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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CD81 is a specific marker that differentiates between rTregs and aTregs in old cells.
“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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Increased brain size and glial cell number in CD81‐null mice
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EWI-2 regulates α3β1 integrin–dependent cell functions on laminin-5
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Self-citationThe tetraspanin superfamily in insects
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Tetraspanin Protein CD9 Is a Novel Paranodal Component Regulating Paranodal Junctional Formation
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Tetraspanin CD81 is linked to ERK/MAPKinase signaling by Shc in liver tumor cells
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CD81 Associates with 14-3-3 in a Redox-regulated Palmitoylation-dependent Manner
Clark, K. L., Oelke, A., Johnson, M. E., Eilert, K. D., Simpson, P. C., & Todd, S. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312626200 · Cited by 73 · see citing works
Miura, Y., Kainuma, M., Jiang, H., Velasco, H., Vogt, P. K., & Hakomori, S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407297101 · Cited by 70 · see citing works
The Role of the Peripherin/RDS Gene in Retinal Dystrophies
Kohl, S., Giddings, I., Besch, D., Apfelstedt-Sylla, E., Zrenner, E., & Wissinger, B. (1998) · Cells Tissues Organs · doi:10.1159/000046471 · Cited by 70 · see citing works
EWI-2 modulates lymphocyte integrin α4β1 functions
Kolesnikova, T. V., Stipp, C. S., Rao, R. M., Lane, W. S., Luscinskas, F. W., & Hemler, M. E. (2003) · Blood · doi:10.1182/blood-2003-07-2201 · Cited by 64 · see citing works
Self-citationCD9-mediated activation of the p46 Shc isoform leads to apoptosis in cancer cells
Murayama, Y., Miyagawa, J., Oritani, K., Yoshida, H., Yamamoto, K., Kishida, O., Miyazaki, T., Tsutsui, S., Kiyohara, T., Miyazaki, Y., et al. (2004) · Journal of Cell Science · doi:10.1242/jcs.01201 · Cited by 54 · see citing works
Allergen-Induced Airway Hyperreactivity Is Diminished in CD81-Deficient Mice
Deng, J., Yeung, V. P., Tsitoura, D. C., DeKruyff, R. H., Umetsu, D. T., & Levy, S. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.9.5054 · Cited by 50 · see citing works
The Tetraspanin CD151 Functions as a Negative Regulator in the Adhesion-dependent Activation of Ras
Sawada, S., Yoshimoto, M., Odintsova, E., Hotchin, N. A., & Berditchevski, F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300210200 · Cited by 47 · see citing works
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A new class of tetraspanins in fungi
Gourgues, M., Clergeot, P.-H., Veneault‐Fourrey, C., Cots, J., Sibuet, S., Brunet, A., Levis, C., Langin, T., & Lebrun, M. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02355-0 · Cited by 42 · see citing works
A novel 2 bp deletion in the TM4SF2 gene is associated with MRX58
Abidi, F., Holinski-Feder, E., Rittinger, O., Kooy, R. F., Lubs, H. A., Stevenson, R. E., & Schwartz, C. E. (2002) · Journal of Medical Genetics · doi:10.1136/jmg.39.6.430 · Cited by 40 · see citing works
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Yantar, a conserved arginine-rich protein is involved in Drosophila hemocyte development
Sinenko, S. A., Kim, E. K., Wynn, R., Manfruelli, P., Andó, I., Wharton, K. A., Perrimon, N., & Mathey-Prévôt, B. (2004) · Developmental Biology · doi:10.1016/j.ydbio.2004.05.022 · Cited by 37 · see citing works
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Oostergetel, G. T., Keegstra, W., & Brisson, A. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5128 · Cited by 22 · see citing works
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Routes and mechanisms of extracellular vesicle uptake
Mulcahy, L. A., Pink, R. C., & Carter, D. R. F. (2014) · Journal of Extracellular Vesicles · doi:10.3402/jev.v3.24641 · Cited by 2,832 · see citing works
“Tetraspanins Tetraspanins are membrane proteins which have numerous functions including cell adhesion, motility, activation and proliferation (reviewed in (52)).”
BackgroundTetraspanins in Extracellular Vesicle Formation and Function
Andreu, Z., & Yáñez-Mó, M. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00442 · Cited by 1,401 · see citing works
“Nat Rev Mol Cell Biol (2005) 6(10):801–11.”
BackgroundAkers, J. C., Gonda, D., Kim, R., Carter, B. S., & Chen, C. C. (2013) · Journal of Neuro-Oncology · doi:10.1007/s11060-013-1084-8 · Cited by 1,423 · see citing works
“Tetraspanins are so termed because they consist of four transmembrane domains that form a stereotypical tertiary structure [36].”
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 · see citing works
“The protein products of ITGB1, CD151, and FERMT1 physically interact at the cell surface to mediate integrin signaling (Calderwood et al., 2013; Hemler, 2005).”
BackgroundExosomes: proteomic insights and diagnostic potential
Simpson, R. J., Lim, J. W., Moritz, R. L., & Mathivanan, S. (2009) · Expert Review of Proteomics · doi:10.1586/epr.09.17 · Cited by 1,113 · see citing works
Lipid rafts: at a crossroad between cell biology and physics
Jacobson, K., Mouritsen, O. G., & Anderson, R. G. W. (2007) · Nature Cell Biology · doi:10.1038/ncb0107-7 · Cited by 1,105 · see citing works
“In some instances, proteins from the four-transmembrane domain tetraspanin superfamil”
BackgroundProteomic profiling of exosomes: Current perspectives
Simpson, R. J., Jensen, S. S., & Lim, J. W. E. (2008) · PROTEOMICS · doi:10.1002/pmic.200800109 · Cited by 850 · see citing works
Trafficking and function of the tetraspanin CD63
Pols, M. S., & Klumperman, J. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.09.020 · Cited by 745 · see citing works
Nazarenko, I. A., Rana, S., Baumann, A., McAlear, J., Hellwig, A., Trendelenburg, M. F., Lochnit, G., Preissner, K. T., & Zöller, M. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2470 · Cited by 686 · see citing works
“Within TEM, tetraspanins act as “molecular facilitators” (10, 18), getting involved in cell motility, adhesion (10, 20–23),”
Juno is the egg Izumo receptor and is essential for mammalian fertilization
Bianchi, E., Doe, B., Goulding, D., & Wright, G. J. (2014) · Nature · doi:10.1038/nature13203 · Cited by 674 · see citing works
“Tetraspanins are known to organise other membrane proteins within microdomains 32 and quantitative differences in sperm adhesion to Cd9-deficient eggs have been reported 33 .”
Rana, S., Yue, S., Stadel, D., & Zöller, M. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.06.018 · Cited by 665 · see citing works
RetractedTetraspanins: push and pull in suppressing and promoting metastasis
Zöller, M. (2008) · Nature reviews. Cancer · doi:10.1038/nrc2543 · Cited by 668 · see citing works
Tetraspanin-enriched microdomains: a functional unit in cell plasma membranes
Yáñez‐Mó, M., Barreiro, O., Gordón‐Alonso, M., Sala-Valdés, M., & Sánchez‐Madrid, F. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.06.004 · Cited by 617 · see citing works
Organization, dynamics and mechanoregulation of integrin-mediated cell–ECM adhesions
Kanchanawong, P., & Calderwood, D. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00531-5 · Cited by 607 · see citing works
Cook‐Mills, J. M., Marchese, M. E., & Abdala‐Valencia, H. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3522 · Cited by 597 · see citing works
Mathivanan, S., Lim, J. W. E., Tauro, B. J., Ji, H. L., Moritz, R. L., & Simpson, R. J. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900152-mcp200 · Cited by 593 · see citing works
“Tetraspanins assemble a network of complexes containing different tetraspanins and transmembrane and cytosolic proteins that are necessary for their functions in cell migration, metastasis, and angiogenesis (57, 58).”
BackgroundExosome release of β-catenin: a novel mechanism that antagonizes Wnt signaling
Chairoungdua, A., Smith, D. L., Pochard, P., Hull, M., & Caplan, M. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201002049 · Cited by 514 · see citing works
“Tetraspanins have been implicated in a multitude of biological processes, such as cell adhesion, migration, cell fusion, and signal transduction through their associated partner molecules (Hemler, 2005; Levy and Shoham, 2005).”
BackgroundExosome mimetics: a novel class of drug delivery systems
Schiffelers, R. M., Kooijmans, S. A. A., Vader, P., van Dommelen, & van Solinge, W. W. (2012) · International Journal of Nanomedicine · doi:10.2147/ijn.s29661 · Cited by 517 · see citing works
“Tetraspanins have been relatively understudied due to their limited ligand-receptor interaction and their small size, which in some cases may prevent biochemical or immunological detection.(117) However, their functions as mediators of fusion, cell migration, cell-cell adhesion, and signaling events designate them as…”
BackgroundLateral 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 · see citing works
“and Hemler, M. E. (2006) Contrasting effects of EWI proteins, integrins”
BackgroundBuschow, S. I., Hoen, E. N. M. N., van Niel, G., Pols, M. S., ten Broeke, T., Lauwen, M. M., OSSENDORP, F. A., Melief, C. J. M., Raposo, G., Wubbolts, R., et al. (2009) · Traffic · doi:10.1111/j.1600-0854.2009.00963.x · Cited by 430 · see citing works
“Hence, deleting one tetraspanin family member is usually without effect (47).”
BackgroundTodeschini, A. R., & Hakomori, S. (2007) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2007.10.008 · Cited by 426 · see citing works
“TSP are palmitoylated and N-glycosylated and associate with integrin receptors, gangliosides and signaling molecules forming a membrane multi molecular complex referred as tetraspanin web [66]; for review see [70].”
Tetraspanin proteins promote multiple cancer stages
Hemler, M. E. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3640 · Cited by 403 · see citing works
Self-citationThe chemokine system in cancer biology and therapy
Mantovani, A., Savino, B., Locati, M., Zammataro, L. A., Allavena, P., & Bonecchi, R. (2009) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2009.11.007 · Cited by 395 · see citing works
“prognosis and metastatic progression, revealing that it is a metastasis-suppressor protein [184].”
BackgroundJunge, H. J., Yang, S. C., Burton, J. B., Paes, K., Shu, X., French, D. M., Costa, M., Rice, D. S., & Ye, W. (2009) · Cell · doi:10.1016/j.cell.2009.07.048 · Cited by 391 · see citing works
“Investigation of several prototypic tetraspanins has led to a model in which tetraspanins organize specialized tetraspanin-enriched microdomains (TEMs) that act as signaling platforms in the plasma membrane (Boucheix and Rubinstein, 2001; Hemler, 2005).”
Microvesicles and Viral Infection
Meckes, D. G., & Raab‐Traub, N. (2011) · Journal of Virology · doi:10.1128/jvi.05853-11 · Cited by 389 · see citing works
“These proteins have four transmembrane domains and conserved motifs, including a CCG motif and two disulfide bonds within the second extracellular loop (65).”
BackgroundA review of the regulatory mechanisms of extracellular vesicles-mediated intercellular communication
Liu, Y.-J., & Wang, C. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01103-6 · Cited by 362 · see citing works
“Tetraspanin-enriched microdomains (TEM) on the surface of EVs gather tetraspanins, adhesion molecules, and transmembrane receptor proteins, and these primary raft-like structures interact with a large variety of transmembrane and cytosolic signaling proteins [98, 99].”
BackgroundKeskin, D. B., Allan, D., Rybalov, B., Andzelm, M. M., Stern, J. N. H., Kopcow, H. D., Koopman, L. A., & Strominger, J. L. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0611098104 · Cited by 370 · see citing works
Palmitoylome profiling reveals S-palmitoylation–dependent antiviral activity of IFITM3
Yount, J. S., Moltedo, B., Yang, Y.-Y., Charron, G., Moran, T. M., López, C. B., & Hang, H. C. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.405 · Cited by 367 · see citing works
Mechanisms of pathogen entry through the endosomal compartments
Gruenberg, J., & van der Goot, F. G. (2006) · Nature reviews. Molecular cell biology · doi:10.1038/nrm1959 · Cited by 360 · see citing works
“Intralumenal vesicles also contain molecules that are not destined for degradation, including members of the family of tetraspanin protein”
BackgroundUroplakins in urothelial biology, function, and disease
Wu, X., Kong, X., Pellicer, À., Kreibich, G., & Sun, T. (2009) · Kidney International · doi:10.1038/ki.2009.73 · Cited by 353 · see citing works
“These two UPs belong to the tetraspanin family comprised of many leukocyte differentiation antigens such as CD9, CD27, CD63, CD81, and CD83.(39,40) UPII possesses an N-terminal signal peptide followed by a heavily glycosylated pro-peptide of 59 amino acids ending in an RGRR consensus substrate for furin, a trans-Golgi…”
BackgroundElyahu, Y., Hekselman, I., Eizenberg-Magar, I., Berner, O., Strominger, I., Schiller, M., Mittal, K., Nemirovsky, A., Eremenko, E., Vital, A., et al. (2019) · Science Advances · doi:10.1126/sciadv.aaw8330 · Cited by 324 · see citing works
“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.”
BackgroundTargeting of tetraspanin proteins — potential benefits and strategies
Hemler, M. E. (2008) · Nature Reviews Drug Discovery · doi:10.1038/nrd2659 · Cited by 345 · see citing works
Self-citationCellular Proteins in Influenza Virus Particles
Shaw, M. L., Stone, K. L., Colangelo, C. M., Gulcicek, E. E., & Palese, P. (2008) · PLoS Pathogens · doi:10.1371/journal.ppat.1000085 · Cited by 324 · see citing works
“Tetraspanins have four transmembrane domains and two extracellular loops and are involved in both homo- and heterotypic interactions in specialized membrane domains referred to as tetraspanin-enriched microdomains (TEMs) [62].”
BackgroundThe Role of Wnt Signaling in Physiological and Pathological Angiogenesis
Dejana, E. (2010) · Circulation Research · doi:10.1161/circresaha.110.223750 · Cited by 347 · see citing works
Crystal Structure of a Full-Length Human Tetraspanin Reveals a Cholesterol-Binding Pocket
Zimmerman, B., Kelly, B., McMillan, B. J., Seegar, T. C. M., Dror, R. O., Kruse, A. C., & Blacklow, S. C. (2016) · Cell · doi:10.1016/j.cell.2016.09.056 · Cited by 307 · see citing works
“Despite their common ancestry, the vertebrate tetraspanins have acquired a variety of discrete and important biological functions, which highlight their critical, though underappreciated, role in mammalian physiology (Hemler, 2005).”
BackgroundSignal co-operation between integrins and other receptor systems
Streuli, C. H., & Akhtar, N. (2009) · Biochemical Journal · doi:10.1042/bj20081948 · Cited by 306 · see citing works
Tetraspanins as Regulators of Protein Trafficking
Berditchevski, F., & Odintsova, E. (2006) · Traffic · doi:10.1111/j.1600-0854.2006.00515.x · Cited by 296 · see citing works
“However, the PKCa-dependent internalization of b1 integrins seems to proceed through caveoli and/or Triton-X-100-resistant microdomains (55), which in most cells exclude tetraspanins (3).”
BackgroundInfluentialIlekis, J. V., Tsilou, E. T., Fisher, S. J., Abrahams, V. M., Soares, M. J., Cross, J. C., Zamudio, S., Illsley, N. P., Myatt, L., Colvis, C. M., et al. (2016) · American Journal of Obstetrics and Gynecology · doi:10.1016/j.ajog.2016.03.001 · Cited by 291 · see citing works
EpCAM: Structure and function in health and disease
Schnell, U., Cirulli, V., & Giepmans, B. N. G. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.04.018 · Cited by 291 · see citing works
Regulation of B1 cell migration by signals through Toll-like receptors
Ha, S.-A., Tsuji, M., Suzuki, K., Meek, B., YASUDA, N., Kaisho, T., & Fagarasan, S. (2006) · The Journal of Experimental Medicine · doi:10.1084/jem.20061041 · Cited by 290 · see citing works
“CD9 is known to be selectively expressed by B1 cells (25) and to regulate cell motility (20).”
BackgroundExtracellular vesicle docking at the cellular port: Extracellular vesicle binding and uptake
French, K. C., Antonyak, M. A., & Cerione, R. A. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.01.002 · Cited by 281 · see citing works
“They often interact with tetraspanins and appear to mediate many cellular outcomes [50, 56].”
BackgroundCooperation Between Integrins and Growth Factor Receptors in Signaling and Endocytosis
Ivaska, J., & Heino, J. (2011) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-092910-154017 · Cited by 279 · see citing works
“The tetraspanins are another family of proteins that may link integrins to GFRs (Hemler 2005).”
BackgroundZeng, A., Li, H., Guo, L., Gao, X., McKinney, S., Wang, Y., Yu, Z., Park, J., Semerad, C. L., Ross, E. J., et al. (2018) · Cell · doi:10.1016/j.cell.2018.05.006 · Cited by 280 · see citing works
Tetraspanins, More than Markers of Extracellular Vesicles in Reproduction
Jankovičová, J., Sečová, P., Michalková, K., & Antalíková, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207568 · Cited by 281 · see citing works
“In general, common components of TEMs within the cell membrane are tetraspanins, integrins, and other adhesion receptors and transmembrane receptor proteins [52,57,81,82].”
BackgroundExosomes as nucleic acid nanocarriers
van den Boorn, J. G., Daßler, J., Coch, C., Schlee, M., & Hartmann, G. (2012) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2012.06.011 · Cited by 280 · see citing works
“They regularly associate with one another forming clusters in tetraspanin membrane domains (TEMs) or with neighboring transmembrane proteins like integrins [62].”
BackgroundHurley, J. H., Bouřa, E., Carlson, L. A., & Różycki, B. (2010) · Cell · doi:10.1016/j.cell.2010.11.030 · Cited by 271 · see citing works
Wang, Y., Zhao, M., Liu, S.-Y., Guo, J., Lu, Y.-R., Cheng, J.-Q., & Liu, J. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-03127-z · Cited by 265 · see citing works
Yang, W., Vizio, D. D., Kirchner, M., Steen, H., & Freeman, M. R. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800448-mcp200 · Cited by 268 · see citing works
“Tetraspanins are a family of integral transmembrane proteins exhibiting substantial sequence identity and common structural features (42).”
BackgroundTetraspanins Function as Regulators of Cellular Signaling
Termini, C. M., & Gillette, J. M. (2017) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2017.00034 · Cited by 268 · see citing works
“TEMs consist of homophilic and heterophilic interactions amongst tetraspanins, interactions between tetraspanins and other membrane proteins, as well as interactions between tetraspanins and proteins at the membrane/cytoplasm interface (Hemler, 2005; Charrin et al., 2009, 2014; Stipp, 2010).”
BackgroundLiu, C., Zhang, W., Li, Y., Chang, J., Tian, F., Zhao, F., Ma, Y., & Sun, J. (2019) · Nano Letters · doi:10.1021/acs.nanolett.9b02841 · Cited by 267 · see citing works
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 · see citing works
“…implicated in regulating various biological functions, including antigen presentation, cell adhesion and migration, cell–cell fusion, cell activation, and proliferation (for reviews see Berditchevski, 2001; Vogt et al., 2002; Hemler, 2003; Stipp et al., 2003; Tarrant et al., 2003; Hemler, 2005).”
BackgroundKuhn, S., Koch, M., Nübel, T., Ladwein, M., Antolovic, D., Klingbeil, P., Hildebrand, D., Moldenhauer, G., Langbein, L., Franke, W. W., et al. (2007) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0384 · Cited by 252 · see citing works
“The following observations supported this hypothesis: (a) the CD44v6/CO-029/EpCAM/ claudin-7 complex is located in tetraspanin-enriched membrane microdomains (TEM) that serve as a signaling platform (8, 9) and (b) the TEM-localized complex supports matrix adhesion, agglomeration, and apoptosis resistance distinctly to…”
BackgroundInfluentialZijlstra, A., Lewis, J. D., Degryse, B., Stuhlmann, H., & Quigley, J. P. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.01.031 · Cited by 250 · see citing works
“Adhesion receptor function is tightly controlled through regulatory pathways that include integrin-associated transmembrane proteins such as CD98 (Feral et al., 2005), CD47 (Brown and Frazier, 2001), and tetraspanins such as CD82 and CD151 (Bienstock and Barrett, 2001; Hemler, 2005 ).”
BackgroundInfluentialRaft domains of variable properties and compositions in plasma membrane vesicles
Levental, I., Grzybek, M., & Simons, K. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1105996108 · Cited by 246 · see citing works
“, in NEM GPMVs) could be the physicochemical analogs of various “nonraft” PM domains inferred from biochemical and nanoscopic observations, including GPI- anchored protein (AP) domains (24), heavy rafts (25), Lubrol rafts (26), Hras domains (27), T-cell receptor islands (28), and tetraspanin webs (29).”
BackgroundMüller, T., Meyer, H. E., Egensperger, R., & Marcus, K. (2008) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2008.05.002 · Cited by 242 · see citing works
“metastasis (Hemler, 2005) AFT activated accompanied by”
BackgroundChiba, M., KIMURA, M., & ASARI, S. (2012) · Oncology Reports · doi:10.3892/or.2012.1967 · Cited by 232 · see citing works
“For example, it has been reported that TSPAN29 (CD9) is associated with ICAM-1, and TSPAN28 (CD81) is associated with CD19 (8-10).”
BackgroundNovel Research Horizons for Presenilins and γ-Secretases in Cell Biology and Disease
Strooper, B. D., & Annaert, W. G. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100109-104117 · Cited by 233 · see citing works
Schlesinger, M., & Bendas, G. (2014) · International Journal of Cancer · doi:10.1002/ijc.28927 · Cited by 230 · see citing works
Verweij, F. J., van Eijndhoven, M. A. J., Hopmans, E. S., Vendrig, T., Würdinger, T., Cahir-McFarland, E. D., Kieff, E. D., Geerts, D., van der Kant, R., Neefjes, J., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.123 · Cited by 230 · see citing works
“In LMP1-transfected HEK293 cells, instead of Triton X-100 we used a 1% Brij-98.”
BackgroundInfluentialKidney 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 · see citing works
Haouzi, D., Assou, S., Mahmoud, K., Tondeur, S., Reme, T. X., Hedon, B., Vos, J. D., & Hamamah, S. (2009) · Human Reproduction · doi:10.1093/humrep/dep039 · Cited by 229 · see citing works
Nikopoulos, K., Gilissen, C., Hoischen, A., Nouhuys, C. E. V., Boonstra, F. N., Blokland, E. A. W., Arts, P., Wieskamp, N., Strom, T. M., Ayuso, C., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2009.12.016 · Cited by 228 · see citing works
“Tetraspanins are suggested to form so-called tetraspaninenriched microdomains that act as specific signaling compartments within the membrane and might form homomultimers, as well as protein complexes, with nontetraspanin membrane proteins.(30,31) In the case that TSPAN12 indeed forms homomultimers, the two missense m…”
BackgroundMembrane Domains and the “Lipid Raft” Concept
Sonnino, S., & Prinetti, A. (2012) · Current Medicinal Chemistry · doi:10.2174/09298673130103 · Cited by 228 · see citing works
“, galectins), intracellular proteins (clathrin in clathrin-coated pits), or membrane proteins (tetraspanins [8], caveolins [9, 10], flotillins [11]).”
BackgroundRegulation and roles for claudin‐family tight junction proteins
Findley, M. K., & Koval, M. H. (2009) · IUBMB Life · doi:10.1002/iub.175 · Cited by 224 · see citing works
“Tetraspanins, such as CD9 and CD81, are also palmitoylated which is critical to their function as membrane chaperones and organizers of higher order membrane domains (16).”
BackgroundExosome target cell selection and the importance of exosomal tetraspanins: a hypothesis
Rana, S., & Zöller, M. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390559 · Cited by 224 · see citing works
Spoden, G. A., Freitag, K., Husmann, M., Böller, K., Sapp, M. J., Lambert, C., & Florin, L. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003313 · Cited by 223 · see citing works
“In addition, typical raft resident proteins, like GPI-anchored proteins and caveolin do not associate with tetraspanins [15].”
BackgroundBarreiro, O., Zamai, M., Yáñez‐Mó, M., Tejera, E., López‐Romero, P., Monk, P. N., Gratton, E., Caiolfa, V. R., & Sánchez‐Madrid, F. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200805076 · Cited by 219 · see citing works
Structural insights into tetraspanin CD9 function
Umeda, R., Satouh, Y., Takemoto, M., Nakada-Nakura, Y., Liu, K., Yokoyama, T., Shirouzu, M., Iwata, S., Nomura, N., Sato, K., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15459-7 · Cited by 217 · see citing works
Tomasetti, M., Lee, W., Santarelli, L., & Neužil, J. (2017) · Experimental & Molecular Medicine · doi:10.1038/emm.2016.153 · Cited by 216 · see citing works
Podocyte–actin dynamics in health and disease
Perico, L., Conti, S., Benigni, A., & Remuzzi, G. (2016) · Nature Reviews Nephrology · doi:10.1038/nrneph.2016.127 · Cited by 211 · see citing works
Lipid Rafts and Alzheimer’s Disease: Protein-Lipid Interactions and Perturbation of Signaling
Hicks, D. A., Nalivaeva, N. N., & Turner, A. J. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00189 · Cited by 205 · see citing works
“They are involved in a whole range of cellular processes, from cell morphology and motility to signaling pathways (Hemler, 2005).”
BackgroundMonti, E., Bonten, E. J., d’Azzo, A., Bresciani, R., Venerando, B., Borsani, G., Schauer, R., & Tettamanti, G. (2010) · Advances in carbohydrate chemistry and biochemistry · doi:10.1016/s0065-2318(10)64007-3 · Cited by 201 · see citing works
Brazzoli, M., Bianchi, A., Filippini, S., Weiner, A. J., Zhu, Q., Pizza, M., & Crotta, S. (2008) · Journal of Virology · doi:10.1128/jvi.00665-08 · Cited by 200 · see citing works
“serves as a scaffold for signaling processes (6, 27, 33).”
BackgroundJolly, C. L., & Sattentau, Q. J. (2007) · Journal of Virology · doi:10.1128/jvi.01845-06 · Cited by 199 · see citing works
“Since tetraspanins are regulators of actin organization (21), we wished to investigate the existence of physical and/or functional associations between the T-cell actin cytoskeleton and HIV-1 assembly and budding platforms at the plasma membrane.”
BackgroundInfluentialMechanisms of MAVS Regulation at the Mitochondrial Membrane
Jacobs, J. L., & Coyne, C. B. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.10.007 · Cited by 197 · see citing works
“TSPAN6 is a member of the membrane-embedded tetraspanin protein family that has been shown to have many different functions in the cell, including various roles in host immunity [87] Interestingly, TSPAN6 does not promote the ubiquitination of MAVS either directly or indirectly but is itself ubiquitinated in order to…”
BackgroundThe role of claudins in cancer metastasis
Tabariès, S., & Siegel, P. M. (2016) · Oncogene · doi:10.1038/onc.2016.289 · Cited by 194 · see citing works
More than one door – Budding of enveloped viruses through cellular membranes
Welsch, S., Müller, B., & Kräusslich, H. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.03.060 · Cited by 196 · see citing works
“membrane and some intracellular membranes (reviewed in [65]).”
Tauro, B., Mathias, R. A., Greening, D., Gopal, S. K., Ji, H., Kapp, E., Coleman, B. M., Hill, A., Kusebauch, U., Hallows, J., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.027086 · Cited by 181 · see citing works
“They are reported to function as scaffolding proteins which interact with integrins; many tetraspanins have been implicated in tumour progression [92-94].”
BackgroundMutations in TSPAN12 Cause Autosomal-Dominant Familial Exudative Vitreoretinopathy
Poulter, J. A., Ali, M., Gilmour, D. F., Rice, A., Kondo, H., Hayashi, K., Mackey, D. A., Kearns, L. S., Ruddle, J. B., Craig, J. E., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.01.012 · Cited by 193 · see citing works
“Members of this protein family are characterized by their ability to interact laterally with other tetraspanins and interacting proteins, thereby facilitating the production of large multimolecular membrane complexes, also called tetraspanin webs.(30) Through a number of cellbased assays and genetic interaction screen…”
BackgroundLatysheva, N., Muratov, G., Rajesh, S., Padgett, M., Hotchin, N. A., Overduin, M., & Berditchevski, F. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00849-06 · Cited by 191 · see citing works
“A considerable body of recent work has firmly established that TERM contribute to regulation of the activities of various transmembrane proteins (19, 29).”
BackgroundExtracellular Vesicles and Exosomes: Insights From Exercise Science
Nederveen, J. P., Warnier, G., Carlo, A. D., Nilsson, M. I., & Tarnopolsky, M. A. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2020.604274 · Cited by 192 · see citing works
“…coupling, or other Ca2+-mediated events while later signals such as hormone release (e.g., cortisol), HPA axis activation (e.g., catecholamines), metabolic stress, and/or reactive oxygen species may potentiate the EV response (Savina et al., 2003; Eldh et al., 2010; Hergenreider et al., 2012).”
BackgroundPalmitoylation of membrane proteins (Review)
Charollais, J., & Goot, F. G. V. D. (2008) · Molecular Membrane Biology · doi:10.1080/09687680802620369 · Cited by 187 · see citing works
“TEMs are viewed as signaling microdomains that regulate integrin-dependent adhesion [51,52,56] and their disassembly leads to altered adhesion and cell spreading [54].”
BackgroundKe, A., Shi, G., Zhou, J., Huang, X., Shi, Y., Ding, Z., Wang, X., Devbhandari, R. P., & Fan, J. (2011) · Gastroenterology · doi:10.1053/j.gastro.2011.02.008 · Cited by 184 · see citing works
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. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-2949 · Cited by 183 · see citing works
“CD151 may link laminin-binding integrins to other proteins within the plasma membrane (38, 39).”
BackgroundSelf-citationThe Norrin/Frizzled4 signaling pathway in retinal vascular development and disease
Ye, X., Wang, Y., & Nathans, J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.07.003 · Cited by 183 · see citing works
“Members of this family participate in diverse cellular processes, and several of them can organize microdomains in the plasma membrane [34].”
Yue, S., Mu, W., Erb, U., & Zöller, M. (2014) · Oncotarget · doi:10.18632/oncotarget.2958 · Cited by 181 · see citing works
Hurwitz, S. N., Conlon, M. M., Rider, M. A., Brownstein, N. C., & Meckes, D. G. (2016) · Journal of Extracellular Vesicles · doi:10.3402/jev.v5.31295 · Cited by 177 · see citing works
“These modifications enable organization of tetraspanin-enriched microdomains (TEMs) on the cell membrane that allow interaction with integrin molecules (92).”
BackgroundEbnet, K. (2017) · Physiological Reviews · doi:10.1152/physrev.00004.2017 · Cited by 177 · see citing works
“Tetraspanins assemble protein complexes in the membrane through lateral associations to form tetraspanin-enriched microdomains (83).”
BackgroundStress response signaling and virulence: insights from entomopathogenic fungi
Ortiz‐Urquiza, A., & Keyhani, N. O. (2014) · Current Genetics · doi:10.1007/s00294-014-0439-9 · Cited by 176 · see citing works
Metastasis suppressors genes in cancer
Stafford, L. J., Vaidya, K. S., & Welch, D. R. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.12.016 · Cited by 175 · see citing works
Dornier, E., Coumailleau, F., Ottavi, J., Moretti, J., Boucheix, C., Mauduit, P., Schweisguth, F., & Rubinstein, E. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201201133 · Cited by 175 · see citing works
“They are expressed in many cell types and have been implicated in various biological processes including cell migration, cell fusion, lymphocyte activation, as well as viral and parasitic infections (Hemler, 2005; Charrin et al., 2009).”
Liver fluke vaccines in ruminants: strategies, progress and future opportunities
Toet, H., Piedrafita, D. M., & Spithill, T. W. (2014) · International Journal for Parasitology · doi:10.1016/j.ijpara.2014.07.011 · Cited by 173 · see citing works
Bacteria-Induced Uroplakin Signaling Mediates Bladder Response to Infection
Thumbikat, P., Berry, R. E., Zhou, G., Billips, B. K., Yaggie, R. E., Zaichuk, T. A., Sun, T., Schaeffer, A. J., & Klumpp, D. J. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000415 · Cited by 173 · see citing works
“Tetraspanins typically function as transmembrane linkers in a complex with other proteins that then transduce signals [48].”
BackgroundMicrovesicles/exosomes as potential novel biomarkers of metabolic diseases
ller, G. M. A. U. (2012) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s32923 · Cited by 169 · see citing works
“Tetraspanins have been implicated in a multitude of biological processes, such as cell adhesion, migration, fusion, and signal transduction through their associated partner molecules.(72,73) Microarray analysis showed that CD9 expression in tumor cells correlated with the down-regulation of several Wnt family genes an…”
BackgroundVicente‐Manzanares, M., & Horwitz, A. R. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-207-6_1 · Cited by 169 · see citing works
Rethinking glomerular basement membrane thickening in diabetic nephropathy: adaptive or pathogenic?
Marshall, C. B. (2016) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00313.2016 · Cited by 168 · see citing works
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 · see citing works
Self-citationLaminin-binding integrins and their tetraspanin partners as potential antimetastatic targets
Stipp, C. S. (2010) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399409001355 · Cited by 165 · see citing works
“and Hemler, M.E. (2003) EWI-2 regulates alpha3beta1 integrin-”
Tabariès, S., Dong, Z., Annis, M. G., Ömeroğlu, A., Pepin, F., Ouellet, V., Russo, C., Hassanain, M. M., Metrakos, P. P., Diaz, Z., et al. (2010) · Oncogene · doi:10.1038/onc.2010.518 · Cited by 164 · see citing works
“In this regard, tetraspanins are essential for adhesion strengthening of integrin-containing complexes and individual tetraspanins have been found in complexes with numerous integrin partners (Hemler, 2005; Lazo, 2007).”
BackgroundBeckmann, J., Scheitza, S., Wernet, P., Fischer, J., & Giebel, B. (2007) · Blood · doi:10.1182/blood-2006-11-055921 · Cited by 160 · see citing works
“However, little is known about their function, though tetraspanins seem to take part in regulating the activation, the motility and the antigen presentation of different leukocytes.(37,38) Interestingly, it has been shown that, in addition to the cell surface, many tetraspanins including CD53 and CD63 are localized on…”
Background
- 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
- Health Sciences › Medicine › Rheumatology › 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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