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Tetraspanin functions and associated microdomains
Abstract
Cell-surface proteins of the tetraspanin family are small, and often hidden by a canopy of tall glycoprotein neighbours in the cell membrane. Consequently, tetraspanins have been understudied and underappreciated, despite their presence on nearly all cell and tissue types. Important new genetic evidence has now emerged, and is bolstered by new insights into the cell biology, signalling and biochemistry of tetraspanins. These new findings provide a framework for better understanding of these mysterious molecules in the regulation of cellular processes, from signalling to motility.
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“Further analysis of the Tregs subsets in the old cells revealed that CD81 [a member of the tetraspanin family (40)] is a specific marker that differentiates between rTregs and aTregs.”
From Aging promotes reorganization of the CD4 T cell landscape toward extreme regulatory and effector phenotypes (2019) · cites this paper as [40]
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Cites
Functions of lipid rafts in biological membranes.
Brown, D. A., & London, E. (1998) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.14.1.111 · Cited by 3,027
Protein kinase Cα activates RAF-1 by direct phosphorylation
Kölch, W., Heidecker, G., Kochs, G., Hummel, R., Vahidi, H., Mischak, H., Finkenzeller, G., Marmé, D., & Rapp, U. R. (1993) · Nature · doi:10.1038/364249a0 · Cited by 1,278
Escola, J.-M., Kleijmeer, M. J., Stoorvogel, W., Griffith, J. M., Yoshie, O., & Geuze, H. J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.32.20121 · Cited by 1,228
The tetraspanin superfamily: molecular facilitators
Maecker, H. T., Todd, S. C., & Levy, S. (1997) · The FASEB Journal · doi:10.1096/fasebj.11.6.9194523 · Cited by 931
Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
Foster, L. J., de Hoog, C. L., & Mann, M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0631608100 · Cited by 834
Hemler, M. E. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111301.153609 · Cited by 831
Self-citationDigenic Retinitis Pigmentosa Due to Mutations at the Unlinked Peripherin/ RDS and ROM1 Loci
Kajiwara, K., Berson, E. L., & Dryja, T. P. (1994) · Science · doi:10.1126/science.8202715 · Cited by 783
KAI1 , a Metastasis Suppressor Gene for Prostate Cancer on Human Chromosome 11p11.2
Dong, J., Lamb, P. W., Rinker-Schaeffer, C. W., Vukanovic, J., Ichikawa, T., Isaacs, J. T., & Barrett, J. C. (1995) · Science · doi:10.1126/science.7754374 · Cited by 758
Alpha 3 beta 1 integrin has a crucial role in kidney and lung organogenesis
Kreidberg, J. A., Donovan, M. J., Goldstein, S. L., Rennke, H. G., Shepherd, K. E., Jones, R. C., & Jaenisch, R. (1996) · Development · doi:10.1242/dev.122.11.3537 · Cited by 731
PDZ Domains: Structural Modules for Protein Complex Assembly
Hung, A. Y., & Sheng, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.r100065200 · Cited by 699
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Gangliosides play an important role in the organization of CD82-enriched microdomains
Odintsova, E., Butters, T. D., Monti, E., Sprong, H., Gerrit van, M. E. E. R., & Berditchevski, F. (2006) · Biochemical Journal · doi:10.1042/bj20060259 · Cited by 94
“Tetraspanins interact with each other, thereby providing a structural platform for the recruitment of other transmembrane and cytoplasmic proteins into TERM [8,11,12].”
Weng, J., Krementsov, D. N., Khurana, S., Roy, N. H., & Thali, M. (2009) · Journal of Virology · doi:10.1128/jvi.00163-09 · Cited by 89
The Tetraspanin Protein CD37 Regulates IgA Responses and Anti-Fungal Immunity
van Spriel, A. B., Sofi, M., Gartlan, K. H., van der Schaaf, A., Verschueren, I., Torensma, R., Raymakers, R. A. P., Loveland, B. E., Netea, M. G., Adema, G. J., et al. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000338 · Cited by 95
“Tetraspanins, or transmembrane-four superfamily proteins, are implicated in organizing (immuno)-receptors, integrins, and signaling molecules into functional membrane complexes (tetraspanin microdomains) [9–12].”
BackgroundPancreatic cancer stem cell markers and exosomes - the incentive push
Heiler, S., Wang, Z., & Zöller, M. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i26.5971 · Cited by 91
Function of the tetraspanin molecule CD81 in B and T cells
Levy, S. (2014) · Immunologic Research · doi:10.1007/s12026-014-8490-7 · Cited by 93
“Tetraspanins associate with each other in subcellular membrane microdomains, which are dynamic membrane entities that act as signaling platforms [6–8].”
BackgroundEvans, J. P. (2011) · Annual Review of Physiology · doi:10.1146/annurev-physiol-020911-153339 · Cited by 92
The Many and Varied Roles of Tetraspanins in Immune Cell Recruitment and Migration
Yeung, L., Hickey, M. J., & Wright, M. D. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01644 · Cited by 92
Redox Signaling of NADPH Oxidases Regulates Oxidative Stress Responses, Immunity and Aging
Ewald, C. Y. (2018) · Antioxidants · doi:10.3390/antiox7100130 · Cited by 88
“Because mammalian tetraspanin is found enriched in membrane microdomains, which are important for cell-cell communication [41-43], it is tempting”
BackgroundExosome: A New Player in Translational Nanomedicine
Aheget, H., Tristán‐Manzano, M., Mazini, L., Cortijo-Gutierréz, M., Galindo‐Moreno, P., Herrera, C., Martı́n, F., Marchal, J. A., & Benabdellah, K. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9082380 · Cited by 93
“These protein superfamilies, together with a wide variety of transmembrane and cytosolic proteins, mediate the organization of tetraspanin-enriched microdomains (TEMS) in the plasma membrane and the biogenesis of exosomes [42,43].”
Choi, H., & Moon, A. (2018) · Archives of Pharmacal Research · doi:10.1007/s12272-018-1051-1 · Cited by 93
“Tetraspanins, cell surface proteins, are associated with adhesion receptors in the integrin family (Hemler 2005).”
BackgroundMesenchymal stem cell–derived small extracellular vesicles and bone regeneration
Wang, X., & Thomsen, P. (2020) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.13478 · Cited by 91
The role of tetraspanins in the pathogenesis of infectious diseases
van Spriel, A. B., & Figdor, C. G. (2009) · Microbes and Infection · doi:10.1016/j.micinf.2009.11.001 · Cited by 98
“Important progress in our understanding of tetraspanin function has been made with the generation and study of tetraspanin-deficient mice (reviewed in [2,7]).”
BackgroundLocalization and signaling of GPCRs in lipid rafts
Villar, V. A. M., Cuevas, S., Zheng, X., & José, P. A. (2016) · Methods in cell biology · doi:10.1016/bs.mcb.2015.11.008 · Cited by 91
Tetraspanins regulate the protrusive activities of cell membrane
Bari, R., Guo, Q., Xia, B., Zhang, Y. H., Giesert, E. E., Levy, S., Zhang, X. A., & Zhang, X. A. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.10.121 · Cited by 93
“These observations are also consistent with the involvement of tetraspanin in viral entry and release [5,31].”
BackgroundResultCD151 Regulates Tumorigenesis by Modulating the Communication between Tumor Cells and Endothelium
Sądej, R., Romańska, H., Baldwin, G., Gkirtzimanaki, K., Novitskaya, V., Filer, A. D., Krcova, Z., Kusińska, R., Ehrmann, J., Buckley, C. D., et al. (2009) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-08-0574 · Cited by 89
“tility, differentiation, and cell-cell fusion (1-3).”
BackgroundThe L6 Protein TM4SF1 Is Critical for Endothelial Cell Function and Tumor Angiogenesis
Shih, S., Zukauskas, A., Li, D., Liu, G., Ang, L., Nagy, J. A., Brown, L. F., & Dvorak, H. F. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4886 · Cited by 89
“Thus, TM4SF1, such as classic tetraspanins (18), interacts with integrins, and its pairing depends on the state of EC activation.”
BackgroundSelective release of molecules from Weibel-Palade bodies during a lingering kiss
Babich, V., Meli, A., Knipe, L., Dempster, J., Skehel, P., Hannah, M. J., & Carter, T. D. (2008) · Blood · doi:10.1182/blood-2007-09-113746 · Cited by 89
Tetraspanins in human epithelial malignancies
Romańska, H., & Berditchevski, F. (2010) · The Journal of Pathology · doi:10.1002/path.2779 · Cited by 89
Lazareth, H., Hénique, C., Lenoir, O., Puelles, V. G., Flamant, M., Bollée, G., Fligny, C., Camus, M., Guyonnet, L., Millien, C., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11013-2 · Cited by 88
Werner, E., Kowalczyk, A. P., & Faúndez, V. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603676200 · Cited by 88
Rana, S., Claas, C., Kretz, C. C., Nazarenko, I. A., & Zoeller, M. (2010) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2010.10.002 · Cited by 88
RetractedMosquito immune responses and compatibility between Plasmodium parasites and anopheline mosquitoes
Jaramillo-Gutierrez, G., Rodrigues, J., Ndikuyeze, G. H., Povelones, M., Molina-Cruz, A., & Barillas-Mury, C. V. (2009) · BMC Microbiology · doi:10.1186/1471-2180-9-154 · Cited by 88
“They are expressed on the surface of numerous cell types and are involved in diverse processes from cell adhesion to signal transduction and some of them inhibit the function of other members of the same family of proteins [14].”
BackgroundÁlvarez, F. J., Douglas, L. M., Rosebrock, A. P., & Konopka, J. B. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0479 · Cited by 90
“Tetraspanins contain only a small first extracellular loop and a larger second extracellular loop with a distinct type of Cys-containing motif (Hemler, 2005).”
InfluentialTetraspanins and tumor progression
Richardson, M. M., Jennings, L. K., & Zhang, X. A. (2010) · Clinical & Experimental Metastasis · doi:10.1007/s10585-010-9365-5 · Cited by 87
TSPAN12 is a critical factor for cancer–fibroblast cell contact-mediated cancer invasion
Otomo, R., Otsubo, C., Matsushima‐Hibiya, Y., Miyazaki, M., Tashiro, F., Ichikawa, H., Kohno, T., Ochiya, T., Yokota, J., Nakagama, H., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1412062112 · Cited by 88
Update on Pathogenesis of Opisthorchiasis and Cholangiocarcinoma
Sripa, B., Tangkawattana, S., & Brindley, P. J. (2018) · Advances in Parasitology/Advances in parasitology · doi:10.1016/bs.apar.2018.10.001 · Cited by 90
Tetraspanins: Architects of Viral Entry and Exit Platforms
Hantak, M. P., Qing, E., Earnest, J. T., & Gallagher, T. (2018) · Journal of Virology · doi:10.1128/jvi.01429-17 · Cited by 93
“Distinct LEL- and cytoplasmic tail-dependent interactions with integrins (6, 7), adhesion molecules (8), and other tetraspanins and their associated partners (9) give rise to web-like tetraspanin-enriched microdomains (TEMs) on cellular membranes (10, 11).”
BackgroundBjörling, E., Lindskog, C., Oksvold, P., Linné, J., Kampf, C., Hober, S., Uhlén, M., & Pontén, F. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m700411-mcp200 · Cited by 85
“Tetraspanins serve as molecular organizers of multiprotein microdomains in cell membranes and regulate cell migration, fusion, and signaling events (18).”
BackgroundIntegrin-Associated CD151 Drives ErbB2-Evoked Mammary Tumor Onset and Metastasis
Deng, X., Li, Q., Hoff, J. J., Novak, M., Yang, H. L., Jin, H., Erfani, S., Sharma, C., Zhou, P., Rabinovitz, I., et al. (2012) · Neoplasia · doi:10.1593/neo.12922 · Cited by 86
“In addition, CD151 orchestrates assembly of other tetraspanins and nontetraspanin components into large complexes on the cell surface, known as tetraspanin-enriched membrane microdomains (TEMs) [13].”
BackgroundInfluentialSelf-citationTetraspanin CD151 Regulates Transforming Growth Factor β Signaling: Implication in Tumor Metastasis
Sądej, R., Romańska, H., Kavanagh, D. P. J., Baldwin, G., Takahashi, T., Kalia, N., & Berditchevski, F. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3497 · Cited by 86
Boavida, L. C., Qin, P., Broz, M. L., Becker, J. D., & McCormick, S. (2013) · PLANT PHYSIOLOGY · doi:10.1104/pp.113.216598 · Cited by 85
Host factors mediating HIV-1 replication
Friedrich, B. M., Dziuba, N., Li, G., Endsley, M. A., Murray, J. L., & Ferguson, M. R. (2011) · Virus Research · doi:10.1016/j.virusres.2011.08.001 · Cited by 86
The CD63-Syntenin-1 Complex Controls Post-Endocytic Trafficking of Oncogenic Human Papillomaviruses
Gräßel, L., Fast, L. A., Scheffer, K. D., Boukhallouk, F., Spoden, G. A., Tenzer, S., Böller, K., Bago, R., Rajesh, S., Overduin, M., et al. (2016) · Scientific Reports · doi:10.1038/srep32337 · Cited by 86
Chang, Y., & Finnemann, S. C. (2007) · Journal of Cell Science · doi:10.1242/jcs.006361 · Cited by 88
Lafleur, M. A., Xu, D., & Hemler, M. E. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-11-1149 · Cited by 85
“Deletion of individual tetraspanins in mice and flies has yielded relatively minor developmental effects (Hemler, 2005), likely due to functional compensation among different tetraspanins (Fradkin et al.”
Self-citationTumne, A., Shridhar, V., Chen, Y., Stolz, D. B., Saha, K., Ratner, D. M., Ding, M., Watkins, S. C., & Gupta, P. (2009) · Journal of Virology · doi:10.1128/jvi.02629-08 · Cited by 85
“Cellular microdomains consisting of tetraspanin scaffolds (19, 28, 48, 51), something exosome membranes are highly enriched for (13, 40, 41), have been shown to be critical mediators of intracellular trafficking and lateral membrane protein translocation in immune cells (28, 39, 48, 51).”
BackgroundGeng, R., Geller, S. F., Hayashi, T., Ray, C. A., Reh, T. A., Bermingham‐McDonogh, O., Jones, S. M., Wright, C. G., Melki, S. J., Imanishi, Y., et al. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp210 · Cited by 85
“Threshold 14 days 42.2+ 8.4 (4) 76.5+ 6.1 ( 6 )”
InfluentialNew observations on the trafficking and diapedesis of monocytes
Kamei, M., & Carman, C. V. (2009) · Current Opinion in Hematology · doi:10.1097/moh.0b013e3283333949 · Cited by 88
Shi, Y., Zhou, W., Cheng, L., Chen, C., Huang, Z., Fang, X., Wu, Q., He, Z., Xu, S., Lathia, J. D., et al. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.110 · Cited by 84
“Tetraspanins are featured by four transmembrane domains that form multimeric complexes with other cell surface proteins to modulate diverse cellular processes, including cell fusion, adhesion and motility.(10,12) To investigate the role of tetraspanins in the GSC maintenance, we screened for the tetraspanins preferent…”
BackgroundParkinson, J., Wasmuth, J. D., Salinas, G., Bizarro, C. V., Sanford, C., Berriman, M., Ferreira, H. B., Zaha, A., Blaxter, M., Maizels, R. M., et al. (2012) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0001897 · Cited by 84
“TSPs regulate migration, fusion and signaling by acting as organizers of multimolecular membrane complexes involving the plasma membrane, intracellular vesicular compartments and exosomes (reviewed by [118] and [125]).”
BackgroundModeling and Preventing Progressive Hearing Loss in Usher Syndrome III
Geng, R., Akil, O., Gopal, S. R., Chen, D. H. ‐., Stepanyan, R., Basch, M. L., Dinculescu, A., Furness, D. N., Saperstein, D. A., Hauswirth, W. W., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-13620-9 · Cited by 90
Lim, J., Lee, C., Kim, K. Y., Jung, H., Choi, J., Cho, J., Park, S.-H., Kim, Y.-L., Baek, M., Park, J. B., et al. (2018) · PLoS ONE · doi:10.1371/journal.pone.0204204 · Cited by 84
Isolation and characterization of exosomes released from mosquito cells infected with dengue virus
Reyes-Ruíz, J. M., Osuna‐Ramos, J. F., Jesús‐González, L. A. D., Hurtado-Monzón, A. M., Farfán-Morales, C. N., Cervantes-Salazar, M., Bolaños, J., Cigarroa-Mayorga, O. E., Martín‐Martínez, E. S., Medina, F., et al. (2019) · Virus Research · doi:10.1016/j.virusres.2019.03.015 · Cited by 83
Clayton, E. L., Minogue, S., & Waugh, M. G. (2013) · Progress in Lipid Research · doi:10.1016/j.plipres.2013.04.002 · Cited by 84
“PI4KII activity has been observed by several groups in complex with tetraspanins (transmembrane-4 superfamily proteins) [40, [102] [103] [104] [105] [106] [107] which are cell surface, plasma membrane spanning proteins with important roles in adhesion and signalling [108] [109] [110] .”
BackgroundRole of TI-VAMP and CD82 in EGFR cell-surface dynamics and signaling
Danglot, L., Chaineau, M., Dahan, M., Gendron, M., Boggetto, N., Perez, F., & Galli, T. (2010) · Journal of Cell Science · doi:10.1242/jcs.062497 · Cited by 95
“Tetraspanins associate at the plasma membrane and facilitate lateral positioning of various receptors (Berditchevski and Odintsova, 2007; Charrin et al., 2003a; Hemler, 2005) by establishing the tetraspanin web, a network of so-called tetraspaninenriched microdomains (TEMs).”
BackgroundGreco, C., Bralet, M., Ailane, N., Dubart‐Kupperschmitt, A., Rubinstein, E., Naour, F. L., & Boucheix, C. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-4482 · Cited by 92
Takeda, Y., He, P., Tachibana, I., Zhou, B., Miyado, K., Kaneko, H., Suzuki, M., Minami, S., Iwasaki, T., Goya, S., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801902200 · Cited by 83
Hong, I.-K., Byun, H.-J., Lee, J., Jin, Y.-J., Wang, S.-J., Jeoung, D., Kim, Y.-M., & Lee, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.534206 · Cited by 76
“Through this mechanism, tetraspanins influence a broad range of cellular activities including adhesion, proliferation, activation, differentiation, migration, and signaling (4, 8).”
BackgroundIntercellular trafficking via plasmodesmata: molecular layers of complexity
Li, Z. P., Paterlini, A., Glavier, M., & Bayer, E. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03622-8 · Cited by 80
Vences‐Catalán, F., Rajapaksa, R., Srivastava, M. K., Marabelle, A., Kuo, C.-C., Levy, R., & Levy, S. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-1021 · Cited by 84
“Tetraspanins serve as membrane "docking" molecules that interact with cell surface receptors, such as integrins (3) and with intracellular signaling molecules (1, 2), and have been shown to play a role in cancer progression (4, 5).”
BackgroundIntracellular trafficking of raft/caveolae domains: Insights from integrin signaling
Echarri, A., Muriel, O., & del Pozo, M. Á. (2007) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2007.08.004 · Cited by 82
Mazzocca, A., Liotta, F., & Carloni, V. (2008) · Gastroenterology · doi:10.1053/j.gastro.2008.03.024 · Cited by 80
CD44v6 Coordinates Tumor Matrix-triggered Motility and Apoptosis Resistance
Jung, T., Groß, W., & Zöller, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.208421 · Cited by 80
Lewandrowski, U., Zahedi, R. P., Moebius, J., Walter, U., & Sickmann, A. (2007) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m600390-mcp200 · Cited by 80
“The tetraspanins, of which five members (tetraspanins 9, 13, 15, and 27 and CD63) could be identified in this study, share the structural detail of four transmembrane-spanning regions and are supposed to be involved in organizing multimolecular complexes in the plasma membrane ( 27 , 28).”
BackgroundExtracellular Vesicles and Thrombosis: Update on the Clinical and Experimental Evidence
Zifkos, K., Dubois, C., & Schäfer, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179317 · Cited by 79
“Tetraspanins are membrane proteins involved in cell adhesion, activation and proliferation [74] and abundantly expressed on the surface of EVs.”
BackgroundIntegrin Regulation of Epidermal Functions in Wounds
Longmate, W. M., & DiPersio, C. M. (2014) · Advances in Wound Care · doi:10.1089/wound.2013.0516 · Cited by 78
Rappa, G., Santos, M. F., Green, T. M., Karbanová, J., Hassler, J. R., Bai, Y., Barsky, S. H., Corbeil, D., & Lorico, A. (2017) · Oncotarget · doi:10.18632/oncotarget.14804 · Cited by 79
“Given the fusogenic role of CD9 [31, 32], the CD9 Ab may as well facilitate membrane fusion between EVs and recipient cells, particularly in N-ALE.”
BackgroundClinical significance of CD151 overexpression in subtypes of invasive breast cancer
Kwon, M. J., Park, S., Choi, J. Y., Oh, E., Kim, Y., Park, Y., Cho, E. Y., Kwon, M. J., Nam, S. J., Im, Y.-H., et al. (2012) · British Journal of Cancer · doi:10.1038/bjc.2012.11 · Cited by 77
“Tetraspanin proteins form complexes between themselves or with other non-tetraspanin molecules such as integrins, immunoglobulin superfamily members, and signalling molecules, and carry out several functions depending on interacting partners (Hemler, 2005; Zoller, 2009).”
BackgroundExtracellular vesicles set the stage for brain plasticity and recovery by multimodal signalling
Hermann, D. M., Peruzzotti‐Jametti, L., Giebel, B., & Pluchino, S. (2023) · Brain · doi:10.1093/brain/awad332 · Cited by 79
“Different membrane microdomains are organized by different proteins, such as tetraspanins and flotillins 50,51 (Box 2).”
BackgroundJohnson, J. L., Winterwood, N. E., DeMali, K. A., & Stipp, C. S. (2009) · Journal of Cell Science · doi:10.1242/jcs.045997 · Cited by 77
“…into several classes, including regulation of (i) pericellular matrix proteolysis (Gesierich et al., 2006; Hasegawa et al., 2007; Hong et al., 2006; Hong et al., 2005; Huang et al., 2007; Saito et al., 2006; Sugiura and Berditchevski, 1999), (ii) integrin cell-surface expression and trafficking…”
Focal Contact and Hemidesmosomal Proteins in Keratinocyte Migration and Wound Repair
Hopkinson, S. B., Hamill, K. J., Wu, Y., Eisenberg, J. L., Hiroyasu, S., & Jones, J. (2013) · Advances in Wound Care · doi:10.1089/wound.2013.0489 · Cited by 82
“This complex has been termed a tetraspanin ‘‘web’’(123) or tetraspaninenriched microdomain.(124) In mouse skin, CD151 expression is upregulated at the migrating front of the epithelium 256 HOPKINSON ET AL.”
BackgroundCell Surface Tetraspanin CD9 Mediates Chemoresistance in Small Cell Lung Cancer
Kohmo, S., Kijima, T., Otani, Y., Mori, M., Minami, T., Takahashi, R., Nagatomo, I., Takeda, Y., Kida, H., Goya, S., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-0996 · Cited by 77
A Family of Tetraspans Organizes Cargo for Sorting into Multivesicular Bodies
MacDonald, C., Payne, J. A., Aboian, M., Smith, W., Katzmann, D. J., & Piper, R. C. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.03.007 · Cited by 79
“They cluster in membrane microdomains and form complexes with a wide variety of membrane proteins (Hemler, 2005; Stipp et al., 2003).”
BackgroundIntegrin-mediated regulation of epidermal wound functions
DiPersio, C. M., Zheng, R., Kenney, J., & Water, L. V. D. (2016) · Cell and Tissue Research · doi:10.1007/s00441-016-2446-2 · Cited by 76
“…associations with other cell surface proteins, such as members of the tetraspanin family, growth factor receptors, caveolin, or urokinase receptor (uPAR) (Berditchevski 2001; Chapman et al. 1999; Comoglio et al. 2003; Hemler 2005; Porter and Hogg 1998; Salanueva et al. 2007; Wei et al. 2001).”
CD9 induces cellular senescence and aggravates atherosclerotic plaque formation
Cho, J. H., Kim, E.-C., Son, Y., Lee, D.-W., Park, Y. S., Choi, J. H., Cho, K., Kwon, K., & Kim, J.-R. (2020) · Cell Death and Differentiation · doi:10.1038/s41418-020-0537-9 · Cited by 73
Tetraspanin 3 Is Required for the Development and Propagation of Acute Myelogenous Leukemia
Kwon, H. Y., Bajaj, J., Ito, T., Blevins, A., Konuma, T., Weeks, J. L., Lytle, N. K., Koechlein, C. S., Rizzieri, D. A., Chuah, C. T. H., et al. (2015) · Cell stem cell · doi:10.1016/j.stem.2015.06.006 · Cited by 80
“The tetraspanin (tetraspan or TM4SF) family forms a large group of integral membrane proteins possessing four membrane-spanning domains separated by short intracellular and extracellular domains, as well as one long extracellular domain (Hemler, 2005).”
InfluentialPoulter, J. A., Davidson, A. E., Ali, M., Gilmour, D. F., Parry, D. A., Mintz-Hittner, H. A., Carr, I., Bottomley, H. M., Long, V. W., Downey, L., et al. (2012) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.11-8629 · Cited by 75
“Within the LEL, tetraspanins have a signature CCG motif plus additional cysteine residues, which form disulfide bonds and are crucial for protein folding.(37) The p.”
BackgroundKazerounian, S., Duquette, M. A., Reyes, M. A., Lawler, J. T., Song, K., Perruzzi, C. A., Primo, L., Khosravi‐Far, R., Bussolino, F., Rabinovitz, I., et al. (2011) · Blood · doi:10.1182/blood-2010-09-305284 · Cited by 80
Rocha‐Perugini, V., Zamai, M., González, J. M., Barreiro, O., Tejera, E., Yáñez‐Mó, M., Caiolfa, V. R., & Sánchez‐Madrid, F. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00302-13 · Cited by 75
“Tetraspanins are ubiquitous proteins that modulate the function of their associated partners and play important roles in a wide variety of physiological and pathological processes, including immunity and inflammation (16).”
BackgroundMethodCysteine tagging for MS‐based proteomics
Giron, P., Dayon, L., & Sanchez, J. (2010) · Mass Spectrometry Reviews · doi:10.1002/mas.20285 · Cited by 77
“Tetraspanins are important transmembrane proteins that ‘‘regulate cell morphology, motility, invasion, fusion and signaling, in the brain, immune system, on tumors and elsewhere’’ (Hemler, 2005).”
BackgroundInterneuronal exchange and functional integration of synaptobrevin via extracellular vesicles
Vilcaes, A. A., Chanaday, N. L., & Kavalali, E. T. (2021) · Neuron · doi:10.1016/j.neuron.2021.01.007 · Cited by 73
“Tetraspanins are a family of highly conserved proteins that regulate membrane morphology and dynamics affecting intracellular trafficking, exocytosis and endocytosis, cell motility and intercellular signaling (Hemler, 2005), but their role in neurotransmission remains unexplored.”
BackgroundFunctional interplay between tetraspanins and proteases
Yáñez‐Mó, M., Gutiérrez‐López, M. D., & Cabañas, C. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0746-y · Cited by 74
Yoshida, T., Kawano, Y., Sato, K., Ando, Y., Aoki, J., Miura, Y., Komano, J. A., Tanaka, Y., & Koyanagi, Y. (2008) · Traffic · doi:10.1111/j.1600-0854.2007.00700.x · Cited by 74
Castro‐Sánchez, L., Soto-Guzmán, A., Navarro‐Tito, N., Martinez-Orozco, R., & Salazar, E. P. (2010) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.07.004 · Cited by 74
“…in a large variety of physiological and pathological proesses, and there are at least 32 distinct members in mammals, CD9, D37, CD53, CD81, CD151, TM4SF2 and ROM being the best charcterized (Maecker et al., 1997; Hemler, 2005; Hemler et al., 1996; oucheix et al., 2001; Levy and Shoham, 2005).”
BackgroundInfluentialEffect of ICSI on gene expression and development of mouse preimplantation embryos
Giritharan, G., Li, M. W., Sebastiano, F. D., Esteban, F. J., Horcajadas, J. A., Lloyd, K. C. K., Donjacour, A. A., Maltepe, E., & Rinaudo, P. F. (2010) · Human Reproduction · doi:10.1093/humrep/deq266 · Cited by 74
“Cd81 encodes a tetraspanin that functions as an organizer of multi-molecular membrane complexes and as a result, regulates cell migration, fusion and signaling (Hemler, 2005).”
BackgroundTetraspanins CD37 and CD151 differentially regulate Ag presentation and T‐cell co‐stimulation by DC
Sheng, K., van Spriel, A. B., Gartlan, K. H., Sofi, M., Apostolopoulos, V., Ashman, L. K., & Wright, M. D. (2008) · European Journal of Immunology · doi:10.1002/eji.200838798 · Cited by 74
Zhou, P., Erfani, S., Liu, Z., Jia, C., Chen, Y., Xu, B., Deng, X., Alfaro, J., Chen, L., Napier, D. L., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4896 · Cited by 72
“Tetraspanin CD151 is implicated in mediating diverse physiological and pathological processes by impacting the function or signaling of its associated protein complexes, instead of directly interacting with signaling molecules [17, 28].”
BackgroundTobón‐Arroyave, S. I., Celis‐Mejía, N., Córdoba‐Hidalgo, M. P., & Isaza‐Guzmán, D. M. (2019) · Journal Of Clinical Periodontology · doi:10.1111/jcpe.13099 · Cited by 73
“…transmembrane receptors, adhesion molecules, enzymes, signalling proteins and each other, thus forming func‐ tional tetraspanin‐enriched microdomains (Hemler, 2005; Charrin et al., 2009; Yáñez‐Mó, Barreiro, Gordon‐Alonso, Sala‐Valdés, & Sánchez‐Madrid, 2009), which are involved in numerous…”
BackgroundLeung, K. T., Chan, K. Y. Y., Ng, P. C., Lau, T. K., Chiu, W. M., Tsang, K. S., Li, C. K., Kong, C. K. L., & Li, K. (2010) · Blood · doi:10.1182/blood-2010-04-281329 · Cited by 73
Nakazawa, Y., Sato, S., Naito, M., Kato, Y., Mishima, K., Arai, H., Tsuruo, T., & Fujita, N. (2008) · Blood · doi:10.1182/blood-2007-11-124693 · Cited by 73
Protty, M. B., Watkins, N. A., Colombo, D., Thomas, S. G., Heath, V. L., Herbert, J. M. J., Bicknell, R., Senis, Y. A., Ashman, L. K., Berditchevski, F., et al. (2008) · Biochemical Journal · doi:10.1042/bj20081126 · Cited by 73
“As a control, the collagen-binding α2β1 integrin, which is not thought to be tetraspanin-associated [ 4 ], was predominantly immunoprecipitated as a doublet corresponding to the molecular weights of the integrin α 2a ndβ1 chains (Figure 6A, left panel).ForeachimmunoprecipitationinTritonX-100(Figure6A, upper right pane…”
BackgroundInfluentialTetraspanin CD151 plays a key role in skin squamous cell carcinoma
Li, Q., Yang, X. H., Xu, F., Sharma, C., Wang, H.-X., Knoblich, K., Rabinovitz, I., Granter, S. R., & Hemler, M. E. (2012) · Oncogene · doi:10.1038/onc.2012.205 · Cited by 73
Self-citationSiegmund, U., Heller, J., van Kan, J. A. L., & Tudzynski, P. (2013) · PLoS ONE · doi:10.1371/annotation/84c258cf-4f98-43d8-a4f0-7032cba36f22 · Cited by 73
Evolutionary Dynamics of Abundant Stop Codon Readthrough
Jungreis, I., Chan, C. S., Waterhouse, R. M., Fields, G., Lin, M. F., & Kellis, M. (2016) · Molecular Biology and Evolution · doi:10.1093/molbev/msw189 · Cited by 71
“Tetraspanin 86D contains four transmembrane domains and is involved with nervous system development, border follicle cell migration, and positive regulation of Notch signaling pathway (Hemler 2005; Dornier et al. 2012).”
BackgroundMigrasome and Tetraspanins in Vascular Homeostasis: Concept, Present, and Future
Zhang, Y., Wang, J., Ding, Y., Zhang, J., Xu, Y., Xu, J., Zheng, S., & Yang, H. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00438 · Cited by 71
“TSPANs contain a number of shared structural features, including TM1, TM2, TM3 and TM4, a very short intracellular loop (typically four amino acids) between TM2 and TM3, a short ECL1 between TM1 and TM2, a large ECL2 between TM3 and TM4, short amino- and carboxy-terminal tails, and a large central pocket inside the in…”
BackgroundZhu, J., Cai, T., Zhou, J., Du, W., Zeng, Y., Liu, T., Fu, Y., Li, Y., Qian, Q., Yang, X. H., et al. (2021) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-021-01998-4 · Cited by 75
“CD151 regulated laminin-binding integrins and control tumor cell migration and invasion through its effect on their adhesive and signaling functions [12].”
BackgroundEarnest, J. T., Hantak, M. P., Park, J.-E., & Gallagher, T. (2015) · Journal of Virology · doi:10.1128/jvi.00543-15 · Cited by 78
“TEMs are operationally distinguished from classical lipid rafts by their insolubility in zwitterionic detergents, such as CHAPS and Brij 98 (56), and by their complete disruption by nonionic detergents, such as TX100 (44) (Fig.”
BackgroundClaudins—Key Pieces in the Tight Junction Puzzle
Koval, M. H. (2006) · Cell Communication & Adhesion · doi:10.1080/15419060600726209 · Cited by 72
“Tetraspanins, transmembrane proteins which enhance membrane assembly and trafficking to the plasma membrane, are also palmitoylated (61, 62).”
BackgroundSantos, R. C. D., Garay, C., & Antonescu, C. N. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.07.004 · Cited by 70
Wu, L., Yang, S., Li, H., Zhang, Y., Feng, L., Zhang, C., Wei, J., Gu, X., Xu, G., Wang, Z., et al. (2022) · Journal of Nanobiotechnology · doi:10.1186/s12951-022-01732-y · Cited by 71
Tetraspanins in Cell Migration
Jiang, X., Zhang, J., & Huang, Y. (2015) · Cell Adhesion & Migration · doi:10.1080/19336918.2015.1005465 · Cited by 71
“Tetraspanin proteins are structurally characterized by 4 transmembrane domains, 2 extracellular loops, and short intracellular N- and C-termini.(1) One of the 2 extracellular loops is short (EC1), and the other is longer (EC2).”
BackgroundThe Tetraspanin CD63 Is Required for Efficient IgE-Mediated Mast Cell Degranulation and Anaphylaxis
Kraft, S., Jouvin, M., Kulkarni, N. N., Kissing, S., Morgan, E. S., Dvořàk, A. M., Schröder, B., Säftig, P., & Kinet, J. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1202323 · Cited by 71
“This strong, but partial inhibition may be due to the role of tetraspanins in multimeric complexes, which incorporate other members of the tetraspanin family (12, 35), allowing for other tetraspanins to compensate for absent or inhibited CD63.”
BackgroundMolecular Regulation of Sprouting Angiogenesis
Duran, C. L., Howell, D. W., Dave, J. M., Smith, R. L., Torrie, M. E., Essner, J. J., & Bayless, K. J. (2017) · Comprehensive physiology · doi:10.1002/cphy.c160048 · Cited by 80
Transmembrane proteins tetraspanin 4 and CD9 sense membrane curvature
Dharan, R., Goren, S., Cheppali, S. K., Shendrik, P., Brand, G., Vaknin, A., Yu, L., Kozlov, M. M., & Sorkin, R. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2208993119 · Cited by 70
“TSPANs regulate cell morphology, adhesion, motility, fusion, and signaling in diverse organs (3).”
BackgroundOsteoclast cell fusion: mechanisms and molecules
Ishii, M., & Saeki, Y. (2008) · Modern Rheumatology · doi:10.1007/s10165-008-0051-2 · Cited by 70
Lekishvili, T., Fromm, E., Mujoomdar, M., & Berditchevski, F. (2008) · Journal of Cell Science · doi:10.1242/jcs.020347 · Cited by 70
“L6-Ag regulates surface expression of tetraspanins Induced overexpression or downregulation of various tetraspanins in various cell types changes their migratory potential (Hemler, 2005).”
BackgroundTugues, S., Honjo, S., König, C. M., Padhan, N., Kroon, J., Gualandi, L., Li, X., Barkefors, I., Thijssen, V. L., Griffioen, A. W., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.468199 · Cited by 69
“four transmembrane domains, two extracellular loops flanked by short intracellular N and C termini, and a highly conserved sequence motif within the larger extracellular domain (8).”
BackgroundIntegrin α3β1 as a breast cancer target
Subbaram, S., & DiPersio, C. M. (2011) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2011.609557 · Cited by 72
“Through this interaction, CD151 can recruit a3b1 into specialized tetraspaninenriched microdomains (TEMs) on the cell surface, wherein its signaling functions may be influenced by other tetraspanins or TEM-associated proteins [23,26].”
BackgroundTermini, C. M., Cotter, M. L., Marjon, K. D., Buranda, T., Lidke, K. A., & Gillette, J. M. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-11-0660 · Cited by 69
“Tetraspanins also recruit and maintain intracellular signaling molecules in close proximity with membrane proteins, thus regulating downstream biochemical pathways (Hemler, 2005; Wang et al., 2007; Choi et al., 2009; Li et al., 2010).”
BackgroundCai, X., Pacheco–Rodriguez, G., Fan, Q., Haughey, M., Samsel, L., El‐Chemaly, S., Wu, H.-P., McCoy, J. P., Steagall, W. K., Lin, J., et al. (2010) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201003-0489oc · Cited by 69
“Tetraspanins form complexes with other tetraspanins and a variety of transmembrane proteins at tetraspanin-enriched membrane microdomains (42, 43).”
Background
Metadata
- Authors
- Hemler, M. E.
- Affiliations
- Harvard University (US)
- Corresponding author
- Hemler, Martin E.
- ORCID
- Hemler, Martin E.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2005-10
- Volume
- 6
- Issue
- 10
- Pages
- 801-811
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2063186096
- Cited by
- 1,355
- References
- 122
- Citations by year
- 2026: 38 · 2025: 52 · 2024: 67 · 2023: 60 · 2022: 55 · 2021: 77 · 2020: 80 · 2019: 57 · 2018: 69 · 2017: 67 · 2016: 64 · 2015: 65 · 2014: 73 · 2013: 82 · 2012: 74
- FWCI
- 5.25
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- tetraspanins, cell surface proteins, signal transduction, cell motility, cell adhesion, membrane protein regulation, genetic evidence
- MeSH terms
- Animals, Cell Movement, Humans, Membrane Glycoproteins, Signal Transduction, Membrane Microdomains
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