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PP2A holoenzyme assembly: in cauda venenum (the sting is in the tail)
Abstract
Protein phosphatase 2A (PP2A), a major phospho-serine/threonine phosphatase, is conserved throughout eukaryotes. It dephosphorylates a plethora of cellular proteins, including kinases and other signaling molecules involved in cell division, gene regulation, protein synthesis and cytoskeleton organization. PP2A enzymes typically exist as heterotrimers comprising catalytic C-, structural A- and regulatory B-type subunits. The B-type subunits function as targeting and substrate-specificity factors; hence, holoenzyme assembly with the appropriate B-type subunit is crucial for PP2A specificity and regulation. Recently, several biochemical and structural determinants have been described that affect PP2A holoenzyme assembly. Moreover, the effects of specific post-translational modifications of the C-terminal tail of the catalytic subunit indicate that a 'code' might regulate dynamic exchange of regulatory B-type subunits, thus affecting the specificity of PP2A.
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“The unstructured C-terminus of PP2A/C is subject to post-translational modifications during the process of trimeric PP2A biogenesis, including phosphorylation of T304 and Y307 and carboxymethylation on L309 (Janssens et al., 2008; Lee and Pallas, 2007; Löw et al., 2014).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Janssens et al., 2008
In the citing paper
“Besides twenty PP2A subunit encoding genes, some of which are tissue-specifically expressed, five additional genes encode major regulators of active PP2A trimer assembly, and at least seven genes encode cellular PP2A inhibitors”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [13]
In the citing paper
“the PME-1 and LCMT-1 transgenic models provide nevertheless further evidence for a role of these PP2A trimers in tau dephosphorylation, and additionally, in the regulation of APP phosphorylation.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [13]
In the citing paper
“Initial studies have pointed to the reversible methylation of a specific residue (L309) at the C-terminal tail of the catalytic subunit [ 63 – 65 ]. This modification appears to be critical in modulating the binding affinity of the regulatory subunit, contributing to the formation of distinct heterotrimeric complexes.”
From Targeting PP2A in cancer: an underrated option (2025) · cites this paper as [64]
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Metadata
- Authors
- Janssens, V., Longin, S., & Goris, J.
- Affiliations
- KU Leuven (BE)
- Corresponding author
- Goris, Jozef
- ORCID
- Janssens, Veerle
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2008-03
- Volume
- 33
- Issue
- 3
- Pages
- 113-121
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2165421630
- Cited by
- 390
- References
- 77
- Citations by year
- 2026: 2 · 2025: 9 · 2024: 8 · 2023: 18 · 2022: 19 · 2021: 16 · 2020: 17 · 2019: 21 · 2018: 15 · 2017: 25 · 2016: 29 · 2015: 17 · 2014: 33 · 2013: 37 · 2012: 31
- FWCI
- 2.39
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Biochemical Sciences (publishedVersion)
- PubMed (publishedVersion)
- Lirias (submittedVersion)
- Funders
- Fonds Wetenschappelijk Onderzoek
- Vlaamse regering
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- protein phosphatase 2A, post-translational modification, substrate specificity, phosphatase regulation, Caenorhabditis elegans
- MeSH terms
- Animals, Catalysis, Humans, Models, Biological, Protein Conformation, Substrate Specificity, Protein Structure, Secondary, Holoenzymes, Protein Subunits, Protein Phosphatase 2
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