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WD40 Repeat Proteins Striatin and S/G2 Nuclear Autoantigen Are Members of a Novel Family of Calmodulin-binding Proteins That Associate with Protein Phosphatase 2A
Open accessAbstract
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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“The three Striatin family members share four conserved domains: a coiled coil domain, a caveolin-binding domain, and a calmodulin-binding domain within the N-terminus; and a WD40 repeat domain within the C-terminus (Chen et al., 2014; Moreno et al., 2000).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Moreno et al., 2000
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Metadata
- Authors
- Moreno, C. S., Park, S., Nelson, K., Ashby, D., Hubalek, F., Lane, W. S., & Pallas, D. C.
- Affiliations
- Emory University (US)
- Dana-Farber Cancer Institute (US)
- Harvard University (US)
- Corresponding author
- Pallas, David C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-02
- Volume
- 275
- Issue
- 8
- Pages
- 5257-5263
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC3505218
- OpenAlex
- W1964595176
- Cited by
- 194
- References
- 28
- Citations by year
- 2026: 3 · 2025: 9 · 2024: 4 · 2023: 2 · 2022: 3 · 2021: 3 · 2020: 6 · 2019: 7 · 2018: 8 · 2017: 11 · 2016: 6 · 2015: 7 · 2014: 10 · 2013: 6 · 2012: 6
- FWCI
- 4.22
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (CA57327, R01CA057327)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- protein phosphatase 2A, calmodulin-binding proteins, WD40 repeat proteins, striatin, calmodulin, postsynaptic density, cell cycle
- MeSH terms
- Amino Acid Sequence, Animals, Epitopes, Autoantigens, Calcium, Calmodulin-Binding Proteins, Histones, Membrane Proteins, Methylation, Molecular Sequence Data, Nerve Tissue Proteins, Phosphoprotein Phosphatases, Phosphorylation, Precipitin Tests, Protein Binding, Mass Spectrometry, Signal Transduction, 3T3 Cells, Conserved Sequence, Sequence Homology, Amino Acid, Mice, Protein Phosphatase 2
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