Dysregulation of Ezrin Phosphorylation Prevents Metastasis and Alters Cellular Metabolism in Osteosarcoma
Open accessPublished version of a preprint
Abstract
Ezrin links the plasma membrane to the actin cytoskeleton where it plays a pivotal role in the metastatic progression of several human cancers; however, the precise mechanistic basis for its role remains unknown. Here, we define transitions between active (phosphorylated open) and inactive (dephosphorylated closed) forms of Ezrin that occur during metastatic progression in osteosarcoma. In our evaluation of these conformations we expressed C-terminal mutant forms of Ezrin that are open (phosphomimetic T567D) or closed (phosphodeficient T567A) and compared their biologic characteristics to full-length wild-type Ezrin in osteosarcoma cells. Unexpectedly, cells expressing open, active Ezrin could form neither primary orthotopic tumors nor lung metastases. In contrast, cells expressing closed, inactive Ezrin were also deficient in metastasis but were unaffected in their capacity for primary tumor growth. By imaging single metastatic cells in the lung, we found that cells expressing either open or closed Ezrin displayed increased levels of apoptosis early after their arrival in the lung. Gene expression analysis suggested dysregulation of genes that are functionally linked to carbohydrate and amino acid metabolism. In particular, cells expressing closed, inactive Ezrin exhibited reduced lactate production and basal or ATP-dependent oxygen consumption. Collectively, our results suggest that dynamic regulation of Ezrin phosphorylation at amino acid T567 that controls structural transitions of this protein plays a pivotal role in tumor progression and metastasis, possibly in part by altering cellular metabolism. Cancer Res; 72(4); 1001–12. ©2011 AACR.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cytoskeletal linker ezrin provides a scaffold for PI3K-AKT signalling and facilitates survival through stresses that disseminated tumour cells first encounter within the lung.
“The cytoskeletal linker ezrin provides a scaffold for PI3K-AKT signalling and facilitates survival through the stresses that disseminated tumour cells first encounter within the lung 72,73,74 .”
From Osteosarcoma (2022) · cites this paper as [74]
Ex vivo techniques have been adapted to study tumour-host interactions, screen for metastasis-related vulnerabilities, and validate hits from other screens.
“These techniques have been adapted to study tumour-host interactions, to screen for metastasis-related vulnerabilities and to validate hits identified in other screens 74,75,92,216,217,218,219 .”
From Osteosarcoma (2022) · cites this paper as [74]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation
Vander Heiden, M. G., Cantley, L. C., & Thompson, C. B. (2009) · Science · doi:10.1126/science.1160809 · Cited by 16,197 · see citing works
Dissemination and growth of cancer cells in metastatic sites
Chambers, A. F., Groom, A. C., & MacDonald, I. C. (2002) · Nature reviews. Cancer · doi:10.1038/nrc865 · Cited by 3,920 · see citing works
Breast cancer metastasis: markers and models
Weigelt, B., Peterse, J. L., & van't Veer, L. J. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1670 · Cited by 2,232 · see citing works
Organizing the cell cortex: the role of ERM proteins
Fehon, R. G., McClatchey, A. I., & Bretscher, A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2866 · Cited by 1,044 · see citing works
Fidler, I. J. (1970) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/45.4.773 · Cited by 1,025 · see citing works
Brick by brick: metabolism and tumor cell growth
DeBerardinis, R. J., Sayed, N., Ditsworth, D., & Thompson, C. B. (2008) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2008.02.003 · Cited by 1,018 · see citing works
Wu, M., Neilson, A., Swift, A. L., Moran, R., Tamagnine, J., Parslow, D., Armistead, S., Lemire, K., Orrell, J., Teich, J., et al. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00247.2006 · Cited by 922 · see citing works
Tsukita, S., Oishi, K., Sato, N., Sagara, J., Kawai, A., & Tsukita, S. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.126.2.391 · Cited by 779 · see citing works
The membrane-cytoskeleton linker ezrin is necessary for osteosarcoma metastasis
Khanna, C., Wan, X., Bose, S., Cassaday, R., Olomu, O., Mendoza, A., Yeung, C., Gorlick, R., Hewitt, S. M., & Helman, L. J. (2004) · Nature Medicine · doi:10.1038/nm982 · Cited by 705 · see citing works
Self-citationReczek, D., Berryman, M. A., & Bretscher, A. P. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.1.169 · Cited by 571 · see citing works
Yu, Y., Khan, J. I., Khanna, C., Helman, L. J., Meltzer, P. S., & Merlino, G. T. (2004) · Nature Medicine · doi:10.1038/nm966 · Cited by 525 · see citing works
Self-citationOsteosarcoma: a review of diagnosis, management, and treatment strategies.
Geller, D. S., & Gorlick, R. G. (2010) · PubMed · Cited by 470 · see citing works
Cameron, M. D., Schmidt, E. E., Kerkvliet, N. I., Nadkarni, K. V., Morris, V. L., Groom, A. C., Chambers, A. F., & MacDonald, I. C. (2000) · PubMed · Cited by 400 · see citing works
Phosphoinositide binding and phosphorylation act sequentially in the activation mechanism of ezrin
Fiévet, B., Gautreau, A. M., Roy, C., Maestro, L. D., Mangeat, P. H., Louvard, D., & Arpin, M. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200307032 · Cited by 383 · see citing works
Structural basis of the membrane‐targeting and unmasking mechanisms of the radixin FERM domain
Hamada, K., Shimizu, T., Matsui, T., Tsukita, S., Tsukita, S., & Hakoshima, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.17.4449 · Cited by 377 · see citing works
Lamellipodia and filopodia in metastasis and invasion
Machesky, L. M. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.03.039 · Cited by 301 · see citing works
Metastasis-associated differences in gene expression in a murine model of osteosarcoma.
Khanna, C., Khan, J. I., Nguyen, P., Prehn, J., Caylor, J., Yeung, C. L., Trepel, J. B., Meltzer, P. S., & Helman, L. J. (2001) · PubMed · Cited by 282 · see citing works
Self-citationGautreau, A. M., Louvard, D., & Arpin, M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.1.193 · Cited by 280 · see citing works
Apoptosis: an early event in metastatic inefficiency.
Wong, C. W., Lee, A., Shientag, L., Yu, J. H., Dong, Y., Kao, G., Al‐Mehdi, A. B., Bernhard, E. J., & Muschel, R. J. (2001) · PubMed · Cited by 276 · see citing works
Oshiro, N., Fukata, Y., & Kaibuchi, K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.34663 · Cited by 226 · see citing works
Khanna, C., Prehn, J., Yeung, C., Caylor, J., Tsokos, M., & Helman, L. (2000) · Clinical & Experimental Metastasis · doi:10.1023/a:1006767007547 · Cited by 207 · see citing works
Self-citationThe ubiquitin ligase gp78 promotes sarcoma metastasis by targeting KAI1 for degradation
Tsai, Y. C., Mendoza, A., Mariano, J. M., Zhou, M., Kostova, Z., Chen, B., Veenstra, T., Hewitt, S. M., Helman, L. J., Khanna, C., et al. (2007) · Nature Medicine · doi:10.1038/nm1686 · Cited by 186 · see citing works
Self-citationPignochino, Y., Grignani, G., Cavalloni, G., Motta, M., Tapparo, M., Bruno, S., Bottos, A., Gammaitoni, L., Migliardi, G., Camussi, G., et al. (2009) · Molecular Cancer · doi:10.1186/1476-4598-8-118 · Cited by 180 · see citing works
Ezrin Regulates E-Cadherin-dependent Adherens Junction Assembly through Rac1 Activation
Pujuguet, P., Maestro, L. D., Gautreau, A. M., Louvard, D., & Arpin, M. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-07-0410 · Cited by 161 · see citing works
Chambers, A. F., Naumov, G. N., Vantyghem, S. A., & Tuck, A. B. (2000) · Breast Cancer Research · doi:10.1186/bcr86 · Cited by 137 · see citing works
The actin-cytoskeleton linker protein ezrin is regulated during osteosarcoma metastasis by PKC
Ren, L., Hong, S., Cassavaugh, J. M., Osborne, T. S., Chou, A. J., Kim, S. Y., Gorlick, R. G., Hewitt, S. M., & Khanna, C. (2008) · Oncogene · doi:10.1038/onc.2008.437 · Cited by 131 · see citing works
Self-citationMäkitie, T., Carpén, O., Vaheri, A. I., & Kivelä, T. (2001) · PubMed · Cited by 112 · see citing works
Weng, W., Åhlén, J., Åström, K., Lui, W., & Larsson, C. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-0548 · Cited by 111 · see citing works
Establishment and characterization of a new highly metastatic human osteosarcoma cell line
Su, Y., Luo, X., He, B., Wang, Y., Liang, C., Zuo, G., Liu, B., Bi, Y., Huang, J., Zhu, G., et al. (2009) · Clinical & Experimental Metastasis · doi:10.1007/s10585-009-9259-6 · Cited by 104 · see citing works
Ezrin in primary cutaneous melanoma
Ilmonen, S., Vaheri, A. I., Asko-Seljavaara, S. L., & Carpén, O. (2004) · Modern Pathology · doi:10.1038/modpathol.3800300 · Cited by 104 · see citing works
Rac1 Mediates Collapse of Microvilli on Chemokine-Activated T Lymphocytes
Nijhara, R., van Hennik, P. B., Gignac, M. L., Kruhlak, M. J., Hordijk, P. L., Delon, J., & Shaw, S. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.173.8.4985 · Cited by 95 · see citing works
Ezrin silencing by small hairpin RNA reverses metastatic behaviors of human breast cancer cells
Li, Q., Wu, M., Wang, H., Xu, G., Zhu, T., Zhang, Y., Liu, P., Song, A., Chen, G., Han, Z., et al. (2008) · Cancer Letters · doi:10.1016/j.canlet.2007.11.018 · Cited by 94 · see citing works
Modeling metastasis biology and therapy in real time in the mouse lung
Mendoza, A., Hong, S.-H., Osborne, T., Khan, M. A., Campbell, K., Briggs, J., Eleswarapu, A., Buquo, L., Ren, L., Hewitt, S. M., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci40252 · Cited by 92 · see citing works
Self-citationKhanna, C., Jaboin, J. J., Drakos, E., Tsokos, M., & Thiele, C. J. (2002) · PubMed · Cited by 79 · see citing works
Self-citationEstradiol-induced ezrin overexpression in ovarian cancer: a new signaling domain for estrogen
Song, J., Fadiel, A., Edusa, V., Chen, Z., So, J., Sakamoto, H., Fishman, D. A., & Naftolin, F. N. (2004) · Cancer Letters · doi:10.1016/j.canlet.2004.04.024 · Cited by 69 · see citing works
Madan, R., Brandwein‐Gensler, M. S., Schlecht, N. F., Elias, K., Gorbovitsky, E., Belbin, T. J., Mahmood, R., Breining, D., Qian, H., Childs, G. J., et al. (2006) · Head & Neck · doi:10.1002/hed.20435 · Cited by 60 · see citing works
Ezrin Directly Interacts with the α1b-Adrenergic Receptor and Plays a Role in Receptor Recycling
Stanasila, L., Abuin, L., Diviani, D., & Cotecchia, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m511989200 · Cited by 55 · see citing works
Phosphorylated ezrin is located in the nucleus of the osteosarcoma cell
Cristofano, C. D., Leopizzi, M., Miraglia, A., Sardella, B., Moretti, V., Ferrara, A., Petrozza, V., & Rocca, C. D. (2010) · Modern Pathology · doi:10.1038/modpathol.2010.77 · Cited by 51 · see citing works
Elliott, B. E., Qiao, H., Louvard, D., & Arpin, M. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20033 · Cited by 50 · see citing works
Interaction of actin with the enzymes of carbohydrate metabolism
POGLAZOV, B. F., & Livanova, N. B. (1986) · Advances in Enzyme Regulation · doi:10.1016/0065-2571(86)90020-8 · Cited by 37 · see citing works
Modeling metastasis in the mouse
McClatchey, A. I. (1999) · Oncogene · doi:10.1038/sj.onc.1203086 · Cited by 32 · see citing works
Preclinical studies of treosulfan demonstrate potent activity in Ewing’s sarcoma
Werner, S., Mendoza, A., Hilger, R. A., Erlacher, M., Reichardt, W., Lissat, A., Konanz, C., Uhl, M., Niemeyer, C. M., Khanna, C., et al. (2007) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-007-0566-9 · Cited by 27 · see citing works
Self-citationHong, S., Briggs, J., Newman, R. J., Hoffman, K. E., Mendoza, A., LeRoith, D., Helman, L. J., Yakar, S., & Khanna, C. (2008) · International Journal of Cancer · doi:10.1002/ijc.24169 · Cited by 18 · see citing works
Self-citationActin and coordination of metabolic processes.
Bf, P. (1983) · PubMed · Cited by 18 · see citing works
Moulding the shape of a metastatic cell
Fais, S. (2010) · Leukemia Research · doi:10.1016/j.leukres.2010.02.006 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Beird, H. C., Bielack, S. S., Flanagan, A. M., Gill, J., Heymann, D., Janeway, K. A., Livingston, J. A., Roberts, R. D., Strauss, S. J., & Gorlick, R. (2022) · Nature Reviews Disease Primers · doi:10.1038/s41572-022-00409-y · Cited by 660 · see citing works
Simpson, S., Dunning, M., de Brot, S., Grau‐Roma, L., Mongan, N. P., & Rutland, C. S. (2017) · Acta veterinaria Scandinavica · doi:10.1186/s13028-017-0341-9 · Cited by 294 · see citing works
Invasion and metastasis in cancer: molecular insights and therapeutic targets
Li, Y., Liu, F., Cai, Q., Deng, L., Ouyang, Q., Zhang, X. H.-F., & Zheng, J. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-025-02148-4 · Cited by 278 · see citing works
Sheng, G., Gao, Y., Yong, Y., & Wu, H. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.780264 · Cited by 202 · see citing works
Cytoskeletal Remodeling in Cancer
Aseervatham, J. (2020) · Biology · doi:10.3390/biology9110385 · Cited by 170 · see citing works
Glutaminase-1 (GLS1) inhibition limits metastatic progression in osteosarcoma
Ren, L., Ruiz‐Rodado, V., Dowdy, T., Huang, S., Issaq, S. H., Beck, J. A., Wang, H., Hoang, C. D., Lita, A., Larion, M., et al. (2020) · Cancer & Metabolism · doi:10.1186/s40170-020-0209-8 · Cited by 102 · see citing works
Self-citationTegavivint and the β-Catenin/ALDH Axis in Chemotherapy-Resistant and Metastatic Osteosarcoma
Nomura, M., Rainusso, N., Lee, Y.-C., Dawson, B., Coarfa, C., Han, R., Larson, J. L., Shuck, R., Kurenbekova, L., & Yustein, J. T. (2019) · JNCI: Journal of the National Cancer Institute · doi:10.1093/jnci/djz026 · Cited by 99 · see citing works
Murad, N., Kokkinaki, M., Gunawardena, N., Gunawan, M. S., Hathout, Y., Janczura, K. J., Theos, A. C., & Golestaneh, N. (2014) · The FEBS Journal · doi:10.1111/febs.13066 · Cited by 73 · see citing works
Wu, V., Mickens, J., & Uskoković, V. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.7b08108 · Cited by 63 · see citing works
Adada, M. M., Canals, D., Hannun, Y. A., & Obeid, L. M. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2013.07.002 · Cited by 55 · see citing works
Role of Ezrin in Osteosarcoma Metastasis
Ren, L., & Khanna, C. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-04843-7_10 · Cited by 52 · see citing works
Self-citationEzrin Inhibition Up-regulates Stress Response Gene Expression
Çelik, H., Bulut, G., Han, J. J., Graham, G. T., Minas, T. Z., Conn, E. J., Hong, S.-H., Pauly, G. T., Hayran, M., Li, X., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.718189 · Cited by 52 · see citing works
Self-citationMu, X., Isaac, C. E., Schott, T., Huard, J., & Weiss, K. R. (2013) · Sarcoma · doi:10.1155/2013/480713 · Cited by 50 · see citing works
Lizardo, M. M., Morrow, J. J., Miller, T. E., Hong, E. S., Ren, L., Mendoza, A., Halsey, C. H., Scacheri, P. C., Helman, L. J., & Khanna, C. (2016) · Neoplasia · doi:10.1016/j.neo.2016.09.001 · Cited by 50 · see citing works
Self-citationMetabolomics uncovers a link between inositol metabolism and osteosarcoma metastasis
Ren, L., Hong, E. S., Mendoza, A., Issaq, S. H., Hoang, C. T., Lizardo, M. M., LeBlanc, A. K., & Khanna, C. (2017) · Oncotarget · doi:10.18632/oncotarget.15872 · Cited by 46 · see citing works
Self-citationAntelmi, E., Cardone, R. A., Greco, M. R., Rubino, R., Sole, F. D., Martino, N. A., Casavola, V., Carcangiu, M.-L., Moro, L., & Reshkin, S. J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075113 · Cited by 42 · see citing works
Mu, Y., Zhang, H., Che, L., & Li, K. (2013) · Medical Oncology · doi:10.1007/s12032-013-0821-3 · Cited by 39 · see citing works
Scaffolding during the cell cycle by A-kinase anchoring proteins
Han, B., Poppinga, W. J., & Schmidt, M. (2015) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-015-1718-0 · Cited by 29 · see citing works
Wang, A., Lu, C., Ning, Z., Gao, W., Xie, Y., Zhang, N., Liang, J., Abbasi, F. S., Yan, Q., & Liu, J. (2017) · Oncotarget · doi:10.18632/oncotarget.16001 · Cited by 30 · see citing works
Protein phosphatase 2A Cα regulates proliferation, migration, and metastasis of osteosarcoma cells
Yang, D., Okamura, H., Morimoto, H., Teramachi, J., & Haneji, T. (2016) · Laboratory Investigation · doi:10.1038/labinvest.2016.82 · Cited by 29 · see citing works
Re-calculating! Navigating through the osteosarcoma treatment roadblock
McGuire, J., Utset‐Ward, T. J., Reed, D. R., & Lynch, C. C. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.12.004 · Cited by 26 · see citing works
Role of Acid Sphingomyelinase-Induced Signaling in Melanoma Cells for Hematogenous Tumor Metastasis
Carpinteiro, A., Beckmann, N., Seitz, A. P., Hessler, G., Wilker, B., Soddemann, M., Helfrich, I., Edelmann, B., Gulbins, E., & Becker, K. A. (2016) · Cellular Physiology and Biochemistry · doi:10.1159/000438604 · Cited by 23 · see citing works
Silver, K. I., Patkar, S., Mazcko, C. N., Berger, E. P., Beck, J. A., & LeBlanc, A. K. (2023) · Veterinary and Comparative Oncology · doi:10.1111/vco.12927 · Cited by 22 · see citing works
Clinical implications of Ezrin and CD44 co-expression in breast cancer
Li-fang, M., & Jiang, T. (2013) · Oncology Reports · doi:10.3892/or.2013.2641 · Cited by 22 · see citing works
Li, T., Deng, L., He, X., Jiang, G., Hu, F., Ye, S., You, Y., Duanmu, J., Dai, H., Huang, G., et al. (2019) · Cancer Management and Research · doi:10.2147/cmar.s219689 · Cited by 22 · see citing works
Sun, W. Y., Ma, X., Shen, J., Yin, F., Wang, C., & Cai, Z. (2016) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2016.2657 · Cited by 21 · see citing works
ERM Proteins Play Distinct Roles in Cell Invasion by Extracellular Amastigotes of Trypanosoma cruzi
Ferreira, É. R., Bonfim‐Melo, A., Cordero, E. M., & Mortara, R. A. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.02230 · Cited by 21 · see citing works
Fritsche‐Guenther, R., Gloaguen, Y., Kirchner, M., Mertins, P., Tunn, P., & Kirwan, J. (2020) · Cancers · doi:10.3390/cancers12061371 · Cited by 20 · see citing works
Cytoskeletal and Cytoskeleton-Associated Proteins: Key Regulators of Cancer Stem Cell Properties
Li, Y., Wang, D., Ge, H., Güngör, C., Gong, X., & Chen, Y. (2022) · Pharmaceuticals · doi:10.3390/ph15111369 · Cited by 17 · see citing works
Whittle, S. B., Offer, K., Roberts, R. D., LeBlanc, A. K., London, C. A., Majzner, R. G., Huang, A. Y.-C., Houghton, P. J., Sweet-Cordero, A., Grohar, P. J., et al. (2021) · Pediatric Blood & Cancer · doi:10.1002/pbc.29188 · Cited by 18 · see citing works
Discovery of Biomarkers for Osteosarcoma by Proteomics Approaches
Suehara, Y., Kubota, D., Kikuta, K., Kaneko, K., Kawai, A., & Kondo, T. (2012) · Sarcoma · doi:10.1155/2012/425636 · Cited by 16 · see citing works
Proudfit, A. M., Bhunia, N., Pore, D., Parker, Y., Lindner, D. J., & Gupta, N. (2020) · Sarcoma · doi:10.1155/2020/9010496 · Cited by 16 · see citing works
Inhibition of osteosarcoma metastasis in vivo by targeted downregulation of MMP1 and MMP9
Doppelt‐Flikshtain, O., Asbi, T., Younis, A., Ginesin, O., Cohen, Z., Tamari, T., Berg, T., Yanovich, C., Aran, D., Zohar, Y., et al. (2024) · Matrix Biology · doi:10.1016/j.matbio.2024.09.002 · Cited by 15 · see citing works
Bidirectional Tumor-Promoting Activities of Macrophage Ezrin
Khan, K., Long, B., Deshpande, G. M., & Fox, P. L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207716 · Cited by 14 · see citing works
Insights in Osteosarcoma by Proton Nuclear Magnetic Resonance Serum Metabonomics
Quintero, M., Costa, T. B. B. C., Martins, L. G., da Costa, S. S., Lengert, A. V. H., Boldrini, É., da Silva, S. R. M., Lopes, L. F., Vidal, D. O., Krepischi, A. C. V., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.506959 · Cited by 14 · see citing works
Argyle, D. J., & Khanna, C. (2012) · Elsevier eBooks · doi:10.1016/b978-1-4377-2362-5.00002-5 · Cited by 14 · see citing works
Self-citationMilia-Argeiti, E., Mourah, S., Vallée, B., Huet, E., Karamanos, N. K., Theocharis, A. D., & Menashi, S. (2014) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2014.02.026 · Cited by 14 · see citing works
Xiao, Y., Sun, M., Zhan, Z., Ye, Y., Huang, M., Zou, Y., Liang, L., Yang, X., & Xu, H. (2014) · Lara D. Veeken · doi:10.1093/rheumatology/keu013 · Cited by 13 · see citing works
Immunohistochemical Characterisation of GLUT1, MMP3 and NRF2 in Osteosarcoma
Rutland, C. S., Cockcroft, J. M., Lothion‐Roy, J. H., Harris, A. E., Jeyapalan, J. N., Simpson, S., Alibhai, A. A., Bailey, C., Ballard-Reisch, A. C., Rizvanov, A. A., et al. (2021) · Frontiers in Veterinary Science · doi:10.3389/fvets.2021.704598 · Cited by 12 · see citing works
Pancreatic Ductal Adenocarcinoma Cortical Mechanics and Clinical Implications
Angstadt, S. M., Zhu, Q., Jaffee, E. M., Robinson, D. N., & Anders, R. A. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.809179 · Cited by 14 · see citing works
Zhang, X., Xie, J., Liao, L., Long, L., Xie, Y., Li, E., & Xu, L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0124680 · Cited by 8 · see citing works
Jin, Q., Liu, G., Domeier, P. P., Ding, W., & Mulder, K. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066439 · Cited by 8 · see citing works
Yao, Q., Zhao, H., & Xie, B. (2015) · Orthopaedic Surgery · doi:10.1111/os.12186 · Cited by 7 · see citing works
Immunohistochemical assessment of ezrin and moesin in colorectal carcinoma
Abdou, A. G., Sakr, S. A., El-Wahed, M. M. A., & Eladly, E. K. (2016) · Ultrastructural Pathology · doi:10.3109/01913123.2016.1155683 · Cited by 5 · see citing works
Post-translational modifications of ezrin: a crucial regulator for diseases
Li, Y. E., Yuan, H.-K., & Yin, L.-M. (2025) · Amino Acids · doi:10.1007/s00726-025-03472-3 · Cited by 2 · see citing works
Argyle, D. J., Khanna, C., & Giancristofaro, N. (2019) · Elsevier eBooks · doi:10.1016/b978-0-323-59496-7.00002-5 · Cited by 2 · see citing works
Self-citationDeniz, E., Tiwari, P., Tiwari, P. B., Glasgow, E. F., Harris, B. T., Tiwari, A., Hou, C., Ma, J. R., Toretsky, J. A., & Üren, A. (2026) · Science Signaling · doi:10.1126/scisignal.ady8367 · Cited by 1 · see citing works
Xie, C. L. J. (2014) · Journal of Cancer Science & Therapy · doi:10.4172/1948-5956.1000287 · Cited by 1 · see citing works
Gene and proteomic profiling of osteosarcoma
Patiño‐García, A., & Lecanda, F. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-416721-6.00020-0
Genomic and proteomic profiling of osteosarcoma
Patiño‐García, A., & Lecanda, F. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821666-8.00054-2
- Authors
- Ren, L., Hong, S.-H., Chen, Q.-R., Briggs, J., Cassavaugh, J., Srinivasan, S., Lizardo, M. M., Mendoza, A., Xia, A. Y., Avadhani, N., Khan, J., & Khanna, C.
- Affiliations
- National Institute of Allergy and Infectious Diseases (US)
- Authors' Affiliations: 1Tumor and Metastasis Biology Section, 2Oncogenomics Section, Pediatric Oncology Branch, Center for Cancer Research, National Cancer Institute; 3Office of Biomedical Informatics, Division of Allergy, Immunology and Transplantation, National Institute of Allergy and Infectious Diseases, Bethesda, Maryland; and 4Department of Animal Biology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, Pennsylvania
- Corresponding author
- Khanna, Chand
- ORCID
- Venue
- Cancer Research
- Published
- 2012-02-14
- Volume
- 72
- Issue
- 4
- Pages
- 1001-1012
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- PMC
- PMC3867810
- OpenAlex
- W1974284378
- Cited by
- 50
- References
- 45
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 3 · 2021: 4 · 2020: 6 · 2019: 3 · 2017: 5 · 2016: 7 · 2015: 3 · 2014: 6 · 2013: 6 · 2012: 2
- FWCI
- 2.20
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Cancer Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Cancer Institute (R01CA022762, R01 CA-22762)
- Topics
- Health Sciences › Medicine › Oncology › Cancer Cells and Metastasis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mechanisms of cancer metastasis
- Keywords
- ezrin, phosphorylation, osteosarcoma, metastasis, actin cytoskeleton, plasma membrane, cellular metabolism, lactic acid production, oxygen consumption, apoptosis, lung metastasis, carbohydrate metabolism, amino acid metabolism
- MeSH terms
- Ezrin, Animals, Cytoskeletal Proteins, Humans, Lung Neoplasms, Mutation, Phenotype, Phosphorylation, Protein Conformation, Osteosarcoma, Gene Expression, Microscopy, Video, Cell Line, Tumor, Mice
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review