Towards a Comprehensive Analysis of the Protein Phosphatase 1 Interactome in Drosophila

Bennett, Daimark; Lyulcheva, Ekaterina; Alphey, Luke

doi:10.1016/j.jmb.2006.08.094

Cited by 31 publications

(25 citation statements)

References 71 publications

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“…Neurabin I and Neurabin II/Spinophilin were identified to bind PP1g1 and PP1a, but not PP1d (MacMillan et al 1999;TerryLorenzo et al 2002), and several PP1a-and PP1g1-specific regulators have been identified in mouse fetal lung epithelial cells (Flores-Delgado et al 2005). In Drosophila, even though the majority of PP1c regulatory subunits seem to bind all four PP1c isozymes in the yeast two-hybrid system (Bennett et al 2006), we identified three interactors that bind PP1a specifically or with greatly increased affinity compared to PP1b (L. Alphey, unpublished results). One of them, CG11416 Expressing HA-PP1b in a PP1a87B, PP1a96A mutant background (from cross w ; arm-Gal4 ; PP1a87B (uri), is essential for viability (J. Kirchner and L. Alphey, unpublished results) and could mediate an essential requirement for PP1a.…”

Section: Table 5 Summary Of Overexpression Experimentsmentioning

confidence: 92%

“…Such targeting and regulatory proteins are therefore key to investigating the role of PP1 in specific subcellular processes [e.g., glycogen metabolism through PTG (Printen et al 1997) or Dpp receptor type 1 deactivation through Sara (Bennett and Alphey 2002)]. In a yeast two-hybrid assay for PP1c-binding proteins in Drosophila, we found that the large majority of PP1c-binding proteins bind all four PP1c isozymes (Bennett et al 2006). Very few proteins have been identified that specifically bind some PP1c isozymes but not others.…”

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confidence: 94%

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Essential, Overlapping and Redundant Roles of the Drosophila Protein Phosphatase 1α and 1β Genes

et al. 2007

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Protein serine/threonine phosphatase type 1 (PP1) has been found in all eukaryotes examined to date and is involved in the regulation of many cellular functions, including glycogen metabolism, muscle contraction, and mitosis. In Drosophila, four genes code for the catalytic subunit of PP1 (PP1c), three of which belong to the PP1a subtype. PP1b9C (flapwing) encodes the fourth PP1c gene and has a specific and nonredundant function as a nonmuscle myosin phosphatase. PP1a87B is the major form and contributes $80% of the total PP1 activity. We describe the first mutant alleles of PP1a96A and show that PP1a96A is not an essential gene, but seems to have a function in the regulation of nonmuscle myosin. We show that overexpression of the PP1a isozymes does not rescue semilethal PP1b9C mutants, whereas overexpression of either PP1a96A or PP1b9C does rescue a lethal PP1a87B mutant combination, showing that the lethality is due to a quantitative reduction in the level of PP1c. Overexpression of PP1b9C does not rescue a PP1a87B, PP1a96A double mutant, suggesting an essential PP1a-specific function in Drosophila.

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Section: Table 5 Summary Of Overexpression Experimentsmentioning

confidence: 92%

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confidence: 94%

Essential, Overlapping and Redundant Roles of the Drosophila Protein Phosphatase 1α and 1β Genes

et al. 2007

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“…The majority of the putative PP1 interactions proposed derived primarily from biochemical approaches, highthroughput Yeast Two-Hybrid (YTH) screens, mass spectrometry and in silico screenings (Bennett et al, 2006;Fardilha et al, 2011b;Flores-Delgado et al, 2007;Hendrickx et al, 2009;Hrabchak and Varmuza, 2004;Moorhead et al, 2008;TrinkleMulcahy et al, 2006). The YTH system provides a sensitive method for detecting relatively weak and transient protein interactions (Fields and Song, 1989).…”

Section: Introductionmentioning

confidence: 99%

Protein Phosphatase 1α Interacting Proteins in the Human Brain

Esteves

Domingues

Fardilha

et al. 2012

OMICS: A Journal of Integrative Biology

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Protein Phosphatase 1 (PP1) is a major serine/threonine-phosphatase whose activity is dependent on its binding to regulatory subunits known as PP1 interacting proteins (PIPs), responsible for targeting PP1 to a specific cellular location, specifying its substrate or regulating its action. Today, more than 200 PIPs have been described involving PP1 in panoply of cellular mechanisms. Moreover, several PIPs have been identified that are tissue and event specific. In addition, the diversity of PP1/PIP complexes can further be achieved by the existence of several PP1 isoforms that can bind preferentially to a certain PIP. Thus, PP1/PIP complexes are highly specific for a particular function in the cell, and as such, they are excellent pharmacological targets. Hence, an in-depth survey was taken to identify specific PP1a PIPs in human brain by a high-throughput Yeast Two-Hybrid approach. Sixty-six proteins were recognized to bind PP1a, 39 being novel PIPs. A large protein interaction databases search was also performed to integrate with the results of the PP1a Human Brain Yeast Two-Hybrid and a total of 246 interactions were retrieved.

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“…The PNUTS C-terminal region contains a zinc finger domain implying a possible interaction with nucleic acids [14], although this domain in PNUTS is not known to bind either RNA or DNA. The polypeptide region between the TFIIS LW and zinc finger domains in PNUTS is highly unstructured and plays a conserved role in binding to PP1 [15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Biophysical Analysis of the N-Terminal Domain from the Human Protein Phosphatase 1 Nuclear Targeting Subunit PNUTS Suggests an Extended Transcription Factor TFIIS-Like Fold

et al. 2016

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Towards a Comprehensive Analysis of the Protein Phosphatase 1 Interactome in Drosophila

Cited by 31 publications

References 71 publications

Essential, Overlapping and Redundant Roles of the Drosophila Protein Phosphatase 1α and 1β Genes

Essential, Overlapping and Redundant Roles of the Drosophila Protein Phosphatase 1α and 1β Genes

Protein Phosphatase 1α Interacting Proteins in the Human Brain

Biophysical Analysis of the N-Terminal Domain from the Human Protein Phosphatase 1 Nuclear Targeting Subunit PNUTS Suggests an Extended Transcription Factor TFIIS-Like Fold

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