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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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Regulation of MHC II and CD1 antigen presentation: from ubiquity to security
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“Knock-down of CD151, but not other tetraspanins, impaired the formation of TERMs and its deletion inhibited the function of many membrane proteins [5].”
BackgroundInfluentialChen, L., Yuan, D., Wang, G., Wang, Y., Wu, Y., & Zhu, J. (2010) · Journal of Korean Medical Science · doi:10.3346/jkms.2010.25.10.1438 · Cited by 40
“The molecule may accept extracellular signals when located on the membrane and carry out functions in the cytoplasm, like other tetraspanins such as CD9, CD82 and CD63 (27, 28).”
BackgroundTetraspanins: Spanning from solid tumors to hematologic malignancies
Yang, Y., Sari, I. N., Zia, M. F., Lee, S. R., Song, S. J., & Kwon, H. Y. (2016) · Experimental Hematology · doi:10.1016/j.exphem.2016.02.006 · Cited by 40
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Extracellular Vesicle miRNAs in the Promotion of Cardiac Neovascularisation
Kesidou, D., Martins, P. A. D. C., Windt, L. J. D., Brittan, M., Beqqali, A., & Baker, A. H. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.579892 · Cited by 41
“The glycoproteins [e.g., Heparan sulphate proteoglycans (HSPG) (Christianson et al., 2013)] and proteins [e.g., integrins (Morelli et al., 2004), tetraspanins (Hemler, 2005)] on the surfaces of EVs and their target cells are recognised as critical factors that determine the uptake mechanism.”
BackgroundDufrançais, O., Mascarau, R., Poincloux, R., Maridonneau‐Parini, I., Raynaud‐Messina, B., & Vérollet, C. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-021-03875-x · Cited by 40
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“Tspan6 belongs to the tetraspanin family of proteins that bind and modulate integrin function (Hemler, 2005).”
BackgroundExploring the function of long non-coding RNA in the development of bovine early embryos
Caballero, J., Gilbert, I., Fournier, É., Gagné, D., Scantland, S., Macaulay, A. D., & Robert, C. (2014) · Reproduction Fertility and Development · doi:10.1071/rd14338 · Cited by 45
“The third gene is CD9, which is a member of the 448 tetraspanin family associated with many cell functions such as differentiation, adhesion and 449 signal transduction (Hemler 2005).”
BackgroundIsraels, S. J., & McMillan‐Ward, E. (2009) · Thrombosis Research · doi:10.1016/j.thromres.2009.07.005 · Cited by 40
“These primary complexes are connected through a larger network of secondary interactions to multiple tetraspanin family members, other transmembrane molecules and signaling enzymes [3,13,37].”
BackgroundProductive HIV-1 infection of tissue macrophages by fusion with infected CD4+ T cells
Mascarau, R., Woottum, M., Fromont, L., Gence, R., Cantaloube-Ferrieu, V., Vahlas, Z., Lévêque, K., Bertrand, F., Beunon, T., Métais, A., et al. (2023) · The Journal of Cell Biology · doi:10.1083/jcb.202205103 · Cited by 41
“As tetraspanins are organized in membrane microdomains, CD81 could trap proteins involved in cell fusion, such as integrins among others (Dufrancais et al., 2021; Hemler, 2005).”
Devbhandari, R. P., Shi, G., Ke, A., Wu, F., Huang, X., Wang, X., Shi, Y., Ding, Z., Xu, Y., Dai, Z., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024901 · Cited by 39
“Our results also showed that the integrin b1 subunit often forms structural complexes with the CD151 and integrin a subunit, in line with a previous report [9].”
BackgroundResultInfluentialUsardi, A., Iyer, K., Sigoillot, S. M., Dusonchet, A., & Selimi, F. (2016) · Developmental Neurobiology · doi:10.1002/dneu.22412 · Cited by 39
Lee, J., Byun, H.-J., Lee, M.-S., Jin, Y., Jeoung, D., Kim, Y., & Lee, H. (2016) · Oncotarget · doi:10.18632/oncotarget.13767 · Cited by 39
“Several tetraspanin proteins have been suggested to regulate the matrix-binding affinity, signaling activity, and membrane trafficking of the associated integrins in the multi-molecular TEM structure [1, 4, 35].”
MiR-124 aggravates failing hearts by suppressing CD151-facilitated angiogenesis in heart
Zhao, Y., Yan, M., Chen, C., Gong, W., Yin, Z., Li, H., Fan, J., Zhang, X. A., Wang, D. W., & Zuo, H. (2018) · Oncotarget · doi:10.18632/oncotarget.24205 · Cited by 39
“CD151, a tetraspanin protein family member, is associated tightly with integrins (α3β1, α6β1, α6β4 and α7β1), and thereby modulates integrin-dependent cell morphology, migration, signaling, and adhesion strength [37].”
Rops, A. L. W. M. M., Jansen, E., van der Schaaf, A., Pieterse, E., Rother, N., Hofstra, J. M., Dijkman, H. B. P. M., van de Logt, A.-E., Wetzels, J. F. M., van der Vlag, J., et al. (2018) · Kidney International · doi:10.1016/j.kint.2018.01.005 · Cited by 42
Anderson, K. R., Singer, R. A., Balderes, D. A., Hernandez‐Lagunas, L., Johnson, C. W., Artinger, K., & Sussel, L. (2011) · Development · doi:10.1242/dev.058693 · Cited by 39
“TEMs have been shown to function as signaling centers crucial for adhesion, migration and proliferation (Hemler, 2005; Hemler, 2008; Yunta and Lazo, 2003).”
BackgroundVjugina, U., Zhu, X., Oh, E., Bracero, N. J., & Evans, J. P. (2009) · Biology of Reproduction · doi:10.1095/biolreprod.108.075275 · Cited by 39
Targeting tetraspanins in cancer
Sala-Valdés, M., Ailane, N., Greco, C., Rubinstein, E., & Boucheix, C. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2012.712688 · Cited by 38
“Finally, other tetraspanin partners which are being investigated as potential targets are EWI-2, which affects cell spreading/invasion on T-leukaemic cells and in vivo tumour growth in glioblastoma cells [17,103], and EWIF, due to the potent in vivo tumour-induced angiogenesis and tumour growth inhibition of a truncat…”
BackgroundInfluentialCD9 Is Critical for Cutaneous Wound Healing through JNK Signaling
Zhang, J., Dong, J., Gu, H., Yu, S. S. B., Zhang, X., Gou, Y., Xu, W., Burd, A. R., Huang, L., Miyado, K., et al. (2011) · Journal of Investigative Dermatology · doi:10.1038/jid.2011.268 · Cited by 38
The dual role of tetraspanin CD63 in HIV-1 replication
Li, G., Endsley, M. A., Somasunderam, A., Gbota, S. L., Mbaka, M. I., Murray, J. L., & Ferguson, M. R. (2014) · Virology Journal · doi:10.1186/1743-422x-11-23 · Cited by 37
“CD63 is a type II cellular membrane protein belonging to the tetraspanin superfamily [12,13].”
BackgroundLee, S. E. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.06.004 · Cited by 37
Extracellular Vesicle Release Promotes Viral Replication during Persistent HCV Infection
Aydın, Y., Köksal, A. R., Reddy, V., Lin, D., Osman, H., Heidari, Z., Rhadhi, S. M., Wimley, W. C., Parsi, M. A., & Dash, S. (2021) · Cells · doi:10.3390/cells10050984 · Cited by 38
“Tetraspanins (TSPAN) CD9, CD63, and CD81 are enriched in the membrane of exosomes, which are often used as exosomal markers [31].”
BackgroundMetastasis Suppressors and Their Roles in Breast Carcinoma
Vaidya, K. S., & Welch, D. R. (2007) · Journal of Mammary Gland Biology and Neoplasia · doi:10.1007/s10911-007-9049-1 · Cited by 38
“superfamily which includes 32 known members in mammals alone [41].”
BackgroundReyes, R., Monjas, A., Yáñez‐Mó, M., Cardeñes, B., Morlino, G., Gilsanz, Á., Machado-Pineda, Y., Lafuente, E. M., Monk, P. N., Sánchez‐Madrid, F., et al. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.05.018 · Cited by 37
“Tetraspanin–integrin interactions seem to be consistently mediated through the variable region of the LEL domain of tetraspanins [8,20,35,79]; in this regard our pull-down experiments with a recombinant construct corresponding to the CD9 LEL-domain indicate that the”
The effect of cell–ECM adhesion on signalling via the ErbB family of growth factor receptors
Alexi, X., Berditchevski, F., & Odintsova, E. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390568 · Cited by 37
Multispectral imaging reveals the tissue distribution of tetraspanins in human lymphoid organs
de Winde, C. M., Zuidscherwoude, M., Vasaturo, A., van der Schaaf, A., Figdor, C. G., & van Spriel, A. B. (2015) · Histochemistry and Cell Biology · doi:10.1007/s00418-015-1326-2 · Cited by 37
“Tetraspanin-enriched microdomains (TEM) are functional multimolecular complexes in the plasma membrane (Rubinstein et al. 1996; Hemler 2005; Yanez-Mo et al. 2009; Charrin et al. 2014) in which tetraspanins interact with each other and with partner molecules, like transmembrane immunoreceptors,…”
The tetraspanin CD81 mediates the growth and metastases of human osteosarcoma
Mizoshiri, N., Shirai, T., Terauchi, R., Tsuchida, S., Mori, Y., Hayashi, D., Kishida, T., Arai, Y., Mazda, O., Nakanishi, T., et al. (2019) · Cellular Oncology · doi:10.1007/s13402-019-00472-w · Cited by 38
“In addition, it has been suggested that CD81 may regulate mitosis [9] and enhance the motility and metastatic potential of hepatocarcinoma and malignant melanoma cells [10, 11].”
Ping-Pong—Tumor and Host in Pancreatic Cancer Progression
Mu, W., Wang, Z., & Zöller, M. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.01359 · Cited by 37
“The latter accounts for dimerization and association with non-tetraspanin molecules (200, 201).”
BackgroundGonzález‐Méndez, L., Gradilla, A., Sánchez‐Hernández, D., González, E., Aguirre‐Tamaral, A., Jiménez‐Jiménez, C., Guerra, M., Aguilar, G., Andrés, G., Falcón‐Pérez, J. M., et al. (2020) · The EMBO Journal · doi:10.15252/embj.2019103629 · Cited by 36
“These mutant conditions resulted in a minor accumulative effect on Ptc (Appendix Fig S5), probably because of the long half-life and functional redundancy of tetraspa-nins (Hemler, 2005; Andreu & Yanez-Mo, 2014).”
Implications for tetraspanin-enriched microdomain assembly based on structures of CD9 with EWI-F
Oosterheert, W., Xenaki, K. T., Neviani, V., Pos, W., Doulkeridou, S., Manshande, J., Pearce, N. M., Kroon-Batenburg, L. M. J., Lutz, M., Henegouwen, P. M. P. V. B. E., et al. (2020) · Life Science Alliance · doi:10.26508/lsa.202000883 · Cited by 37
“Tetraspanins form dynamic platforms termed tetraspanin-enriched microdomains (TEMs), also referred to as the tetraspanin web (Hemler, 2005; Yáñez-Mó et al, 2009; Charrin et al, 2009a).”
BackgroundDogrammatzis, C., Saleh, S., Deighan, C., & Kalamvoki, M. (2020) · Journal of Virology · doi:10.1128/jvi.02357-20 · Cited by 37
Exosome-Mediated Insulin Delivery for the Potential Treatment of Diabetes Mellitus
Rodríguez-Morales, B., Antunes‐Ricardo, M., & González‐Valdez, J. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13111870 · Cited by 37
In silico directed mutagenesis identifies the CD 81/claudin‐1 hepatitis C virus receptor interface
Davis, C., Harris, H. J., Hu, K., Drummer, H. E., McKeating, J. A., Mullins, J. G. L., & Balfe, P. (2012) · Cellular Microbiology · doi:10.1111/cmi.12008 · Cited by 37
“CD81 was the first cellular protein identified to bind HCV and is a member of the tetraspanin family of proteins that are widely expressed and involved in multiple biological functions, including cell proliferation and cell–cell adhesion (Hemler, 2005).”
BackgroundMembrane Compartment Occupied by Can1 (MCC) and Eisosome Subdomains of the Fungal Plasma Membrane
Douglas, L. M., Wang, H. X., Li, L., & Konopka, J. B. (2011) · Membranes · doi:10.3390/membranes1040394 · Cited by 37
“Also, Sur7 and Nce102 share interesting similarity to mammalian tetraspanner proteins that play key roles in PM organization, including Claudin proteins at tight junctions and Tetraspanin-enriched domains in lymphocytes [17,74–76].”
BackgroundJiang, X., Zhang, D., Teng, M., Zhang, Q., Zhang, J.-P., & Huang, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077806 · Cited by 36
“Although originally identified in the cells derived from the hematopoietic lineage, CD9 is also constitutively expressed in a diverse variety of other cell types [2,3] to facilitate various cellular and physiological processes, including cell motility [4], migration and adhesion [5,6].”
BackgroundEnhancing integrin function by VEGF/neuropilin signaling
Goel, H. L., & Mercurio, A. M. (2012) · Cell Adhesion & Migration · doi:10.4161/cam.22419 · Cited by 36
“Another facet of integrin regulation is their ability to associate with a variety of cell surface proteins including growth factor receptors(6) and tetraspanins.(7) Such interactions regulate integrin affinity, localization and trafficking.”
BackgroundWang, H., Kolesnikova, T. V., Denison, C., Gygi, S. P., & Hemler, M. E. (2011) · Journal of Cell Science · doi:10.1242/jcs.085449 · Cited by 36
“These protein– protein interactions underlie the assembly of structural and functional units called tetraspanin-enriched microdomains (TEMs) (Espenel et al., 2008; Hemler, 2005; Nydegger et al., 2006; YanezMo et al., 2009).”
BackgroundSelf-citationTetraspanin CD151 Promotes Initial Events in Human Cytomegalovirus Infection
Hochdorfer, D., Florin, L., Sinzger, C., & Lieber, D. (2016) · Journal of Virology · doi:10.1128/jvi.00145-16 · Cited by 36
Ventress, J. K., Partridge, L. J., Read, R. C., Cozens, D., MacNeil, S., & Monk, P. N. (2016) · PLoS ONE · doi:10.1371/journal.pone.0160387 · Cited by 36
“TEM have been implicated in many cell functions, including cell adherence and fusion, membrane trafficking, endocytosis, leukocyte adherence and motility but can also be exploited by protozoa, viruses and bacteria as gateways for infection [3, 4].”
BackgroundTetraspanin microdomains control localized protein kinase C signaling in B cells
Zuidscherwoude, M., Dunlock, V.-M. E., van den Bogaart, G., van Deventer, S. J., van der Schaaf, A., van Oostrum, J., Goedhart, J., Hout, J. I. ’., Hämmerling, G. J., Tanaka, S., et al. (2017) · Science Signaling · doi:10.1126/scisignal.aag2755 · Cited by 36
“By organizing membrane proteins such as integrins and signaling receptors, tetraspanins are implicated in diverse cellular processes, including cell adhesion and activation (10, 14, 15).”
BackgroundChaiyadet, S., Krueajampa, W., Hipkaeo, W., Plosan, Y., Piratae, S., Sotillo, J., Smout, M. J., Sripa, B., Brindley, P. J., Loukas, A. C., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-13527-5 · Cited by 35
Tetraspanin-enriched microdomains regulate digitation junctions
Huang, C., Fu, C., Wren, J. D., Wang, X., Zhang, F., Zhang, Y. H., Connell, S. A., Chen, T., & Zhang, X. A. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2803-2 · Cited by 36
“Considering that DJs mark dynamic contacts between cells and that tetraspanins interact with cadherin, claudin, and IgSF protein [5, 6], DJs reflect the transition processes before the establishment or after the disassembly of stable cell–cell junctions, such as adherens and tight junctions, and, therefore, serve as a…”
InfluentialYu, J., Ji, X. S., Wang, X., Li, T., Wang, H., & Zeng, Q. (2019) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2018.12.075 · Cited by 36
Gerber, H., Mosser, S., Boury‐Jamot, B., Stumpe, M., Piersigilli, A., Goepfert, C., Dengjel, J., Albrecht, U., Magara, F., & Fraering, P. C. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0660-3 · Cited by 36
Proteomic markers of low and high fertility bovine spermatozoa separated by Percoll gradient
D’Amours, O., Calvo, E. L., Bourassa, S., Vincent, P., Blondin, P., & Sullivan, R. (2019) · Molecular Reproduction and Development · doi:10.1002/mrd.23174 · Cited by 36
“Tetraspanin complexes form microdomains, termed tetraspanin‐enriched membrane (TEM) domains (Hemler, 2005), and are implicated in various biological processes such as membrane fusion, cell adhesion, or protein trafficking (Berditchevski & Odintsova, 2007; Fanaei et al., 2011).”
BackgroundPrognostic value and multifaceted roles of tetraspanin CD9 in cancer
Ondruššek, R., Kvokačková, B., Kryštofová, K., Brychtová, S., Souček, K., & Bouchal, J. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1140738 · Cited by 36
“Tetraspanins generally form tetraspanin-enriched microdomains (TEMs) in cell membranes.”
BackgroundInfluentialAlvares, S. M., Dunn, C. A., Brown, T. A., Wayner, E. A., & Carter, W. G. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.01.010 · Cited by 36
DeSalle, R., Marés, R., & García‐España, A. (2010) · Molecular Phylogenetics and Evolution · doi:10.1016/j.ympev.2010.02.015 · Cited by 36
“…depends upon their ability to form large integrated signaling complexes or tetraspanin-enriched microdomains by their primary association with multiple transmembrane and intracellular signaling/cytoskeletal proteins, and secondary associations with themselves (Hemler, 2005; Levy and Shoham, 2005).”
Pharmacological Modulation of AMPAR Rescues Intellectual Disability-Like Phenotype in Tm4sf2−/y Mice
Murru, L., Vezzoli, E., Longatti, A., Ponzoni, L., Falqui, A., Folci, A., Moretto, E., Bianchi, V., Braida, D., Sala, M., et al. (2017) · Cerebral Cortex · doi:10.1093/cercor/bhx221 · Cited by 36
“Structurally, these proteins are characterized by 4 transmembrane domains, 2 extracellular loops and short intracellular N- and C- termini (Hemler 2005).”
BackgroundWang, Y., Tong, X., Omoregie, E. S., Liu, W., Meng, S., & Ye, X. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.390401 · Cited by 35
“It is well established that tetraspanins interact with multiple immune-related molecules, including immune receptors, integrins, and signaling molecules, and function as important immune response modulators (11, 12).”
BackgroundRoschzttardtz, H., Paéz-Valencia, J., Dittakavi, T., Jali, S., Reyes, F. C., Baisa, G. A., Anne, P., Gissot, L., Palauqui, J., Masson, P., et al. (2014) · PLANT PHYSIOLOGY · doi:10.1104/pp.114.246314 · Cited by 35
“VCC proteins also share similarities with TETRASPANIN (TET) proteins, which consist of 200 to 350 amino acids and contain several conserved Cys residues and four transmembrane domains with polar amino acid residues (Hemler, 2005).”
BackgroundReimann, R., Kost, B., & Dettmer, J. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.00545 · Cited by 35
“…domains, membrane bound proteases and intracellular signaling molecules (Little et al., 2004; Andre et al., 2006; Le Naour et al., 2006) thereby forming distinct tetraspanin-enriched microdomains (TEMs) that function as mobile signaling hubs within membranes (Hemler, 2005; Yáñez-Mó et al., 2009).”
BackgroundInfluentialExosomes: Fighting Cancer With Cancer
Alyamani, H., Obeid, M. A., Tate, R. J., & Ferro, V. A. (2018) · Therapeutic Delivery · doi:10.4155/tde-2018-0051 · Cited by 35
Russell, J. C., Merrihew, G. E., Robbins, J. E., Postupna, N. O., Kim, T.-K., Golubeva, A., Noori, A., Wang, K., Keene, C. D., MacCoss, M. J., et al. (2020) · GeroScience · doi:10.1007/s11357-020-00204-1 · Cited by 33
EpCAM proteolysis and release of complexed claudin-7 repair and maintain the tight junction barrier
Higashi, T., Saito, A. C., Fukazawa, Y., Furuse, M., Higashi, A. Y., Ono, M., & Chiba, H. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202204079 · Cited by 35
Inoué, S., Kondo, S., Parichy, D. M., & Watanabe, M. (2013) · Pigment Cell & Melanoma Research · doi:10.1111/pcmr.12192 · Cited by 36
“We further show that dali encodes Tetraspanin 3c, a member of the tetraspanin superfamily (Hemler, 2003, 2005; Zoller, 2009) expressed by melanophores and xanthophores.”
BackgroundFunctional Consequences of Interactions between FAK and Epithelial Membrane Protein 2 (EMP2)
Morales, S. A., Mareninov, S., Coulam, P., Wadehra, M., Goodglick, L., Braun, J. G., & Gordon, L. K. (2009) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.08-3315 · Cited by 35
“Tetraspan proteins have been shown to participate in the formation of a variety of complexes to form the so-called tetraspan web,(41,42) which is the creation of scaffolds and membrane domains that regulate signaling and sorting processes.(41,43) These complexes can modulate the signaling, trafficking, and structural…”
Targeting the tetraspanin CD81 blocks monocyte transmigration and ameliorates EAE
Dijkstra, S., Kooij, G., Verbeek, R., van der Pol, S. M. A., Amor, S., Geisert, E. E., Dijkstra, C. D., van Noort, J. M., & de Vries, H. E. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.05.018 · Cited by 35
“The LEL contains an absolutely conserved CCG motif along with two additional cysteine residues that together contribute to crucial disulphide bonds within the LEL (Hemler, 2005).”
BackgroundInfluentialThe glycoprotein CD147 defines miRNA‐enriched extracellular vesicles that derive from cancer cells
Ko, S. Y., Lee, W., Weigert, M., Jonasch, E. W., Lengyel, E. R., & Naora, H. (2023) · Journal of Extracellular Vesicles · doi:10.1002/jev2.12318 · Cited by 35
“Tetraspanins act as membrane-organizing scaffolds by engaging with one another and other membrane proteins and protrude only 4–5 nm from the membrane (Hemler, 2005; Kitadokoro et al., 2001).”
Oxygen-Generating Biomaterials for Translational Bone Regenerative Engineering
Hosseini, F. S., Abedini, A. A., Chen, F., Whitfield, T., Ude, C. C., & Laurencin, C. T. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c20715 · Cited by 35
Migrasomes: Biogenesis, physiological roles, and therapeutic potentials
Jiao, H., & Yu, L. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202403051 · Cited by 34
“Tetraspanins, which are transmembrane proteins with four domains, organize into tetraspanin-enriched microdomains (TEMs) within the membrane, each ∼ 100 nm across (Charrin et al., 2009; Hemler, 2005).”
BackgroundOkamoto, T., Iwata, S., Yamazaki, H., Hatano, R., Komiya, E., Dang, N. H., Ohnuma, K., & Morimoto, C. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086671 · Cited by 34
“Despite proposed differences in the biochemical properties and molecular contents of TEM and lipid raft [24,41], it should be noted that CD26 has been preferentially detected in TEM of metastatic colon cancer cells [30], data which partially support our present findings.”
BackgroundResultInfluentialVpu Is the Main Determinant for Tetraspanin Downregulation in HIV-1-Infected Cells
Lambelé, M., Koppensteiner, H., Symeonides, M., Roy, N. H., Chan, J., Schindler, M., & Thali, M. (2015) · Journal of Virology · doi:10.1128/jvi.03719-14 · Cited by 34
Yin, M., Soikkeli, J., Jahkola, T., Virolainen, S., Saksela, O., & Hölttä, E. (2014) · American Journal Of Pathology · doi:10.1016/j.ajpath.2013.11.020 · Cited by 35
Understanding lipid rafts and other related membrane domains
Neumann, A. K., Itano, M. S., & Jacobson, K. (2010) · F1000 Biology Reports · doi:10.3410/b2-31 · Cited by 34
“Tetraspanins, a widely expressed and highly conserved class of transmembrane proteins (reviewed in [34]), form tetraspanin-enriched microdomains (TEMs) through lateral tetraspanin-tetraspanin interactions and binding to non-tetraspanin membrane proteins.”
BackgroundExpression and function of CD9 in melanoma cells
Fan, J., Zhu, G., & Niles, R. M. (2009) · Molecular Carcinogenesis · doi:10.1002/mc.20580 · Cited by 34
“In mammals, there are at least 32 members of the tetraspanin family [5,6].”
BackgroundMutations in the TSPAN12 Gene in Japanese Patients with Familial Exudative Vitreoretinopathy
Kondo, H., Kusaka, S., Yoshinaga, A., Uchio, E., Tawara, A., Hayashi, K., & Tahira, T. (2011) · American Journal of Ophthalmology · doi:10.1016/j.ajo.2010.11.026 · Cited by 34
Han, J., Reddig, K. R., & Li, H. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601929 · Cited by 34
“Sun is a member of the tetraspanin family that have been implicated in cell adhesion, motility, invasion and prolifera- tion (Hemler, 2005).”
Zhang, N., Zuo, L., Zheng, H., Li, G., & Hu, X. (2018) · Medical Science Monitor · doi:10.12659/msm.911612 · Cited by 34
“Tetraspanin-enriched microdomains can form in the cell membrane with their partner proteins, including integrins and immunoglobulins, to regulate cell adhesion, migration, and invasion and through these mechanisms, tetraspanins also play a role in tumor progression [4,5].”
BackgroundMigrasome biogenesis: when biochemistry meets biophysics on membranes
Wang, D., & Yu, L. (2024) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.06.004 · Cited by 33
Microdomains in the membrane landscape shape antigen-presenting cell function
Zuidscherwoude, M., de Winde, C. M., Cambi, A., & van Spriel, A. B. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.0813440 · Cited by 33
“Interestingly, some tetraspanins contain a PDZ domain binding motif in their C-terminal tail, which facilitates the anchoring of transmembrane proteins to the cytoskeleton, and hold together signaling complexes, thus providing a direct way to sequester components of a signaling cascade to TEMs [24, 76].”
BackgroundInhibition of Tetraspanin Functions Impairs Human Papillomavirus and Cytomegalovirus Infections
Fast, L. A., Mikuličić, S., Fritzen, A., Schwickert, J., Boukhallouk, F., Hochdorfer, D., Sinzger, C., Suárez, H., Monk, P. N., Yáñez‐Mó, M., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103007 · Cited by 33
“They are structurally conserved harboring four transmembrane domains, three intracellular domains as well as a small and a large extracellular loop [7] [8] [9] [10] [11] .”
BackgroundFloren, M., Cruz, S. R., Termini, C. M., Marjon, K. D., Lidke, K. A., & Gillette, J. M. (2020) · Oncogene · doi:10.1038/s41388-020-1261-0 · Cited by 33
Dancing with Trojan horses: an interplay between the extracellular vesicles and viruses
Badierah, R., Uversky, V. N., & Redwan, E. M. M. M. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1756409 · Cited by 34
“…by the addition of palmitate resulting in the formation at the cell surface of the ‘tetraspanin web’, or ‘tetraspanin platforms’, or ‘tetraspanin-enriched microdomains’ (TEMs) containing several tetraspanins and associated components (Berditchevski et al., 2002; Hemler, 2005; Levy & Shoham, 2005).”
BackgroundAlonso-Gardón, M., Elorza‐Vidal, X., Castellanos, A., Sala, G. L., Armand‐Ugón, M., Gilbert, A., Pietro, C. D., Pla-Casillanis, A., Ciruela, F., Gasull, X., et al. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddab155 · Cited by 33
“Tetraspanins are transmembrane proteins that span the plasma membrane four times and that associate with other tetraspanins by homo-and heterooligomerization (59).”
Thölmann, S., Seebach, J., Otani, T., Florin, L., Schnittler, H., Gerke, V., Furuse, M., & Ebnet, K. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04140-5 · Cited by 33
“Since Tspan-mediated interactions are often sensitive to Triton X-100 or NP40-based lysis conditions [39, 41], our observation that the interaction of JAM-A with α3β1 integrin is sensitive to NP40-based lysis but detectable in Brij98-based lysis buffers suggested that the JAM-A–α3β1 integrin interaction is indirect an…”
BackgroundRoles of the interactions between Env and Gag proteins in the HIV‐1 replication cycle
Murakami, T. (2008) · Microbiology and Immunology · doi:10.1111/j.1348-0421.2008.00008.x · Cited by 33
“Members of this family form large integrated complexes for signal transduction and immune response called ‘tetraspanin-enriched microdomains (TEM)’ in association with various molecules (83).”
BackgroundImhof, I., Gasper, W. J., & Derynck, R. (2008) · Journal of Cell Science · doi:10.1242/jcs.021717 · Cited by 33
“…antigen with a molecular mass of 24-27 kDa on lympho-hemopoietic cells (Kersey et al., 1981), CD9 is also widely expressed on non-hematopoietic tissues and has been implicated in a variety of biological functions including motility (Garcia-Lopez et al., 2005; Hemler, 2005; Longhurst et al., 2002).”
BackgroundProteomic Analysis of Lipid Raft-Like Detergent-Resistant Membranes of Lens Fiber Cells
Wang, Z., & Schey, K. L. (2015) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.15-18273 · Cited by 32
“In addition, almost all tetraspanins are modified by the posttranslational addition of palmitate to membrane-proximal cysteine residues.(57) Palmitoylation of MP20 has not been reported, but CSS-Palm software(58) predicts palmitoylation of cysteine 11 in MP20.”
BackgroundExtracellular vesicles – biogenesis, composition, function, uptake and therapeutic applications
Petrovčíková, E., Vičíková, K., & Leksa, V. (2018) · Biologia · doi:10.2478/s11756-018-0047-0 · Cited by 34
“Many of them interact with integrins (Hemler 2005).”
Milstein, M. L., Cavanaugh, B. L., Roussey, N. M., Volland, S., Williams, D. S., & Goldberg, A. F. X. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912513117 · Cited by 32
CD37 in B Cell Derived Tumors—More than Just a Docking Point for Monoclonal Antibodies
Bobrowicz, M., Kubacz, M., Ślusarczyk, A., & Winiarska, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249531 · Cited by 32
“Tetraspanins, the so-called transmembrane-four superfamily proteins (TM4SF), are a large family of evolutionarily conserved proteins present on the cell surface and intracellular vesicles [1].”
BackgroundTSPAN1, a novel tetraspanin member highly involved in carcinogenesis and chemoresistance
Garcia‐Mayea, Y., Mir, C., Carballo-Perich, L., Sánchez-García, A., Bataller, M., & LLeonart, M. E. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188674 · Cited by 32
Zhou, Z., Yang, Z., Zhou, L., Yang, M., & He, S. (2023) · Cell & Bioscience · doi:10.1186/s13578-023-00995-8 · Cited by 32
“However, the structure and function of ECL1 and ICL have remained unclear so far [4].”
BackgroundThe role of MPP1/p55 and its palmitoylation in resting state raft organization in HEL cells
Biernatowska, A., Podkalicka, J., Majkowski, M., Hryniewicz‐Jankowska, A., Augoff, K., Kozak, K., Korzeniewski, J., & Sikorski, A. F. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.03.009 · Cited by 32
“Since palmitoylation has been reported previously to be involved in regulation of membraneprotein clustering, such as tetraspanin [48,49] or GABAA receptors [50], and has also been shown to promote oligomerization of certain proteins [11,51], we speculate that palmitoylated MPP1 in erythroid cells plays a role in raft…”
BackgroundThe Tetraspanins CD9 and CD81 Regulate CD9P1-Induced Effects on Cell Migration
Chambrion, C., & Naour, F. L. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011219 · Cited by 32
“Likewise, the tetraspanin CD63 associates specifically with H,K-ATPase [26] whereas CD151 associates directly with the integrins a3b1, a6b1, a7b1 and a6b4 [2,16,27].”
BackgroundMosser, S., Alattia, J., Dimitrov, M. I., Matz, A., Pascual, J., Schneider, B. L., & Fraering, P. C. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu449 · Cited by 33
“TSPAN6 belongs to the tetraspanin superfamily of multi-pass membrane proteins interacting with multiple immune-related molecules, including immune receptors, integrins, signaling molecules and functioning as important immune response modulators (16).”
BackgroundTetraspanins and Transmembrane Adaptor Proteins As Plasma Membrane Organizers—Mast Cell Case
Hálová, I., & Dráber, P. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00043 · Cited by 33
“In some cases, mice lacking a particular tetraspanin mimicked the phenotype observed in humans with a defect in the same tetraspanin (Hemler, 2005).”
BackgroundOligomerization of the Tetraspanin CD81 via the Flexibility of Its δ -Loop
Schmidt, T. H., Homsi, Y., & Lang, T. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.05.003 · Cited by 32
Seipold, L., Daμμe, M., Prox, J., Rabe, B., Kašpárek, P., Sedláček, R., Altmeppen, H. C., Willem, M., Boland, B., Glatzel, M., et al. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.11.003 · Cited by 32
“Such tetraspanin enriched microdomains [5] organize a spatial arrangement of membrane proteins thereby affecting biological processes like cell adhesion, signaling, endocytosis and proteolysis [5,1,33,34].”
BackgroundThe CD9, CD81, and CD151 EC2 domains bind to the classical RGD-binding site of integrin αvβ3
Yu, F., Lee, C.-Y., Changou, C. A., Cedano-Prieto, D. M., Takada, Y. K., & Takada, Y. (2016) · Biochemical Journal · doi:10.1042/bcj20160998 · Cited by 32
Lee, M., Lee, J., Kim, Y., & Lee, H. (2019) · The Prostate · doi:10.1002/pros.23837 · Cited by 32
Babich, V., Knipe, L., Hewlett, L. J., Meli, A., Dempster, J., Hannah, M. J., & Carter, T. D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809235200 · Cited by 32
Cryo-electron Microscopic Analysis of Single-Pass Transmembrane Receptors
Cai, K., Zhang, X., & Bai, X. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.1c01035 · Cited by 31
Extracellular Vesicles as Drug Delivery System for Cancer Therapy
Wang, J., Yin, B., Lian, J., & Wang, X. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16081029 · Cited by 33
“The tetraspanins superfamily proteins are involved in organizing membrane microdomains, specifically tetraspanin-enriched microdomains (TEMs), by clustering and interacting with a wild variety of transmembrane and cytosolic signaling proteins [245].”
BackgroundTetraspanin 1 is involved in survival, proliferation and carcinogenesis of pancreatic cancer
Hou, F.-Q., LEI, X.-F., Yao, J.-L., Wang, Y., & Zhang, W. (2015) · Oncology Reports · doi:10.3892/or.2015.4272 · Cited by 31
Tetraspanin CD 63 acts as a pro‐metastatic factor via β‐catenin stabilization
Seubert, B., Cui, H., Simonavicius, N., Honert, K., Schafer, S. L., Reuning, U., Heikenwälder, M. F., Mari, B. P., & Krüger, A. (2014) · International Journal of Cancer · doi:10.1002/ijc.29296 · Cited by 31
“Tetraspanins are involved in many biological processes, including cell adhesion, migration, cell fusion, as well as signal transduction by interacting with partner molecules.(9,10) The family member CD63 is of special interest as it is found to be upregulated in patients suffering from breast cancer,(12) astrocytoma(1…”
BackgroundWu, M., Baumgart, T., Hammond, S., Holowka, D., & Baird, B. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.007260 · Cited by 31
MHC Class II and CD9 in Human Eosinophils Localize to Detergent-Resistant Membrane Microdomains
Akuthota, P., Melo, R. C. N., Spencer, L. A., & Weller, P. F. (2011) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2010-0335oc · Cited by 31
“However, unlike lipid rafts, TEMs generally appear to be soluble in stronger detergents, such as Triton X-100 (28, 30).”
BackgroundInfluential
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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