife · 2020Article
- Local Juvenile Hormone activity regulates gut homeostasis and tumor growth in adult Drosophila.Scientific reports · 2017Article
- Article
- Mating-Induced Increase in Germline Stem Cells via the Neuroendocrine System in Female Drosophila.PLoS genetics · 2016Article
- Article
- Juvenile hormone regulation of Drosophila aging.BMC biology · 2013Article
- Development of a population suppression strain of the human malaria vector mosquito, Anopheles stephensi.Malaria journal · 2013Article
- Sequential phosphorylation of smoothened transduces graded hedgehog signaling.Science signaling · 2011Article
- Female-specific flightless phenotype for mosquito control.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Post-translational regulation of the Drosophila circadian clock requires protein phosphatase 1 (PP1).Genes & development · 2007Article
- The essential role of PP1beta in Drosophila is to regulate nonmuscle myosin.Molecular biology of the cell · 2004Article
- The nuclear scaffold protein NIPP1 is essential for early embryonic development and cell proliferation.Molecular and cellular biology · 2004Article
- Ectopic expression of inhibitors of protein phosphatase type 1 (PP1) can be used to analyze roles of PP1 in Drosophila development.Genetics · 2003Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The catalytic subunit of type 1 Ser/Thr protein phosphatases (PP1c) forms complexes with many proteins that target it to particular subcellular locations and regulate its activity towards specific substrates. We report the identification of a Drosophila orthologue of nuclear inhibitor of PP1 (NIPP1Dm) through interaction with PP1c in the yeast two-hybrid system. NIPP1Dm shares many properties with mammalian NIPP1 including inhibition of PP1c in vitro, binding to RNA and PP1c, and localization to nuclear speckles. However, the mechanism controlling interaction of PP1c with NIPP1 is not conserved in Drosophila. NIPP1 can function independently of PP1c as a splicing factor, but the relative importance of this function is unknown. Over-expression of NIPP1Dm in Drosophila is cell-lethal in a range of tissues and developmental stages. The effects of ectopic NIPP1Dm are suppressed by co-expression of PP1c, indicating that the only effect of ectopic NIPP1Dm is to affect PP1c function. Co-expression of NIPP1Dm and PP1c does not have any detectable physiological effect in vivo, suggesting that the NIPP1Dm-PP1c holoenzyme is not normally limiting in Drosophila. These data show that NIPP1Dm and PP1c interact in vivo and suggest that NIPP1's role as a phosphatase regulator is conserved in Drosophila.
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