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

Moreno, Carlos S.; Park, Susan; Nelson, Kasey; Ashby, Danita; Hubalek, Frantisek; Lane, William S.; Pallas, David C.

doi:10.1074/jbc.275.8.5257

Cited by 194Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesSignaling Pathways in Disease

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

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Moreno, Carlos S., Park, Susan, Nelson, Kasey, Ashby, Danita, Hubalek, Frantisek, Lane, William S., Pallas, David C.·2000·Journal of Biological Chemistry

DOI 10.1074/jbc.275.8.5257PMC PMC3505218

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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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Striatin family members share a coiled-coil domain, a caveolin-binding domain, and a calmodulin-binding domain in the N-terminus, plus a C-terminal WD40 repeat domain.
“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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Background
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Self-citation
A PP2A Phosphatase High Density Interaction Network Identifies a Novel Striatin-interacting Phosphatase and Kinase Complex Linked to
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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.
ORCID: Moreno, Carlos S.
Park, Susan
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2000-02
Volume: 275
Issue: 8
Pages: 5257-5263
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.275.8.5257
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7555 d)
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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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

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