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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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Expression and Function of Tetraspanins and Their Interacting Partners in B Cells
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“Based on the sensitivity and stringency to different detergents, the interactions of tetraspanins and partners in TEM were classified into three categories (13, 14).”
BackgroundA dynamic interaction between CD19 and the tetraspanin CD81 controls B cell co-receptor trafficking
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Tspan8 and CD151 promote metastasis by distinct mechanisms
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“Tet-raspanins connect with a multitude of transmembrane and cytosolic molecules in glycolipid-enriched membrane domains (TEM) [27].”
RetractedAberrant Underexpression of CD81 in Precursor B-Cell Acute Lymphoblastic Leukemia
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“Tetraspanin enriched membrane micro-domains (TEMs) comprising tetraspanin complexes act as platforms for signalling transduction [12, 79, 80].”
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“Structurally, tetraspanins have four transmembrane segments, one small and one large extracellular loop (domain EC1 and EC2, respectively) and short cytoplasmic N- and C-terminal domains.(11,12) The human 228-amino acid protein CD9 holds a potential N-glycosylation site located in the EC1 domain.”
BackgroundTetraspanins CD9 and CD151 at the immune synapse support T‐cell integrin signaling
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“Tetraspanin Interactions Numerous cis-interactions occur between tetraspanins and neighboring plasma membrane proteins within what are known as tetraspanin-enriched microdomains (Hemler, 2005).”
BackgroundInfluentialTetraspanin CD151 Regulates Glycosylation of α3β1 Integrin
Baldwin, G., Novitskaya, V., Sądej, R., Pocheć, E., Lityń́ska, A., Hartmann, C., Williams, J., Ashman, L. K., Eble, J. A., & Berditchevski, F. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806394200 · Cited by 63
TM4SF3 promotes esophageal carcinoma metastasis via upregulating ADAM12m expression
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Recruitment of CD63 to Cryptococcus neoformans phagosomes requires acidification
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“This is due in part to the fact that both claudins and tetraspanins are palmitoylated, which promotes their partitioning into membrane microdomains and assembly into higher order structures.(14,15,19) Tetraspanins have been found to promote the trafficking and assembly of several classes of proteins, most notably inte…”
BackgroundInfluentialSaito, Y., Tachibana, I., Takeda, Y., Yamane, H., He, P., Suzuki, M., Minami, S., Kijima, T., Yoshida, M., Kumagai, T., et al. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-1131 · Cited by 63
“Rather, the capability of process extension in SCLC may depend on multiple factors, and based on the established concept that CD9 indirectly associates with integrins in tetraspanin-enriched microdomains (8), CD9 presumably acts as modulator of cytoskeletal reorganization.”
Backgroundvon Lersner, A. K., Fernandes, F., Ozawa, P. M. M., Jackson, M., Masureel, M., Ho, H., Lima, S. M., Vagner, T., Sung, B. H., Wehbe, M., et al. (2024) · ACS Nano · doi:10.1021/acsnano.3c11561 · Cited by 65
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“The main regions of conservation between TSP-12 and these apparent human orthologs are in the intracellular loop and in the second extracellular loop, the location of many protein–protein interaction sites (7).”
Molecular characterization of the apical organ of the anthozoan Nematostella vectensis
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“…to its nontetraspanin partner (either directly or indirectly) without involvement of another tetraspanin, from secondary/tertiary tetraspanin interactions, in which the tetraspanin interacts with its nontetraspanin partner through another tetraspanin (Boucheix and Rubinstein, 2001; Hemler, 2005).”
InfluentialMechanisms of integrin αVβ5 clustering in flat clathrin lattices
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Alternative invasion pathways for plasmodium berghei sporozoites
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A stigmatic gene confers interspecies incompatibility in the Brassicaceae
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Fusions involving protein kinase C and membrane-associated proteins in benign fibrous histiocytoma
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Helminth infection–induced malignancy
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CD20 and CD37 antibodies synergize to activate complement by Fc-mediated clustering
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“It has previously been described that membrane proteins can cluster into lipid rafts or tetraspanin-enriched microdomains (TEM), enabling efficient signal transduction.(38,39) We hypothesized that the synergistic interactions in CDC between CD20 and CD37 mAbs could be driven by clustering of both target-bound mAbs int…”
BackgroundSerum exosomal microRNA-34a as a potential biomarker in epithelial ovarian cancer
Maeda, K., Sasaki, H., Ueda, S., Miyamoto, S., Terada, S., Konishi, H., Kogata, Y., Ashihara, K., Fujiwara, S., Tanaka, Y., et al. (2020) · Journal of Ovarian Research · doi:10.1186/s13048-020-00648-1 · Cited by 61
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“In the animal kingdom they function as organizers of multimolecular membrane complexes and regulate, amongst others, cell migration, fusion and signaling events [28].”
BackgroundA novel therapeutic strategy with anti-CD9 antibody in gastric cancers
Nakamoto, T., Murayama, Y., Oritani, K., Boucheix, C., Rubinstein, E., Nishida, M., Katsube, F., Watabe, K., Kiso, S., Tsutsui, S., et al. (2009) · Journal of Gastroenterology · doi:10.1007/s00535-009-0081-3 · Cited by 60
“Tetraspanins can act as molecular facilitators or adaptors, which organize a network of interactions among the cell surface molecules, known as the ‘‘tetraspanin web’’ or tetraspanenriched microdomains [7, 8].”
BackgroundICAM-1 Clustering on Endothelial Cells Recruits VCAM-1
van Buul, J. D., van Rijssel, J., van Alphen, F. P. J., van Stalborch, A.-M. D., Mul, E. P. J., & Hordijk, P. L. (2010) · BioMed Research International · doi:10.1155/2010/120328 · Cited by 60
“A platform for protein complexes is an efficient way to control and merge several signalling pathways [18–20].”
BackgroundTetraspanin CD37 protects against the development of B cell lymphoma
de Winde, C. M., Veenbergen, S., Young, K. H., Xu-Monette, Z. Y., Wang, X., Xia, Y., Jabbar, K. J., van den Brand, M., van der Schaaf, A., Elfrink, S., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci81041 · Cited by 65
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“Exosomes were isolated from the cell culture supernatant according to a previously established ultracentrifugation method [38, 39].”
Smart exosomes enhance PDAC targeted therapy
Creeden, J. F., Sevier, J., Zhang, J., Lapitsky, Y., Brunicardi, F. C., Jin, G., Nemunaitis, J. J., Liu, J., Nestor‐Kalinoski, A. L., Rao, D., et al. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2024.02.037 · Cited by 62
TM4SF1: a tetraspanin-like protein necessary for nanopodia formation and endothelial cell migration
Zukauskas, A., Merley, A., Li, D., Ang, L., Sciuto, T. E., Salman, S., Dvořàk, A. M., Dvorak, H. F., & Jaminet, S.-C. S. (2011) · Angiogenesis · doi:10.1007/s10456-011-9218-0 · Cited by 59
“as a ‘molecular organizer’, modulating cell motility and directional migration [1].”
InfluentialAbnormal Placental Development and Early Embryonic Lethality in EpCAM-Null Mice
Nagao, K., Zhu, J., Heneghan, M. B., Hanson, J. C., Morasso, M. I., Tessarollo, L., Mackem, S., & Udey, M. C. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008543 · Cited by 59
“Enrichment of EpCAM in tetraspanin enriched microdomains (TEMs) that contain b1-integrins, CD44v, claudins and tetraspanins [11–13] is also consistent with the concept that EpCAM is involved in intercellular adhesion, but TEM-associated proteins have also been implicated in cell signaling and more complex processes in…”
BackgroundArnaud, M.-P., Vallée, A., Robert, G., Bonneau, J., Roy, C. L., Varin‐Blank, N., Rio, A.-G., Troadec, M., Galibert, M., & Gandemer, V. (2015) · Blood · doi:10.1182/blood-2015-02-628560 · Cited by 59
Molecular responses of Ostrea edulis haemocytes to an in vitro infection with Bonamia ostreae
Morga, B., Arzul, I., Faury, N., Segarra, A., Chollet, B., & Renault, T. (2010) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2010.10.005 · Cited by 59
Coffey, G., Rajapaksa, R., Liu, R., Sharpe, O., Kuo, C.-C., Krauss, S. W., Sagi, Y., Davis, R. E., Staudt, L. M., Sharman, J. P., et al. (2009) · Journal of Cell Science · doi:10.1242/jcs.045658 · Cited by 61
“…†Stanford University, School of Medicine, Division of Immunology and Rheumatology, GRECC Veterans Affairs Palo Alto Health Care System, Palo Alto CA, 94304, USA ‡Life Sciences Division, University of California Lawrence Berkeley National Laboratory, Bldg 74, 1 Cyclotron Rd, Berkeley, CA 94720, USA.”
BackgroundTetraspanins: Host Factors in Viral Infections
New, C. S., Lee, Z.-Y., Tan, K. S., Wong, A. H., Wang, D. Y., & Tran, T. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111609 · Cited by 62
“Owing to the hydrophobic TM domains, tetraspanins can establish unique platforms at the cell surface, known as tetraspanin-enriched microdomains (TEMs) [1,3], allowing for lateral associations with partner proteins, including laminin-binding integrins, adhesion molecules, growth factor receptors, metalloproteinases, i…”
BackgroundInfluentialThe Extracellular δ-Domain is Essential for the Formation of CD81 Tetraspanin Webs
Homsi, Y., Schloetel, J.-G., Scheffer, K. D., Schmidt, T. H., Destainville, N., Florin, L., & Lang, T. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.05.028 · Cited by 58
“In some cases, the classification level 1 has also been used to refer to direct interactions (also including direct tetraspanin-tetraspanin interactions that are disrupted by strong detergents), whereas level 2 refers to secondary interactions via palmitate residues (3).”
BackgroundResultMolecular Characterization of a Tetraspanin from the Human Liver Fluke, Opisthorchis viverrini
Piratae, S., Tesana, S., Jones, M. K., Brindley, P. J., Loukas, A. C., Lovas, E. M., Eursitthichai, V., Sripa, B., Thanasuwan, S., & Laha, T. (2012) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0001939 · Cited by 56
“contain 4 transmembrane domains and are frequently expressed at the cell surface in association with each other and with other molecules, such as integrins, where they function to regulate cell adhesion, migration, proliferation, and differentiation [12,13].”
BackgroundPorts, M. O., Nagle, R. B., Pond, G. D., & Cress, A. E. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-0354 · Cited by 58
“The ability to block α6 integrin cleavage by extracellular engagement of the receptor points to the possibility that lateral membrane associations with surface-expressed proteins, such as tetraspanins (51, 52) and uPA receptor (uPAR; refs.”
Berthier‐Vergnes, O., Kharbili, M. E., de la Fouchardière, A., Pointecouteau, T., Verrando, P., Wierinckx, A., Lachuer, J., Naour, F. L., & Lamartine, J. (2010) · British Journal of Cancer · doi:10.1038/sj.bjc.6605994 · Cited by 64
“TSPAN8 encodes tetraspanin 8, also known as CO-029, a transmembrane protein overexpressed in numerous carcinomas (Boucheix et al, 2001; Hemler, 2005; Zöller, 2009).”
BackgroundInfluentialA tetraspanin regulates septate junction formation in Drosophila midgut
Izumi, Y., Motoishi, M., Furuse, K., & Furuse, M. (2016) · Journal of Cell Science · doi:10.1242/jcs.180448 · Cited by 58
“Tetraspanins are believed to play a role in membrane compartmentalization and are involved in many biological processes, including cell migration, cell fusion and lymphocyte activation, as well as viral and parasitic infections (Charrin et al., 2014, 2009; Hemler, 2005; Yanez-Mo et al., 2009).”
InfluentialVahidnezhad, H., Youssefian, L., Saeidian, A. H., Mahmoudi, H., Touati, A., Abiri, M., Kajbafzadeh, A. M., Aristodemou, S., Liu, L., McGrath, J. A., et al. (2017) · Matrix Biology · doi:10.1016/j.matbio.2017.11.003 · Cited by 60
“Tetraspanin CD151 is widely distributed in different tissues, including epithelium, endothelium, muscle, renal glomeruli and proximal and distal tubules [15].”
BackgroundChemokine Decoy Receptors: Structure–Function and Biological Properties
Bonecchi, R., Savino, B., Borroni, E. M., Mantovani, A., & Locati, M. (2010) · Current topics in microbiology and immunology · doi:10.1007/82_2010_19 · Cited by 58
“sis and metastatic progression, revealing that it is a metastasis-suppressor protein (Hemler 2005).”
BackgroundOverexpression of CD151 as an adverse marker for intrahepatic cholangiocarcinoma patients
Huang, X., Ke, A., Shi, G., Ding, Z., Devbhandari, R. P., Gu, F., Li, Q., Dai, Z., Zhou, J., & Fan, J. (2010) · Cancer · doi:10.1002/cncr.25485 · Cited by 57
“To date, different types of membrane proteins (including growth factor receptors; integrins; immunoglobulin domains; and glutamic acid, tryptophan, isoleucine [EWI] motifcontaining protein F [a subfamily of immunoglobulin proteins]) have been identified in TEMs.(5,9,12,22) Moreover, functions of these membrane protein…”
BackgroundInfluentialGlioblastoma Inhibition by Cell Surface Immunoglobulin Protein EWI-2, In Vitro and In Vivo
Kolesnikova, T. V., Kazarov, A. R., Lemieux, M. E., Lafleur, M. A., Kesari, S., Kung, A. L., & Hemler, M. E. (2009) · Neoplasia · doi:10.1593/neo.81180 · Cited by 57
“…growth factor receptor ligand binding activities of the membrane-bound forms of transforming growth factor α and heparin-binding EGF-like growth factor [9,10], two molecules that contribute to human malignant glioma cell growth, most likely through juxtacrine and autocrine mechanisms [6,11,12].”
BackgroundSelf-citationZhang, F., Michaelson, J., Moshiach, S., Sachs, N., Zhao, W., Sun, Y., Sonnenberg, A., Lahti, J. M., Huang, H., & Zhang, X. A. (2011) · Blood · doi:10.1182/blood-2011-03-339531 · Cited by 57
Delandre, C., Penabaz, T., Passarelli, A. L., Chapes, S. K., & Clem, R. J. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.03.013 · Cited by 57
“Tetraspanins are relatively small proteins and have been described as “often hidden by a canopy of tall glycoprotein neighbors in the cell membrane” [1].”
BackgroundGartlan, K. H., Wee, J. L. K., Demaria, M. C., Nastovska, R., Chang, T. M., Jones, E. L., Apostolopoulos, V., Pietersz, G. A., Hickey, M. J., van Spriel, A. B., et al. (2013) · European Journal of Immunology · doi:10.1002/eji.201242730 · Cited by 57
Clarin-1, Encoded by the Usher Syndrome III Causative Gene, Forms a Membranous Microdomain
Tian, G., Zhou, Y., Hájková, D., Miyagi, M., Dinculescu, A., Hauswirth, W. W., Palczewski, K., Geng, R., Alagramam, K. N., Isosomppi, J., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.003160 · Cited by 61
Cooperation between integrin α5 and tetraspan TM4SF5 regulates VEGF-mediated angiogenic activity
Choi, S., Lee, S.-A., Kwak, T., Kim, H. J., Lee, M. J., Ye, S., Kim, S., Kim, S., & Lee, S. E. (2008) · Blood · doi:10.1182/blood-2008-05-160671 · Cited by 57
Regulation of the trafficking and the function of the metalloprotease ADAM10 by tetraspanins
Saint‐Pol, J., Eschenbrenner, E., Dornier, E., Boucheix, C., Charrin, S., & Rubinstein, E. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160296 · Cited by 57
Beyond adhesion: emerging roles for integrins in control of the tumor microenvironment
Longmate, W. M., & DiPersio, C. M. (2017) · F1000Research · doi:10.12688/f1000research.11877.1 · Cited by 57
Mazurov, D. V., Heidecker, G., & Derse, D. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607322200 · Cited by 57
CD81 marks immature and dedifferentiated pancreatic β-cells
Salinno, C., Büttner, M., Cota, P., Tritschler, S., Tarquis-Medina, M., Bastidas-Ponce, A., Scheibner, K., Burtscher, I., Böttcher, A., Theis, F. J., et al. (2021) · Molecular Metabolism · doi:10.1016/j.molmet.2021.101188 · Cited by 54
“Tetraspanins are membrane proteins that comprise four transmembrane domains, a small and large extracellular loop and short carboxyl and amino cytoplasmic termini [23].”
Backgroundde Monasterio‐Schrader, P., Patzig, J., Möbius, W., Barrette, B., Wagner, T. L., Kusch, K., Edgar, J. M., Brophy, P., & Werner, H. B. (2013) · Glia · doi:10.1002/glia.22561 · Cited by 58
Molecular Basis of Leukocyte–Endothelium Interactions During the Inflammatory Response
Barreiro, O., & Sánchez‐Madrid, F. (2009) · Revista Española de Cardiología (English Edition) · doi:10.1016/s1885-5857(09)71837-7 · Cited by 56
Deletion of Tetraspanin CD9 Diminishes Lymphangiogenesis in Vivo and in Vitro
Iwasaki, T., Takeda, Y., Maruyama, K., Yokosaki, Y., Tsujino, K., Tetsumoto, S., Kuhara, H., Nakanishi, K., Otani, Y., Jin, Y., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.424291 · Cited by 56
“Although numerous molecules have been reported to associate with tetraspanins, CD9/EWI-F, CD151/ 3 1, and CD81/CD19 have been regarded as primary partners (20).”
BackgroundRetroviral matrix and lipids, the intimate interaction
Hamard-Péron, É., & Muriaux, D. M. (2011) · Retrovirology · doi:10.1186/1742-4690-8-15 · Cited by 64
“They form tetraspanin-enriched microdomains (TEMs) or tetraspanin webs, in close relation with the cytoskeleton (reviewed in [153]).”
BackgroundPalmer, T. D., Martínez, C. H., Vásquez, C., Hebron, K. E., Jones‐Paris, C. R., Arnold, S. A., Chan, S. M., Chalasani, V., Gomez-Lemus, J. A., Williams, A. K., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-0275 · Cited by 56
Molecular mechanisms of resistance to Rituximab and pharmacologic strategies for its circumvention
Stolz, C., & Schüler, M. (2009) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428190902878471 · Cited by 56
“This 37 kDa phosphoprotein belongs to the tetraspanin protein family MS4A (membrane spanning 4A), whose members are known to form oligomeric complexes within the cell membrane [13,16,17].”
BackgroundMunkley, J., McClurg, U. L., Livermore, K. E., Ehrmann, I. E., Knight, B., McCullagh, P. J., McGrath, J. S., Crundwell, M. C., Harries, L. W., Leung, H. Y., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-05489-5 · Cited by 53
Jean, C., Haghighirad, F., Zhu, Y., Chalbi, M., Ziyyat, A., Rubinstein, E., Gourier, C., Yip, P. S. F., Wolf, J., Lee, J. E., et al. (2018) · Human Reproduction · doi:10.1093/humrep/dey340 · Cited by 56
“CD9, an integral membrane protein belonging to tetraspanin super- family (TM4), is expressed by a wide variety of cells (Hemler, 2005; Levy and Shoham, 2005; Charrin et al., 2014).”
BackgroundCurrent Understanding of Extracellular Vesicle Homing/Tropism
Edelmann, M. J., & Kima, P. E. (2022) · Zoonoses · doi:10.15212/zoonoses-2022-0004 · Cited by 56
“Of the 33 tetraspanins in the human genome, several have been shown to localize to small EVs [32-34].”
BackgroundStructural basis for membrane-proximal proteolysis of substrates by ADAM10
Lipper, C. H., Egan, E. D., Gabriel, K.-H., & Blacklow, S. C. (2023) · Cell · doi:10.1016/j.cell.2023.06.026 · Cited by 60
Harlow, D. E., Saul, K. E., Komuro, H., & Macklin, W. B. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.5151-14.2015 · Cited by 55
“In addition, many tetraspanins also associate with intracellular signaling molecules, such as phosphatidylinositol kinases and PKC (Hemler, 2005).”
BackgroundChi, Y. H., Salzman, R. A., Balfe, S., Ahn, J., Sun, W., Moon, J., Yun, D., Lee, S. Y., Higgins, T. J. V., Pittendrigh, B. R., et al. (2008) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2008.00854.x · Cited by 55
“…to collagen transcripts, dietary scN repressed cadherin, syntenin, tetraspanin, tensin and LIM domain proteins, important in cell–cell contact, adhesion and motility (Godt & Tepass, 1998; Zimmermann et al. , 2001; Broday et al. , 2004; Gimferrer et al. , 2005; Hemler, 2005; Sayed et al. , 2007).”
BackgroundPhosphatidylinositol 4-kinases, phosphatidylinositol 4-phosphate and cancer
Waugh, M. G. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.06.009 · Cited by 58
“both the signalling and trafficking of tetraspanin proteins [70–72].”
BackgroundBari, R., Zhang, Y. H., Zhang, F., Wang, N. X., Stipp, C. S., Zheng, J., & Zhang, X. A. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2009.080685 · Cited by 55
Tetraspanins in the humoral immune response
van Spriel, A. B. (2011) · Biochemical Society Transactions · doi:10.1042/bst0390512 · Cited by 55
Zumaquero, E., Muñoz, P., Cobo, M., Lucena, G., Pavón, E. J., Algíbez, A. M., Navarro, P., García-Pérez, A., Ariza, A., Malavasi, F., et al. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.05.032 · Cited by 55
From Normal Skin to Squamous Cell Carcinoma: A Quest for Novel Biomarkers
Voiculescu, V. M., Calenic, B., Ilie, M. A., Lupu, M., Căruntu, A., Moraru, L., Voiculescu, S. E., Ion, A., Greabu, M., Ishkitiev, N., et al. (2016) · Disease Markers · doi:10.1155/2016/4517492 · Cited by 55
“Other proteins involved in skin carcinogenesis are cell surface markers such as tetraspanins, found on virtually all cell types [50].”
BackgroundDriehuis, E., & Clevers, H. C. (2017) · British Journal of Pharmacology · doi:10.1111/bph.13758 · Cited by 55
“Tetraspanins are four-transmembrane proteins that cluster together and serve as signalling platforms on the membrane (Hemler, 2005).”
BackgroundTetraspanins as Organizers of Antigen-Presenting Cell Function
Sáiz, M. L., Rocha‐Perugini, V., & Sánchez‐Madrid, F. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01074 · Cited by 62
“Proc Natl Acad Sci U S A (2017) 114(8):1988–93.”
BackgroundOverexpression of tetraspanins affects multiple myeloma cell survival and invasive potential
Tohami, T., Drucker, L., Shapiro, H., Radnay, J., & Lishner, M. (2007) · The FASEB Journal · doi:10.1096/fj.06-6610com · Cited by 55
“Despite accumulating data that underscore the functional importance and increasing prominence of the tetraspanins, most family members do not carry out typical cellsurface receptor-ligand binding functions and the full extent of their modulation remains unclear (4, 5).”
BackgroundRegulation of hemidesmosome dynamics and cell signaling by integrin α6β4
Molder, L. T., de Pereda, J. M., & Sonnenberg, A. (2021) · Journal of Cell Science · doi:10.1242/jcs.259004 · Cited by 54
Tetraspanins and cell membrane tubular structures
Zhang, X. A., & Huang, C. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-0954-0 · Cited by 56
“These observations are also consistent with the involvement of tetraspanin in viral entry and release [5].”
BackgroundResultInfluentialThe Tetraspanin CD151 Is Required for Met-dependent Signaling and Tumor Cell Growth
Franco, M., Muratori, C., Corso, S., Tenaglia, E., Bertotti, A., Capparuccia, L., Trusolino, L., Comoglio, P. M., & Tamagnone, L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145417 · Cited by 54
The Neurobiology of X-Linked Intellectual Disability
Bassani, S., Zapata, J., Gerosa, L., Moretto, E., Murru, L., & Passafaro, M. (2013) · The Neuroscientist · doi:10.1177/1073858413493972 · Cited by 56
Bissinger, B. W., Donohue, K. V., Khalil, S. M. S., Grozinger, C. M., Sonenshine, D. E., Zhu, J., & Roe, R. M. (2011) · Insect Molecular Biology · doi:10.1111/j.1365-2583.2011.01086.x · Cited by 54
“These proteins are regulators of cell invasion, fusion, morphology, motility and signalling (reviewed by Hemler, 2005).”
BackgroundImmune Targeting of Tetraspanins Involved in Cell Invasion and Metastasis
Vences-Catalán, F., & Levy, S. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01277 · Cited by 52
“Biochemically, very few of these complexes are held together when solubilized by harsh detergents, the majority only withstand mild detergents (31).”
BackgroundImaging of plasmacytoid dendritic cell interactions with T cells
Mittelbrunn, M., del Hoyo, G. M., López‐Bravo, M., Martin-Cofreces, N. B., Scholer, A., Hugues, S., Fetler, L., Amigorena, S., Ardavı́n, C., & Sánchez‐Madrid, F. (2008) · Blood · doi:10.1182/blood-2008-02-139865 · Cited by 54
Curley, N., Levy, D. H., Mai, A., Brown, A. K., Stickney, Z., Marriott, G., & Lü, B. (2020) · Nanoscale · doi:10.1039/d0nr00362j · Cited by 55
Zhou, J., Wang, A., Cai, T., Li, Y., Du, W., Zhang, Y., Zhang, R., Zhang, W., Zhu, J., Zeng, Y., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04928-0 · Cited by 53
“CD151 usually regulates laminin-binding integrins and controls tumour cell invasion and metastasis through their effects on adhesive and signal transduction functions [13].”
BackgroundKAI-1/CD82, the molecule and clinical implication in cancer and cancer metastasis.
Malik, F. A., Sanders, A. J., & Jiang, W. G. (2009) · PubMed · doi:10.14670/hh-24.519 · Cited by 53
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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