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A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation
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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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“The procedure for immunoprecipitation with RP6 was essentially similar to that described previously.(27) To use 3E1 for immunoprecipitation, 100 g of the 3E1 antibody were crosslinked with 100 l of the affinity-purified goat anti-IgY antibody-conjugated Microbeads (2 mg IgG/ml Microbeads, 50% slurry in Tris-buffered s…”
MethodSelf-citationA B56 regulatory subunit of protein phosphatase 2A localizes to nuclear speckles in cardiomyocytes
Gigena, M. S., Ito, A., Nojima, H., & Rogers, T. B. (2005) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.01291.2004 · Cited by 34
“The production and purification of polyclonal anti-B56 was previously described (12).”
BackgroundInfluentialSelf-citationIncreased Expression of a Nucleolar Nop5/Sik Family Member in Metastatic Melanoma Cells
Nakamoto, K., Ito, A., Watabe, K., Koma, Y., Asada, H., Yoshikawa, K., Shinomura, Y., Matsuzawa, Y., Nojima, H., & Kitamura, Y. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62523-0 · Cited by 32
“The method for constructing a subtracted cDNA library has been described previously.(19,21,35) After four rounds of subtraction, 1400 clones were rescued and subjected to Northern blot analysis with the RNA of F10 and BL6 cells.”
MethodSelf-citationModulation of Thr Phosphorylation of Integrin β1 during Muscle Differentiation
Kim, S., Kwon, M. S., Park, C. S., Choi, K.-R., Chun, J., Ahn, J., & Song, W. K. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311581200 · Cited by 32
Sato, J., Shimizu, H., Kasama, T., Yabuta, N., & Nojima, H. (2009) · Genes to Cells · doi:10.1111/j.1365-2443.2009.01296.x · Cited by 27
“Of relevance to this paper is the B′α (alternatively called B56gamma) subunit subfamily, which includes three alternative splicing variants with differing subcellular localizations (Ito et al. 2000), namely, either in the nucleus (B′α1 and B′α2) or in the cytoplasm (B′α3).”
BackgroundMethodInfluentialSelf-citationDeichmann, M., Polychronidis, M., Wacker, J., Thome, M., & Näher, H. (2001) · Melanoma Research · doi:10.1097/00008390-200112000-00004 · Cited by 30
Paxillin phosphorylation at serine 273 and its effects on Rac, Rho and adhesion dynamics
Tang, K., Boudreau, C. G., Brown, C. M., et al. (2018) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1006303 · Cited by 30
A derivative of oleamide potently inhibits the spontaneous metastasis of mouse melanoma BL6 cells
Ito, A. (2004) · Carcinogenesis · doi:10.1093/carcin/bgh208 · Cited by 30
Self-citationFunctional importance of PP2A regulatory subunit loss in breast cancer
Watt, L. F., Panicker, N., Mannan, A., Copeland, B., Kahl, R. G. S., Dun, M. D., Young, B., Roselli, S., & Verrills, N. M. (2017) · Breast Cancer Research and Treatment · doi:10.1007/s10549-017-4403-5 · Cited by 29
Liang, Z., Ge, X., Xu, M., Qin, H., Wu, M., Shen, M., Zhang, Y., Liu, X., Chen, K., Li, W., et al. (2021) · Cancer Science · doi:10.1111/cas.14863 · Cited by 28
Silverstein, A. M., Davis, A. J., Bielinski, V. A., Esplin, E. D., Mahmood, N. A., & Mumby, M. C. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00168-6 · Cited by 28
Ravi, A., Kaushik, S., Ravichandran, A., Pan, C. Q., & Low, B. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.616839 · Cited by 27
“Various processes modulate the functions of DLC1: phosphorylation by Akt (36), interactions with FAK and the tensin family proteins targeting it to FAs (17, 20, 37), its dimerization (38), or masking by other protein partners (24, 39).”
BackgroundInfluentialJanssens, V., Zwaenepoel, K., Rossé, C., Petit, M. M. R., Goris, J., & Parker, P. J. (2016) · Journal of Cell Science · doi:10.1242/jcs.175778 · Cited by 27
“Earlier work has already demonstrated a role for a specific PP2A-B′γ1 complex in regulating paxillin dephosphorylation at focal adhesions (Ito et al., 2000) – further underscoring the importance of localised regulation of protein dephosphorylation at sites of cell–substratum contacts – as well as…”
BackgroundBerrou, E., & Bryckaert, M. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.12.002 · Cited by 26
Ito, A., Koma, Y.-I., Watabe, K., Nagano, T., Endo, Y., Nojima, H., & Kitamura, Y. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)63800-x · Cited by 24
“Our previous work showed that 1 prevents the B56 1-containing PP2A heterotrimer from dephosphorylating its specific substrates.(15) Consistent with this inhibitory effect of 1, NIH3T3 cells that stably express 1 are defective in cell-cycle checkpoint regulation when exposed to -radiation.”
BackgroundMethodResultInfluentialSelf-citationGilan, O., Diesch, J., Amalia, M., Jastrzebski, K., Chüeh, A. C., Verrills, N. M., Pearson, R. B., Mariadason, J. M., Tulchinsky, E. M., Hannan, R. D., et al. (2014) · Oncogene · doi:10.1038/onc.2014.26 · Cited by 24
Tabara, H., Naito, Y., Ito, A., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0026034 · Cited by 24
“Moreover, both GAK and its association partner clathrin heavy chain (CHC), localize to both the cytoplasm and nucleus with distinct association modes, and CHC colocalizes with GAK in the nucleus, while Cyclin G and PP2A B’c are also present in the nucleus [17], [20], [21].”
BackgroundSelf-citationChe, L., Wu, J., Xu, C.-Y., Cai, Y., Lin, J., Du, Z., Shi, J., Han, T., He, Y.-Q., Lin, Y., et al. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115132 · Cited by 23
Pleiotropy of PP2A Phosphatases in Cancer with a Focus on Glioblastoma IDH Wildtype
Kashani, E., & Vassella, E. (2022) · Cancers · doi:10.3390/cancers14215227 · Cited by 22
“Sustained p-ATM activity can trigger phosphorylation of PPP2R5C complexes at Ser510, leading to PPP2R5Ccontaining PP2A complex formation, which contributes to p53 activation [128,132].”
BackgroundInfluential
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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