ArticleThe Journal of biological chemistry2000
WD40 repeat proteins striatin and S/G(2) nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A.
Article in The Journal of biological chemistry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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Who cites it
79 citing papers in PubMed, 188 citations in OpenAlex.
- A cross-vertebrate brain protein interaction map identifies conserved neural and non-neural complexes.Cell reports · 2026Article
- The Calmodulin/Striatin Interaction Is Enhanced in Diabetic Hearts and Defines Novel Signaling Clusters Implicated in Cardiac Remodeling.ACS omega · 2026Article
- PPP2R2C confers radioresistance in nasopharyngeal carcinoma by suppressing ferroptosis via RPS27L stabilization.Cell death & disease · 2026Article
- In Vitro and In Silico Studies on Unique Key Components of Hypericum Species, Focusing on Their Role in Inhibiting Enzymatic Pathways.Chemistry & biodiversity · 2026Article
- Targeting PP2A in cancer: an underrated option.Journal of experimental & clinical cancer research : CR · 2025Review
- VerteBrain reveals novel neural and non-neural protein assemblies conserved across vertebrate evolution.bioRxiv : the preprint server for biology · 2025Article
- Germline mutations in PPP2R1B in patients with a personal and family history of cancer.JCI insight · 2025Article
- Remodeling of the cardiac striatin interactome and its dynamics in the diabetic heart.Scientific reports · 2025Article
- STRIPAK, a fundamental signaling hub of eukaryotic development.Microbiology and molecular biology reviews : MMBR · 2024Review
- Clinical Potential of Misshapen/NIKs-Related Kinase (MINK) 1-A Many-Sided Element of Cell Physiology and Pathology.Current issues in molecular biology · 2024Review
- The profile of expression of the scaffold protein SG2NA(s) differs between cancer types and its interactome in normal vis-a-vis breast tumor tissues suggests its wide roles in regulating multiple cellular pathways.Molecular and cellular biochemistry · 2022Article
- Self-Sustained Regulation or Self-Perpetuating Dysregulation: ROS-dependent HIF-YAP-Notch Signaling as a Double-Edged Sword on Stem Cell Physiology and Tumorigenesis.Frontiers in cell and developmental biology · 2022Review
- Protein phosphatase 2A - structure, function and role in neurodevelopmental disorders.Journal of cell science · 2021Review
- Cryo-EM structure of the Hippo signaling integrator human STRIPAK.Nature structural & molecular biology · 2021Article
- STRIPAK-PP2A regulates Hippo-Yorkie signaling to suppress retinal fate in theJournal of cell science · 2020Article
- STRIPAK Limits Stem Cell Differentiation of a WNT Signaling Center to Control Planarian Axis Scaling.Current biology : CB · 2020Article
- STRIPAK directs PP2A activity toward MAP4K4 to promote oncogenic transformation of human cells.eLife · 2020Article
- Striatin Is Required for Hearing and Affects Inner Hair Cells and Ribbon Synapses.Frontiers in cell and developmental biology · 2020Article
- Redox inhibition of protein phosphatase PP2A: Potential implications in oncogenesis and its progression.Redox biology · 2019Review
- Striatin is a novel modulator of cell adhesion.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
19 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 3 institutions in 1 country.
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Abstract
Protein phosphatase 2A (PP2A) is a multifunctional serine/threonine phosphatase that is critical to many cellular processes including development, neuronal signaling, cell cycle regulation, and viral transformation. PP2A has been implicated in Ca(2+)-dependent signaling pathways, but how PP2A is targeted to these pathways is not understood. We have identified two calmodulin (CaM)-binding proteins that form stable complexes with the PP2A A/C heterodimer and may represent a novel family of PP2A B-type subunits. These two proteins, striatin and S/G(2) nuclear autoantigen (SG2NA), are highly related WD40 repeat proteins of previously unknown function and distinct subcellular localizations. Striatin has been reported to associate with the post-synaptic densities of neurons, whereas SG2NA has been reported to be a nuclear protein expressed primarily during the S and G(2) phases of the cell cycle. We show that SG2NA, like striatin, binds to CaM in a Ca(2+)-dependent manner. In addition to CaM and PP2A, several unidentified proteins stably associate with the striatin-PP2A and SG2NA-PP2A complexes. Thus, one mechanism of targeting and organizing PP2A with components of Ca(2+)-dependent signaling pathways may be through the molecular scaffolding proteins striatin and SG2NA.
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