The DOI matches its Crossref record; 52 of the 53 references it cites were found in a registry or an index.
CD151 Accelerates Breast Cancer by Regulating α6 Integrin Function, Signaling, and Molecular Organization
Open accessPublished version of a preprint
Abstract
CD151, a master regulator of laminin-binding integrins (alpha(6)beta(4), alpha(6)beta(1), and alpha(3)beta(1)), assembles these integrins into complexes called tetraspanin-enriched microdomains. CD151 protein expression is elevated in 31% of human breast cancers and is even more elevated in high-grade (40%) and estrogen receptor-negative (45%) subtypes. The latter includes triple-negative (estrogen receptor, progesterone receptor, and HER2 negative) basal-like tumors. CD151 ablation markedly reduced basal-like mammary cell migration, invasion, spreading, and signaling (through FAK, Rac1, and lck) while disrupting epidermal growth factor receptor (EGFR)-alpha(6) integrin collaboration. Underlying these defects, CD151 ablation redistributed alpha(6)beta(4) integrins subcellularly and severed molecular links between integrins and tetraspanin-enriched microdomains. In a prototypical basal-like mammary tumor line, CD151 ablation notably delayed tumor progression in ectopic and orthotopic xenograft models. These results (a) establish that CD151-alpha(6) integrin complexes play a functional role in basal-like mammary tumor progression; (b) emphasize that alpha(6) integrins function via CD151 linkage in the context of tetraspanin-enriched microdomains; and (c) point to potential relevance of CD151 as a high-priority therapeutic target, with relative selectivity (compared with laminin-binding integrins) for pathologic rather than normal physiology.
Overview
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
Verification
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 source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“ITGB1 and CD151 are known to be pro-tumorigenic by enhancing cell migration and stromal invasion (Reuter et al., 2009, White et al., 2004, Yang et al., 2008, Zijlstra et al., 2008).”
From Multimodal Analysis of Composition and Spatial Architecture in Human Squamous Cell Carcinoma (2020) · cites this paper as Yang et al., 2008
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Molecular portraits of human breast tumours
Perou, C., Sørlie, T., Eisen, M., van de Rijn, M., Jeffrey, S., Rees, C. A., Pollack, J., Ross, D., Johnsen, H., Akslen, L., et al. (2000) · Nature · doi:10.1038/35021093 · Cited by 16,551
A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes
Neve, R. M., Chin, K., Fridlyand, J., Yeh, J., Baehner, F. L., Fevr, T., Clark, L., Bayani, N., Coppé, J., Tong, F. K., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.10.008 · Cited by 3,224
Focal adhesion kinase: in command and control of cell motility
Mitra, S. K., Hanson, D. A., & Schlaepfer, D. D. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1549 · Cited by 2,657
Tetraspanin functions and associated microdomains
Hemler, M. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1736 · Cited by 1,355 · cited 1×
“CD151 may link laminin-binding integrins to other proteins within the plasma membrane (38, 39).”
BackgroundSelf-citationHemler, M. E. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111301.153609 · Cited by 831
Self-citationActivation of Phosphoinositide 3-OH Kinase by the α6β4 Integrin Promotes Carcinoma Invasion
Shaw, L. M., Rabinovitz, I., Wang, H. H.-F., Toker, A., & Mercurio, A. M. (1997) · Cell · doi:10.1016/s0092-8674(00)80486-9 · Cited by 613
Complexes of tetraspanins with integrins: more than meets the eye
Berditchevski, F. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.23.4143 · Cited by 597
Genetic programs of epithelial cell plasticity directed by transforming growth factor-β
Zavadil, J., Bitzer, M., Liang, D., Yang, Y.-C., Massimi, A. B., Kneitz, S., Piek, E., & Böttinger, E. P. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.111614398 · Cited by 534
Control of motile and invasive cell phenotypes by focal adhesion kinase
Schlaepfer, D. D., Mitra, S. K., & Ilić, D. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.04.008 · Cited by 475
β4 Integrin Amplifies ErbB2 Signaling to Promote Mammary Tumorigenesis
Guo, W., Pylayeva, Y., Pepe, A., Yoshioka, T., Muller, W. J., Inghirami, G., & Giancotti, F. G. (2006) · Cell · doi:10.1016/j.cell.2006.05.047 · Cited by 466
EGF-R signaling through Fyn kinase disrupts the function of integrin α6β4 at hemidesmosomes
Mariotti, A., Kedeshian, P. A., Dans, M. J., Curatola, A. M., Gagnoux-Palacios, L., & Giancotti, F. G. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200105017 · Cited by 304
Yáñez‐Mó, M., Alfranca, A., Cabañas, C., Marazuela, M., Tejedor, R., Ursa, M. A., Ashman, L. K., Landázuri, M. O., & Sánchez‐Madrid, F. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.3.791 · Cited by 271
Crew, V. K., Burton, N., Kagan, A., Green, C. A., Levene, C., Flinter, F. A., Brady, R. L., Daniels, G. L., & Anstee, D. J. (2004) · Blood · doi:10.1182/blood-2004-04-1512 · Cited by 263
Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1
Nydegger, S., Khurana, S., Krementsov, D. N., Foti, M., & Thali, M. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200508165 · Cited by 257
Rabinovitz, I., & Mercurio, A. M. (1997) · The Journal of Cell Biology · doi:10.1083/jcb.139.7.1873 · Cited by 243
Yang, X. H., Claas, C., Kraeft, S., Chen, L. B., Wang, Z., Kreidberg, J. A., & Hemler, M. E. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-05-0275 · Cited by 230
Self-citationKidney failure in mice lacking the tetraspanin CD151
Sachs, N., Kreft, M., Weerman, M. A. V. D. B., Beynon, A. J., Peters, T. A., Weening, J. J., & Sonnenberg, A. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200603073 · Cited by 229
Yoon, S.-O., Shin, S., & Mercurio, A. M. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4122 · Cited by 226
Palmitoylation supports assembly and function of integrin–tetraspanin complexes
Yang, X. H., Kovalenko, O. V., Tang, W., Claas, C., Stipp, C. S., & Hemler, M. E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200404100 · Cited by 213
Self-citationα6β4 and α6β1 Integrins Associate with ErbB-2 in Human Carcinoma Cell Lines
Falcioni, R., Antonini, A., Nisticò, P., Stefano, S. D., Crescenzi, M., Natali, P. G., & Sacchi, A. (1997) · Experimental Cell Research · doi:10.1006/excr.1997.3695 · Cited by 202
Friedrichs, K., Ruiz, P., Franke, F. A., Gille, I., Terpe, H.-J., & Imhof, B. A. (1995) · PubMed · Cited by 195
Zahir, N., Lakins, J. N., Russell, A. J., Ming, W., Chatterjee, C., Rozenberg, G. I., Marinkovich, M. P., & Weaver, V. M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200302023 · Cited by 195
Sincock, P. M., Fitter, S., Parton, R. G., Berndt, M. C., Gamble, J. R., & Ashman, L. K. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.6.833 · Cited by 177
Characterization of Mice Lacking the Tetraspanin Superfamily Member CD151
Wright, M. D., Geary, S. M., Fitter, S., Moseley, G. W., Lau, L.-M., Sheng, K., Apostolopoulos, V., Stanley, E. G., Jackson, D. E., & Ashman, L. K. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.13.5978-5988.2004 · Cited by 173
Deletion of tetraspanin Cd151 results in decreased pathologic angiogenesis in vivo and in vitro
Takeda, Y., Kazarov, A. R., Butterfield, C., Hopkins, B. D., Benjamin, L. E., Kaipainen, A., & Hemler, M. E. (2006) · Blood · doi:10.1182/blood-2006-08-041970 · Cited by 167
Self-citationTetraspanin CD151 regulates α6β1 integrin adhesion strengthening
Lammerding, J., Kazarov, A. R., Huang, H., Lee, R. T., & Hemler, M. E. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1337546100 · Cited by 160
Self-citationTesta, J. E., Brooks, P. C., Lin, J., & Quigley, J. P. (1999) · PubMed · Cited by 156
Potentiation of the ligand-binding activity of integrin α3β1 via association with tetraspanin CD151
Nishiuchi, R., Sanzen, N., Nada, S., Sumida, Y., Wada, Y., Okada, M., Takagi, J., Hasegawa, H., & Sekiguchi, K. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409493102 · Cited by 153
Tetraspanin microdomains in immune cell signalling and malignant disease
Wright, M. D., Moseley, G. W., & van Spriel, A. B. (2004) · Tissue Antigens · doi:10.1111/j.1399-0039.2004.00321.x · Cited by 149
Akt/PKB Signaling in Cancer: A Function in Cell Motility and Invasion
Yoeli-Lerner, M., & Toker, A. (2006) · Cell Cycle · doi:10.4161/cc.5.6.2561 · Cited by 149
Deconstructing the molecular portrait of basal-like breast cancer
Yehiely, F., Moyano, J. V., Evans, J. R., Nielsen, T. O., & Cryns, V. L. (2006) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2006.09.004 · Cited by 144
Winterwood, N. E., Varzavand, A., Meland, M. N., Ashman, L. K., & Stipp, C. S. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-11-1042 · Cited by 138
Tetraspanin CD82 regulates compartmentalisation and ligand-induced dimerization of EGFR
Odintsova, E., Voortman, J., Gilbert, E., & Berditchevski, F. (2003) · Journal of Cell Science · doi:10.1242/jcs.00793 · Cited by 132
Clinical significance of CD151 gene expression in non-small cell lung cancer.
Tokuhara, T., Hasegawa, H., Hattori, N., Ishida, H., Taki, T., Tachibana, S., Sasaki, S., & Miyake, M. (2001) · PubMed · Cited by 121
Lau, L.-M., Wee, J. L. K., Wright, M. D., Moseley, G. W., Hogarth, P. M., Ashman, L. K., & Jackson, D. E. (2004) · Blood · doi:10.1182/blood-2003-12-4430 · Cited by 116
Ang, J., Lijovic, M., Ashman, L. K., Kan, K., & Frauman, A. G. (2004) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.1717.13.11 · Cited by 114
Fitter, S., Sincock, P. M., Jolliffe, C. N., & Ashman, L. K. (1999) · PubMed Central · Cited by 107
Kovalenko, O. V., Yang, X. H., & Hemler, M. E. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700183-mcp200 · Cited by 103
Self-citationRabinovitz, I., Tsomo, L., & Mercurio, A. M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4351-4360.2004 · Cited by 101
Fitter, S., Sincock, P. M., Jolliffe, C. N., & Ashman, L. K. (1999) · Biochemical Journal · doi:10.1042/bj3380061 · Cited by 101
Rho family proteins and cell migration.
Ridley, A. J., Allen, W., Peppelenbosch, M. P., & Jones, G. E. (1999) · PubMed · Cited by 91
Wound Healing Is Defective in Mice Lacking Tetraspanin CD151
Cowin, A. J., Adams, D. H., Geary, S. M., Wright, M. D., Jones, J., & Ashman, L. K. (2006) · Journal of Investigative Dermatology · doi:10.1038/sj.jid.5700142 · Cited by 91
Diaz, L. K., Cristofanilli, M., Zhou, X., Welch, K., Smith, T. L., Yang, Y., Sneige, N., Şahin, A. A., & Gilcrease, M. Z. (2005) · Modern Pathology · doi:10.1038/modpathol.3800411 · Cited by 82
Chakraborty, G., Rangaswami, H., Jain, S., & Kundu, G. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512546200 · Cited by 81
McGowan, K. A., & Marinkovich, M. P. (2000) · Microscopy Research and Technique · doi:10.1002/1097-0029(20001101)51:3 · Cited by 76
Contributions of the α6 Integrins to Breast Carcinoma Survival and Progression
Chung, J., & Mercurio, A. M. (2004) · Molecules and Cells · doi:10.1016/s1016-8478(23)13027-5 · Cited by 51
Contributions of the alpha6 integrins to breast carcinoma survival and progression.
Chung, J., & Mercurio, A. M. (2004) · PubMed · Cited by 49
Role of Tetraspanins CD9 and CD151 in Primary Melanocyte Motility
García-López, M. Á., Barreiro, O., García‐Diez, A., Sánchez‐Madrid, F., & Fernández‐Peñas, P. (2005) · Journal of Investigative Dermatology · doi:10.1111/j.0022-202x.2005.23882.x · Cited by 49
Targeting the AIB1 Oncogene through Mammalian Target of Rapamycin Inhibition in the Mammary Gland
Torres‐Arzayus, M. I., Yuan, J., DellaGatta, J. L., Lane, H. A., Kung, A. L., & Brown, M. A. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-2316 · Cited by 49
Self-citationZheng, Z., & Liu, Z. (2006) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.09.001 · Cited by 47
Ogata, H., Sato, H., Takatsuka, J., & Luca, L. M. D. (2001) · Cancer Letters · doi:10.1016/s0304-3835(01)00648-6 · Cited by 43
p56lck CONTROLS PHOSPHORYLATION OF FILAMIN (ABP‐280) AND REGULATES FOCAL ADHESION KINASE (pp125FAK)
Goldmann, W. H. (2002) · Cell Biology International · doi:10.1006/cbir.2002.0900 · Cited by 14
Cited by
Sorted by citations
Matrix Crosslinking Forces Tumor Progression by Enhancing Integrin Signaling
Levental, K. R., Yu, H., Kass, L., Lakins, J. N., Egeblad, M., Erler, J. T., Fong, S. F. T., Csiszar, K., Giaccia, A., Weninger, W., et al. (2009) · Cell · doi:10.1016/j.cell.2009.10.027 · Cited by 4,101
Multimodal Analysis of Composition and Spatial Architecture in Human Squamous Cell Carcinoma
Ji, A. L., Rubin, A. J., Thrane, K., Jiang, S., Reynolds, D. L., Meyers, R. M., Guo, M. G., George, B. M., Mollbrink, A., Bergenstråhle, J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.05.039 · Cited by 1,117
“ITGB1 andCD151 are known to be pro-tumorigenic by enhancing cell migration and stromal invasion (Reuter et al., 2009; White et al., 2004; Yang et al., 2008; Zijlstra et al., 2008).”
BackgroundCharrin, S., Jouannet, S., Boucheix, C., & Rubinstein, E. (2014) · Journal of Cell Science · doi:10.1242/jcs.154906 · Cited by 481
Lateral organization of membrane proteins: tetraspanins spin their web
Charrin, S., Naour, F. L., Silvie, O., Milhiet, P., Boucheix, C., & Rubinstein, E. (2009) · Biochemical Journal · doi:10.1042/bj20082422 · Cited by 440
Tetraspanin proteins promote multiple cancer stages
Hemler, M. E. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3640 · Cited by 403
Self-citation
Metadata
- Authors
- Yang, X. H., Richardson, A. L., Torres-Arzayus, M. I., Zhou, P., Sharma, C., Kazarov, A. R., Andzelm, M. M., Strominger, J. L., Brown, M., & Hemler, M. E.
- Affiliations
- Harvard University (US)
- Brigham and Women's Hospital (US)
- 2Medical Oncology, and
- ORCID
- Venue
- Cancer Research
- Published
- 2008-05-01
- Volume
- 68
- Issue
- 9
- Pages
- 3204-3213
- ISSN
- 0008-5472 (ISSN-L)
- 1538-7445
- PMC
- PMC4764302
- OpenAlex
- W2102040455
- Cited by
- 183
- References
- 53
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 13 · 2020: 8 · 2019: 7 · 2018: 7 · 2017: 9 · 2016: 8 · 2015: 14 · 2014: 7 · 2013: 21 · 2012: 22
- FWCI
- 11.91
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cancer Research (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Breast Cancer Research Foundation
- National Institutes of Health
- National Cancer Institute (CA-42368, R01CA042368)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
- Keywords
- CD151, CD49f, breast cancer, basal-like breast cancer, triple-negative breast cancer, tetraspanin-enriched microdomains, laminin-binding integrins, integrin signaling, tumor progression, EGFR, focal adhesion kinase, Rac1, Lck, tumor cell migration and invasion, therapeutic target
- MeSH terms
- Animals, Breast Neoplasms, Cell Adhesion, Cell Movement, Epidermal Growth Factor, Humans, Mice, Nude, Neoplasm Invasiveness, Protein Binding, Tissue Distribution, Transplantation, Heterologous, Tumor Cells, Cultured, Signal Transduction, Antigens, CD, Gene Expression Regulation, Neoplastic, Disease Progression, Integrin alpha6, Mammary Glands, Human, Mice, Tetraspanin 24
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