Molecular cloning of cDNAs encoding two isoforms of the catalytic subunit of protein phosphatase 2A
Abstract
Clones coding for the catalytic subunit of one of the major protein phosphatases (type 2A) were isolated from a porcine cDNA library. Sequence analysis indicated that two different mRNA species coded for this enzyme. The deduced amino acid sequences of the two forms (alpha and beta) of the enzyme were 98% identical and showed 95% identity with the partial sequence of the rabbit enzyme determined by amino acid sequencing. The use of specific oligonucleotide probes indicated that the mRNAs coding for the alpha and beta forms were about 2 kilobases in length, present in equal amounts in a porcine cell line (LLC-PK1), and were the products of two distinct genes. Southern analysis using the coding region of the alpha phosphatase cDNA as a probe suggested the existence of additional related phosphatase genes.
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PP2A/Cα and PP2A/Cβ share about 98% sequence identity, with the N-terminus being the most variable region.
“The two isoforms share approximately 98% sequence identity, with the most variable region being the N-terminus (Stone et al., 1987).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Stone et al., 1987
The paralogs of PP2A-A (Aα and Aβ) and PP2A-C (Cα and Cβ) share 87% and 98% sequence identity, respectively.
“The paralogs of PP2A-A (Aα and Aβ) and PP2A-C (Cα and Cβ) share 87% and 98% sequence identity, respectively [ 29 , 32 ].”
From Targeting PP2A in cancer: an underrated option (2025) · cites this paper as [32]
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- Authors
- Stone, S. R., Hofsteenge, J., & Hemmings, B. A.
- Affiliations
- Friedrich Miescher Institute (CH)
- ORCID
- Stone, Stuart R.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1987-11
- Volume
- 26
- Issue
- 23
- Pages
- 7215-7220
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2027213610
- Cited by
- 168
- References
- 0
- Citations by year
- 2025: 2 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 1 · 2017: 4 · 2016: 3 · 2015: 4 · 2014: 2 · 2013: 2 · 2012: 1
- FWCI
- 3.44
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemistry (publishedVersion)
- PubMed (publishedVersion)
- 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, catalytic subunit, protein isoforms, alpha and beta subunits, cDNA cloning, pigs, mRNA species, gene identity, phosphatase genes, LLC-PK1 cells
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, DNA, Genes, Isoenzymes, Molecular Sequence Data, Muscles, Phosphoprotein Phosphatases, Rabbits, Swine, Macromolecular Substances, Protein Phosphatase 2
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