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A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation
Open accessAbstract
Both F10 and BL6 sublines of B16 mouse melanoma cells are metastatic after intravenous injection, but only BL6 cells are metastatic after subcutaneous injection. Retrotransposon insertion was found to produce an N-terminally truncated form (Deltagamma1) of the B56gamma1 regulatory subunit isoform of protein phosphatase (PP) 2A in BL6 cells, but not in F10 cells. We found an interaction of paxillin with PP2A C and B56gamma subunits by co-immunoprecipitation. B56gamma1 co-localized with paxillin at focal adhesions, suggesting a role for this isoform in targeting PP2A to paxillin. In this regard, Deltagamma1 behaved similarly to B56gamma1. However, the Deltagamma1-containing PP2A heterotrimer was insufficient for the dephosphorylation of paxillin. Transfection with Deltagamma1 enhanced paxillin phosphorylation on serine residues and recruitment into focal adhesions, and cell spreading with an actin network. In addition, Deltagamma1 rendered F10 cells as highly metastatic as BL6 cells. These results suggest that mutations in PP2A regulatory subunits may cause malignant progression.
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“This notion corroborates with the previous notion on the role of B′ subunits as tumor suppressors [45–49].”
From PP2A-B′ holoenzyme substrate recognition, regulation and role in cytokinesis (2017) · cites this paper as [47]
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“Journal of Cell Science 121 (15) NCK 118 PY PY LIM1 LIM2 LIM3 LIM4LD2 LD3 LD5LD4LD1 31 Focal-adhesion targeting PY PY PTP-PEST PAK GITPIX FAK and Src kinases Rac1 Cell adhesion or integrin signaling PS 273 PP2A Localized lamellipodium formation Dephosphorylation Paxillin Fig.”
BackgroundInfluentialPhosphatase: PP2A structural importance, regulation and its aberrant expression in cancer
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“Moreover, association of increased cell motility and invasiveness due to altered PP2A activity was observed in BL6 mouse melanoma cells [65], lung carcinoma [66] and head and neck squamous carcinoma [67].”
Background
Metadata
- Authors
- Ito, A., Kataoka, T. R., Watanabe, M., Nishiyama, K., Mazaki, Y., Sabe, H., Kitamura, Y., & Nojima, H.
- Affiliations
- Medical & Biological Laboratories (Japan) (JP)
- Research Institute for Microbial Diseases, The University of Osaka (JP)
- Kyoto University (JP)
- Corresponding author
- Nojima, Hiroshi
- Venue
- The EMBO Journal
- Published
- 2000-02-15
- Volume
- 19
- Issue
- 4
- Pages
- 562-571
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC305594
- OpenAlex
- W2062708599
- Cited by
- 159
- References
- 40
- Citations by year
- 2025: 4 · 2024: 3 · 2023: 3 · 2022: 5 · 2021: 2 · 2020: 2 · 2019: 3 · 2018: 2 · 2017: 5 · 2016: 6 · 2015: 11 · 2014: 4 · 2013: 8 · 2012: 5
- FWCI
- 4.45
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- 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 › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- protein phosphatase 2A, protein phosphatase 2A regulatory subunit, truncated protein isoform, paxillin phosphorylation, cell motility, metastasis, melanoma, focal adhesions, retrotransposon insertion, actin cytoskeleton, cell spreading, malignant progression
- MeSH terms
- Animals, Base Sequence, Cell Cycle, Cell Movement, Cytoskeletal Proteins, Cytoskeleton, Melanoma, Experimental, Molecular Sequence Data, Phosphoprotein Phosphatases, Phosphoproteins, Phosphorylation, RNA, Messenger, RNA, Neoplasm, Serine, Tumor Cells, Cultured, Gene Expression, 3T3 Cells, DNA Primers, COS Cells, Protein Structure, Quaternary, Mice, Paxillin
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