Functional importance of PP2A regulatory subunit loss in breast cancer
Abstract
Purpose Protein phosphatase 2A (PP2A) is a family of serine/threonine phosphatases that regulate multiple cellular signalling pathways involved in proliferation, survival and apoptosis. PP2A inhibition occurs in many cancers and is considered a tumour suppressor. Deletion/downregulation of PP2A genes has been observed in breast tumours, but the functional role of PP2A subunit loss in breast cancer has not been investigated.Methods PP2A subunit expression was examined by immunohistochemistry in human breast tumours, and by qPCR and immunoblotting in breast cancer cell lines. PP2A subunits were inhibited by shRNA, and mutant PP2A genes overexpressed, in MCF10A and MCF7 cells, and growth and signalling in standard and three-dimensional cultures were assessed.Results Expression of PP2A-Aα, PP2A-Bα and PP2A-B'α subunits was significantly lower in primary human breast tumours and lymph node metastases, compared to normal mammary tissue. PP2A-Aα and the regulatory subunits PP2A-Bα, -Bδ and -B'γ were also reduced in breast cancer cell lines compared to normal mammary epithelial cells. Functionally, shRNA-mediated knockdown of PP2A-Bα, -B'α and -B'γ, but not PP2A-Aα, induced hyper-proliferation and large multilobular acini in MCF10A 3D cultures, characterised by activation of ERK. Expression of a breast cancer-associated PP2A-A mutant, PP2A-Aα-E64G, which inhibits binding of regulatory subunits to the PP2A core, induced a similar hyper-proliferative phenotype. Knockdown of PP2A-Bα also induced hyper-proliferation in MCF7 breast cancer cells.Conclusion These results suggest that loss of specific PP2A regulatory subunits is functionally important in breast tumourigenesis, and support strategies to enhance PP2A activity as a therapeutic approach in breast cancer.
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Deletions affecting PPP2R2A have been observed in prostate, ovarian and breast epithelial tumors.
“Deletions affecting the PPP2R2A gene have been observed in a number of epithelial tumors in prostate, ovarian and breast cancer patients (Cheng et al., 2011; Watt et al., 2017; Youn and Simon, 2013).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Watt et al., 2017
PP2A is a crucial member of the tumor suppressor family, and its alteration is linked to breast, oral, brain, and colorectal cancers.
“PP2A is a crucial member of the tumor suppressor family, and its alteration has been linked to various human malignancies, such as breast [ 1 , 2 ], oral [ 3 ], brain [ 4 ], and colorectal cancers (CRC) [ 5 ].”
From Targeting PP2A in cancer: an underrated option (2025) · cites this paper as [1]
In breast cancer, PP2A dysfunction is linked to reduced expression of both scaffold (PP2A-Aα and PP2A-Bα) and regulatory (PP2A-B′α) subunits.
“However, in breast cancer, PP2A dysfunction is linked to the reduced expression of both scaffold (PP2A-Aα and PP2A-Bα) and regulatory (PP2A-B′α) subunits.”
From Targeting PP2A in cancer: an underrated option (2025) · cites this paper as [1]
Cites
1 retracted
Chen, W., Arroyo, J. D., Timmons, J. C., Possemato, R., & Hahn, W. C. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1103 · Cited by 159 · see citing works
RetractedComprehensive molecular portraits of human breast tumours
The Cancer Genome Atlas Network (2012) · Nature · doi:10.1038/nature11412 · Cited by 12,129 · see citing works
The genomic and transcriptomic architecture of 2,000 breast tumours reveals novel subgroups
METABRIC Group, Curtis, C., Shah, S. P., Chin, S.-F., Turashvili, G., Rueda, O. M., Dunning, M. J., Speed, D., Lynch, A. G., Samarajiwa, S., et al. (2012) · Nature · doi:10.1038/nature10983 · Cited by 6,097 · see citing works
Debnath, J., Muthuswamy, S. K., & Brugge, J. S. (2003) · Methods · doi:10.1016/s1046-2023(03)00032-x · Cited by 2,001 · see citing works
Modelling glandular epithelial cancers in three-dimensional cultures
Debnath, J., & Brugge, J. S. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1695 · Cited by 1,014 · see citing works
Focal adhesion regulation of cell behavior
Wozniak, M. A., Modzelewska, K., Kwong, L., & Keely, P. J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.04.007 · Cited by 995 · see citing works
Sensing the environment: a historical perspective on integrin signal transduction
Miranti, C. K., & Brugge, J. S. (2002) · Nature Cell Biology · doi:10.1038/ncb0402-e83 · Cited by 851 · see citing works
Molecular mechanisms underlying ErbB2/HER2 action in breast cancer
Harari, D., & Yarden, Y. (2000) · Oncogene · doi:10.1038/sj.onc.1203973 · Cited by 636 · see citing works
ErbB2, but not ErbB1, reinitiates proliferation and induces luminal repopulation in epithelial acini
Muthuswamy, S. K., Li, D., Lelièvre, S. A., Bissell, M. J., & Brugge, J. S. (2001) · Nature Cell Biology · doi:10.1038/ncb0901-785 · Cited by 554 · see citing works
Breast Cancer–Associated PIK3CA Mutations Are Oncogenic in Mammary Epithelial Cells
Isakoff, S. J., Engelman, J. A., Irie, H. Y., Luo, J., Brachmann, S. M., Pearline, R. V., Cantley, L. C., & Brugge, J. S. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-2612 · Cited by 505 · see citing works
Structure of the Protein Phosphatase 2A Holoenzyme
Xu, Y., Xing, Y., Chen, Y., Chao, Y., Lin, Z., Fan, E., Yu, J. W., Strack, S., Jeffrey, P. D., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.11.033 · Cited by 450 · see citing works
PP2A: the expected tumor suppressor
Janssens, V., Goris, J., & Van Hoof, C. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.12.004 · Cited by 426 · see citing works
Protein phosphatase 2A: a target for anticancer therapy
Perrotti, D., & Neviani, P. (2013) · The Lancet Oncology · doi:10.1016/s1470-2045(12)70558-2 · Cited by 400 · see citing works
McCright, B., Rivers, A. M., Audlin, S., & Virshup, D. M. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.36.22081 · Cited by 382 · see citing works
Kuo, Y.-C., Huang, K.-Y., Yang, C.-H., Yang, Y.-S., Lee, W.-Y., & Chiang, C.-W. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709585200 · Cited by 367 · see citing works
Identification of specific PP2A complexes involved in human cell transformation
Chen, W., Possemato, R., Campbell, K. T., Plattner, C. A., Pallas, D. C., & Hahn, W. C. (2004) · Cancer Cell · doi:10.1016/s1535-6108(04)00026-1 · Cited by 325 · see citing works
Tolstykh, T., Lee, J., Vafai, S. B., & Stock, J. B. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5682 · Cited by 233 · see citing works
Outgrowth of single oncogene-expressing cells from suppressive epithelial environments
Leung, C. T., & Brugge, J. S. (2012) · Nature · doi:10.1038/nature10826 · Cited by 227 · see citing works
CIP2A Is Associated with Human Breast Cancer Aggressivity
Côme, C., Laine, A., Chanrion, M., Edgren, H., Mattila, E., Liu, X., Jonkers, J., Ivaska, J., Isola, J., Darbon, J.-M., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-3283 · Cited by 221 · see citing works
Calin, G. A., di Iasio, M. G., Caprini, E., Vorechovsky, I., Natali, P. G., Sozzi, G., Croce, C. M., Barbanti-Brodano, G., Russo, G., & Negrini, M. (2000) · Oncogene · doi:10.1038/sj.onc.1203389 · Cited by 219 · see citing works
Identification of PP2A Complexes and Pathways Involved in Cell Transformation
Sablina, A. A., Hector, M., Colpaert, N., & Hahn, W. C. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-2855 · Cited by 193 · see citing works
Targeting c-MYC by antagonizing PP2A inhibitors in breast cancer
Janghorban, M., Farrell, A. S., Allen-Petersen, B. L., Pelz, C., Daniel, C. J., Oddo, J., Langer, E. M., Christensen, D. J., & Sears, R. C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317630111 · Cited by 186 · see citing works
Longin, S., Zwaenepoel, K., Louis, J. V., Dilworth, S., Goris, J., & Janssens, V. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704059200 · Cited by 184 · see citing works
Debnath, J., Walker, S. J., & Brugge, J. S. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200304159 · Cited by 164 · see citing works
Critical Role for Protein Phosphatase 2A Heterotrimers in Mammalian Cell Survival*
Strack, S., Cribbs, J., & Gomez, L. L. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408015200 · Cited by 160 · see citing works
Yu, X. X., Du, X., Moreno, C. S., Green, R. E., Ogris, E., Feng, Q., Chou, L., McQuoid, M. J., & Pallas, D. C. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.1.185 · Cited by 160 · see citing works
A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation
Ito, A., Kataoka, T. R., Watanabe, M., Nishiyama, K., Mazaki, Y., Sabe, H., Kitamura, Y., & Nojima, H. (2000) · The EMBO Journal · doi:10.1093/emboj/19.4.562 · Cited by 159 · see citing works
Ruediger, R., Pham, H. T., & Walter, G. (2001) · Oncogene · doi:10.1038/sj.onc.1204059 · Cited by 149 · see citing works
Kim, K.-Y., Baek, A., Hwang, J.-E., Choi, Y. A., Jeong, J., Lee, M.-S., Cho, D. H., Lim, J., Kim, K. I., & Yang, Y. D. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2641 · Cited by 135 · see citing works
Roberts, K. G., Smith, A. M., McDougall, F. K., Carpenter, H., Horan, M. P., Neviani, P., Powell, J. A., Thomas, D., Guthridge, M. A., Perrotti, D., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2544 · Cited by 134 · see citing works
Self-citationAdams, D. G., Coffee, R. L., Zhang, H., Pelech, S., Strack, S., & Wadzinski, B. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502464200 · Cited by 133 · see citing works
Brummer, T., Schramek, D., Hayes, V. M., Bennett, H. L., Caldon, C. E., Musgrove, E. A., & Daly, R. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509567200 · Cited by 124 · see citing works
Rincón, R., Cristóbal, I., Zazo, S., Arpí, O., Menéndez, S., Manso, R., Lluch, A. M., Eroles, P., Rovira, A., Albanell, J., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3012 · Cited by 101 · see citing works
Ruediger, R., Ruiz, J., & Walter, G. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05744-11 · Cited by 98 · see citing works
ZHOU, J., PHAM, H. T., RUEDIGER, R., & WALTER, G. (2003) · Biochemical Journal · doi:10.1042/bj20021244 · Cited by 95 · see citing works
Oncogenic pathways in hereditary and sporadic breast cancer
Kenemans, P., Verstraeten, R. A., & Verheijen, R. H. M. (2004) · Maturitas · doi:10.1016/j.maturitas.2004.06.005 · Cited by 92 · see citing works
Protein Phosphatase 2A Holoenzyme Assembly
Strack, S., Ruediger, R., Walter, G., Dagda, R. K., Barwacz, C. A., & Cribbs, J. T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202992200 · Cited by 83 · see citing works
The ErbB2 Signaling Network as a Target for Breast Cancer Therapy
Badache, A., & Gonçalvès, A. (2006) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-006-9009-1 · Cited by 73 · see citing works
Sontag, J. M., & Sontag, E. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6300-7 · Cited by 57 · see citing works
Karakosta, A., Ch, G., Charalabopoulos, A., Peschos, D., Batistatou, A. K., & Charalabopoulos, K. (2005) · PubMed · Cited by 53 · see citing works
Smith, A. M., Dun, M. D., Lee, E. M., Harrison, C. L., Kahl, R. G. S., Flanagan, H. M., Panicker, N., Mashkani, B., Don, A. S., Morris, J. C., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.10167 · Cited by 49 · see citing works
Self-citationBaldacchino, S., Saliba, C., Magri, V. P., Fenech, A. G., Borg, N., & Grech, G. (2014) · The EPMA Journal · doi:10.1186/1878-5085-5-3 · Cited by 46 · see citing works
Copeland, B. T., Bowman, M. J., & Ashman, L. K. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0468 · Cited by 45 · see citing works
Self-citationEsplin, E. D., Ramos, P., Martinez, B., Tomlinson, G. E., Mumby, M. C., & Evans, G. A. (2005) · Genes Chromosomes and Cancer · doi:10.1002/gcc.20284 · Cited by 40 · see citing works
Ripple, M. O., Kalmadi, S., & Eastman, A. R. (2005) · Breast Cancer Research and Treatment · doi:10.1007/s10549-005-4794-6 · Cited by 37 · see citing works
Altered PPP2R2A and Cyclin D1 expression defines a subgroup of aggressive luminal-like breast cancer
de Beça, F. F., Pereira, M., Cameselle‐Teijeiro, J., Martins, D. F., & Schmitt, F. C. (2015) · BMC Cancer · doi:10.1186/s12885-015-1266-1 · Cited by 33 · see citing works
Myeloid Leukemia - Basic Mechanisms of Leukemogenesis
Koschmieder, S., & Krug, U. O. (2011) · InTech eBooks · doi:10.5772/1245 · Cited by 26 · see citing works
Requirement of protein phosphatase 2A for recruitment of IQGAP1 to Rac‐bound β1 integrin
Suzuki, K., Chikamatsu, Y., & Takahashi, K. (2004) · Journal of Cellular Physiology · doi:10.1002/jcp.20249 · Cited by 25 · see citing works
A Working Model for The Time Sequence of Genetic Changes in Breast Tumorigenesis
Singletary, E. S. (2002) · Journal of the American College of Surgeons · doi:10.1016/s1072-7515(01)01108-5 · Cited by 24 · see citing works
Takahashi, K. (2001) · BMC Cell Biology · doi:10.1186/1471-2121-2-23 · Cited by 23 · see citing works
Suzuki, K., & Takahashi, K. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.08.037 · Cited by 21 · see citing works
Mitotic dissociation of IQGAP1 from Rac-bound β1-integrin is mediated by protein phosphatase 2A
Nakajima, E., Suzuki, K., & Takahashi, K. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.11.023 · Cited by 19 · see citing works
Ser/Thr Phosphatases: The New Frontier for Myeloid Leukemia Therapy?
Amanda, M., Kathryn, G., & Nicole, M. (2011) · InTech eBooks · doi:10.5772/26425 · Cited by 3 · see citing works
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Meeusen, B., & Janssens, V. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2017.10.002 · Cited by 96 · see citing works
PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer
(2019) · Advances in Cancer Research · doi:10.1016/bs.acr.2019.03.009 · Cited by 93 · see citing works
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Haanen, T. J., O’Connor, C. M., & Narla, G. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102656 · Cited by 36 · see citing works
Zhao, Z., Kurimchak, A., Nikonova, A. S., Feiser, F., Wasserman, J. S., Fowle, H. A., Varughese, T., Connors, M., Johnson, K. J., Makhov, P. B., et al. (2019) · Oncogenesis · doi:10.1038/s41389-019-0180-9 · Cited by 31 · see citing works
Otani, Y., Sur, H. P., Rachaiah, G., Namagiri, S., Chowdhury, A. K., Lewis, C. T., Shimizu, T., Gangaplara, A., Wang, X., Vézina, A., et al. (2021) · Neuro-Oncology · doi:10.1093/neuonc/noab014 · Cited by 32 · see citing works
Panicker, N., Coutman, M., Lawlor-O’Neill, C., Kahl, R. G. S., Roselli, S., & Verrills, N. M. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00358 · Cited by 27 · see citing works
Self-citationXie, F., Li, F., Li, R., Liu, Z., Shi, J., Zhang, C., & Dong, N. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118086 · Cited by 19 · see citing works
Khanna, A., Thoms, J. A. I., Stringer, B. W., Chung, S. A., Ensbey, K. S., Jue, T. R., Jahan, Z., Subramanian, S., Anande, G., Shen, H. M., et al. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0934 · Cited by 19 · see citing works
Breast Cancer Genomics: Primary and Most Common Metastases
Bennett, C., Carroll, C., Wright, C., Awad, B., Park, J. M., Farmer, M. B., Brown, E. (., Heatherly, A., & Woodard, S. A. (2022) · Cancers · doi:10.3390/cancers14133046 · Cited by 18 · see citing works
Sekihara, K., Saitoh, K., Yang, H., Kawashima, H., Kazuno, S., Kikkawa, M., Arai, H., Miida, T., Hayashi, N., Sasai, K., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0199117 · Cited by 15 · see citing works
Singh, D., Qiu, Z., Spehar, J. M., Fa, P., Thomas, H., Prasad, C. B., Cai, S., Wang, J. J., Yan, C., Zhang, X., et al. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.217110 · Cited by 14 · see citing works
FTY720 in resistant human epidermal growth factor receptor 2-positive breast cancer
Chung, W., Huang, W.-L., Liao, W., Hung, C.-H., Chiang, C., Cheung, C. H. A., & Su, W. (2022) · Scientific Reports · doi:10.1038/s41598-021-04328-y · Cited by 13 · see citing works
Kisspeptin Inhibits Colorectal Cancer Cell Invasiveness by Activating PKR and PP2A
Kim, J. N., Kim, T. H., Yoon, J.-H., & Cho, S. (2018) · Anticancer Research · doi:10.21873/anticanres.12918 · Cited by 10 · see citing works
Yin, S., Chen, Y., Tong, H., Li, T., Qin, Z., Zhu, J., & He, W. (2022) · Oncology Letters · doi:10.3892/ol.2022.13221 · Cited by 10 · see citing works
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Wang, Y., Xie, W., Hou, M., Tian, J., Zhang, X., Ren, Q., Huang, Y., & Chen, J. (2021) · Aging · doi:10.18632/aging.202641 · Cited by 7 · see citing works
Ivovič, D., Kabelíková, P., & Jurkovičová, D. (2023) · Neoplasma · doi:10.4149/neo_2023_230806n411 · Cited by 7 · see citing works
Zach, R., Annis, M., Martin-Guerrero, S. M., Alatawi, A., Chia, K. H., Meredith, M., Osborn, K., Peter, N., Pearce, W., Booth, J., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-62943-z · Cited by 4 · see citing works
Su, B., LIM, D. J., Qi, C., Zhang, Z., Wang, J., Zhang, F., Dong, C., & Feng, Z. (2023) · Cell Death and Disease · doi:10.1038/s41419-023-05649-8 · Cited by 4 · see citing works
Tomasin, R., Rodrigues, A. M., Manucci, A. C., & Bruni‐Cardoso, A. (2023) · Journal of Cell Science · doi:10.1242/jcs.261178 · Cited by 4 · see citing works
Zhang, F., Wang, L., Liu, S., Zhao, L., & Su, Y. (2024) · FEBS Journal · doi:10.1111/febs.17247 · Cited by 2 · see citing works
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Hamouda, A. O., Sarg, N. H., Ibrahim, S. I., Hamdy, R. M., Soliman, S. S. M., & Omar, H. A. (2025) · Archiv der Pharmazie · doi:10.1002/ardp.70064 · Cited by 2 · see citing works
Yamauchi, H., Oishi, A., Ajiro, M., Nakayama, A., Nishimura, K., Kurikawa, M., Yoshida, M., Kudo, R., Koizumi, M., Izumi-Tamura, T., et al. (2025) · BioTechniques · doi:10.1080/07366205.2025.2523093 · Cited by 1 · see citing works
Wang, H., Chen, X., Bao, L., & Zhang, X. (2020) · Medicine · doi:10.1097/md.0000000000022199 · Cited by 1 · see citing works
Tomasin, R., Rodrigues, A. M., Manucci, A. C., & Bruni‐Cardoso, A. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.03.13.532403
Yoga, I. M. B. K., Irmasari, I., Widyardhita, M. H., Maharani, D., Widayanti, W. R., Amalia, A., Ningsih, S. R., Saputra, B. W., Haidar, I., Putri, D. D. P., et al. (2026) · Phytomedicine · doi:10.1016/j.phymed.2026.158698
Wang, Y., Sun, Y., Fu, Y., Wei, Z., Zhao, L., & Zhang, G. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1881297
- Authors
- Watt, L. F., Panicker, N., Mannan, A., Copeland, B., Kahl, R. G. S., Dun, M. D., Young, B., Roselli, S., & Verrills, N. M.
- Affiliations
- Hunter Medical Research Institute (AU)
- City Of Hope National Medical Center (US)
- John Hunter Hospital (AU)
- Corresponding author
- Verrills, Nicole M.
- Venue
- Breast Cancer Research and Treatment
- Published
- 2017-07-25
- Volume
- 166
- Issue
- 1
- Pages
- 117-131
- ISSN
- 0167-6806 (ISSN-L)
- 1573-7217
- OpenAlex
- W2737177090
- Cited by
- 29
- References
- 53
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 2 · 2023: 4 · 2022: 4 · 2021: 2 · 2020: 4 · 2019: 2 · 2018: 4 · 2017: 1
- FWCI
- 1.23
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Breast Cancer Research and Treatment (publishedVersion)
- PubMed (publishedVersion)
- NOVA (University of Newcastle Australia) (submittedVersion)
- Funders
- Cure Cancer Australia Foundation
- Cancer Council NSW
- Pink Frangipani Ball
- Cancer Institute NSW
- Hunter Medical Research Institute
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- protein phosphatase 2A, PP2A regulatory subunit, breast cancer, tumour suppressor, cell proliferation, ERK signaling, lymph node metastasis, tumourigenesis, therapeutic target
- MeSH terms
- Breast Neoplasms, Cell Transformation, Neoplastic, Cells, Cultured, Epithelial Cells, Female, Humans, Immunohistochemistry, Mutation, Gene Expression Regulation, Neoplastic, Protein Subunits, Cell Line, Tumor, Extracellular Signal-Regulated MAP Kinases, Cell Proliferation, Proto-Oncogene Proteins c-akt, Protein Phosphatase 2, Gene Knockdown Techniques
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