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Tetraspanin functions and associated microdomains

Hemler, Martin E.·2005·Nature Reviews Molecular Cell Biology

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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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Background
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Background
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Background
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Background
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Background
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“Tetraspanins are abundantly expressed by EVs in raft-like structures within their plasma membrane and are generally involved in adhesion, displacement, fusion, activation and proliferation (Hemler, 2005; Andreu and Yanez-Mo, 2014).”
Background
A High Level of TM4SF5 Is Associated with Human Esophageal Cancer Progression and Poor Patient Survival
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“Tetraspanins are a large family of proteins grouped according to structural relatedness [6].”
Background
Overexpression of CD151 Predicts Prognosis in Patients with Resected Gastric Cancer
Yang, Y., Zhang, Z., Liu, Q., Sun, Y., Yu, J., & Xu, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058990 · Cited by 20
“They display numerous properties indicative of their physiological importance in cell adhesion, motility, activation and proliferation, as well as their contribution to pathological conditions such as metastasis and pathologic angiogenesis [6,7,8].”
Background
Lipid domains in HIV-1 assembly
Yandrapalli, N., Muriaux, D. M., & Favard, C. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00220 · Cited by 24
“TEM has been shown to co-localize with Gag in T cells (Jolly and Sattentau, 2007; Grigorov et al., 2009) and tetraspanin components are found to be incorporated into HIV-1 particles, especially CD81 (Grigorov et al., 2009).”
BackgroundInfluential
Down-Regulation of CD9 Expression and its Correlation to Tumor Progression in B Lymphomas
Yoon, S.-O., Zhang, X., Freedman, A. S., Zahrieh, D., Lossos, I. S., Li, L., & Choi, Y. S. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.100048 · Cited by 20
Isolation and Analysis of Detergent-Resistant Membrane Fractions
Aureli, M., Grassi, S., Sonnino, S., & Prinetti, A. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3170-5_10 · Cited by 20
Crystallization of the human tetraspanin protein CD9
Umeda, R., Nishizawa, T., & Nureki, O. (2019) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x1801840x · Cited by 20
“…other functional proteins, such as adhesion proteins, cell growth factor receptors and intracellular scaffold proteins, and organize a ‘tetraspanin-enriched microdomain’ (TEM) where tetraspanins and their ‘partner proteins’ form signaling platforms in cells (Hemler, 2005; Yáñez-Mó et al., 2009).”
Background
Selenite and methylseleninic acid epigenetically affects distinct gene sets in myeloid leukemia: A genome wide epigenetic analysis
Khalkar, P., Abdulkadir, H., Codó, P., Díaz-Argelich, N., Martikainen, A., Arzenani, M. K., Lehmann, S., Walfridsson, J., Ungerstedt, J. S., & Fernandes, A. P. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.02.014 · Cited by 19
“CD9, a tetraspanin protein, has been implicated in various physiological processes like motility, adhesion and fertilization [41] and plays a critical role in tumor progression and metastasis [42–44].”
Background
Tetraspanin CD82 is necessary for muscle stem cell activation and supports dystrophic muscle function
Hall, A. J., Fontelonga, T. M., Wright, A., Gwilt, K. B., Widrick, J. J., Pasut, A., Villa, F., Miranti, C. K., Gibbs, D. E., Jiang, E., et al. (2020) · Skeletal Muscle · doi:10.1186/s13395-020-00252-3 · Cited by 19
“Tetraspanins are a heterogeneous and ubiquitous group of membrane-bound proteins that regulate a variety of physiological processes, from stem cell function to tissue regeneration and cancer progression [2, 4, 5].”
Background
Emerging Role of Extracellular Vesicles in Biomarking the Gastrointestinal Diseases
Heydari, R., Abdollahpour‐Alitappeh, M., Shekari, F., & Meyfour, A. (2021) · Expert Review of Molecular Diagnostics · doi:10.1080/14737159.2021.1954909 · Cited by 21
Recruitment of Tetraspanin TSP-15 Regulates Plasma Membrane Repair in C. elegans Epidermis
Wang, Y., Yang, Q., Meng, X., Wijaya, C. S., Ren, X., & Xu, S. (2021) · Developmental Cell · doi:10.1016/j.devcel.2022.06.004 · Cited by 20
Acute toxic effects of diclofenac exposure on freshwater crayfish (Procambarus clarkii): Insights from hepatopancreatic pathology, molecular regulation and intestinal microbiota
Zhang, Y. X., Li, Z., Zhang, Y., Sun, K., Ren, N., & Li, M. (2022) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2022.114068 · Cited by 19
Tumor-Derived Small Extracellular Vesicles Involved in Breast Cancer Progression and Drug Resistance
Feng, L., Guo, L., Tanaka, Y., & Su, L. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315236 · Cited by 19
The tetraspanin CD53 protects stressed hematopoietic stem cells via promotion of DREAM complex–mediated quiescence
Greenberg, Z. J., Paracatu, L. C., Monlish, D. A., Dong, Q., Rettig, M. P., Roundy, N., Gaballa, R., Li, W., Yang, W., Luke, C. J., et al. (2022) · Blood · doi:10.1182/blood.2022016929 · Cited by 18
CD81 Controls Immunity to Listeria Infection through Rac-Dependent Inhibition of Proinflammatory Mediator Release and Activation of Cytotoxic T Cells
del Hoyo, G. M., Ramírez‐Huesca, M., Levy, S., Boucheix, C., Rubinstein, E., de la Escalera, M. M., González-Cintado, L., Ardavı́n, C., Veiga, E., Yáñez‐Mó, M., et al. (2015) · The Journal of Immunology · doi:10.4049/jimmunol.1402957 · Cited by 19
Viruses and Tetraspanins: Lessons from Single Molecule Approaches
Dahmane, S., Rubinstein, E., & Milhiet, P. (2014) · Viruses · doi:10.3390/v6051992 · Cited by 19
“, the integrin α3ß1 or α6ß1), CD9 or CD81 with EWI-2 or EWI-F/CD9P-1, or Tspan5, Tspan14, Tspan15 with ADAM10 [45,46].”
BackgroundInfluential
Identification of novel antigens within the Schistosoma japonicum tetraspanin family based on molecular characterization
Wu, W., Cai, P., Chen, Q., & Wang, H. (2011) · Acta Tropica · doi:10.1016/j.actatropica.2011.01.001 · Cited by 19
Egg CD9 protein tides correlated with sperm oscillations tune the gamete fusion ability in mammal
Ravaux, B., Favier, S., Perez, É., & Gourier, C. (2018) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjy005 · Cited by 19
On the structure–function of MHC class II molecules and how single amino acid polymorphisms could alter intracellular trafficking
Thibodeau, J., Moulefera, M. A., & Balthazard, R. (2018) · Human Immunology · doi:10.1016/j.humimm.2018.10.001 · Cited by 18
Exosomal miRNA: an alternative mediator of cell-to-cell communication
Li, J., Jiang, X., & Wang, K. (2019) · ExRNA · doi:10.1186/s41544-019-0025-x · Cited by 20
Tetraspanins are involved in Burkholderia pseudomallei-induced cell-to-cell fusion of phagocytic and non-phagocytic cells
Sangsri, T., Saiprom, N., Tubsuwan, A., Monk, P. N., Partridge, L. J., & Chantratita, N. (2020) · Scientific Reports · doi:10.1038/s41598-020-74737-y · Cited by 19
Establishing Clonal Cell Lines with Endothelial-Like Potential from CD9hi, SSEA-1− Cells in Embryonic Stem Cell-Derived Embryoid Bodies
Lian, Q., Yeo, K. Y. B., Que, J., Tan, E. K. W., Yu, F., Yin, Y., Salto‐Tellez, M., Oakley, R. M. E., & Lim, S. K. (2006) · PLoS ONE · doi:10.1371/journal.pone.0000006 · Cited by 19
“Tetraspanins play important roles in numerous various signalling events that affect proliferation, apoptosis, cell morphology, motility and tumour progression[34,35].”
Background
In situ chemical cross-linking on living cells reveals CD9P-1 cis-oligomer at cell surface
André, M., Chambrion, C., Charrin, S., Soave, S., Chaker, J., Boucheix, C., Rubinstein, E., & Naour, F. L. (2009) · Journal of Proteomics · doi:10.1016/j.jprot.2009.08.005 · Cited by 19
Tetraspanin proteins in membrane remodeling processes
Dharan, R., & Sorkin, R. (2024) · Journal of Cell Science · doi:10.1242/jcs.261532 · Cited by 18
“…to their mode of action and are thought to play a major role in membrane compartmentalization by forming TSPAN-enriched microdomains (TEMs) (Hemler, 2005; Le Naour et al., 2006; Charrin et al., 2009; Yáñez-Mó et al., 2009; Charrin et al., 2014; Zuidscherwoude et al., 2015; van Deventer et…”
Analysis of 30 chromosome-level Drosophila genome assemblies reveals dynamic evolution of centromeric satellite repeats
Gebert, D., Hay, A. D., Hoang, J. P., Gibbon, A. E., Henderson, I. R., & Teixeira, F. K. (2025) · Genome biology · doi:10.1186/s13059-025-03527-4 · Cited by 19
“Another example is provided by a cluster of Tetraspanin genes ( Tsp42Ea-r ) on the C element, of which little is known beyond the fact that these genes encode transmembrane proteins implicated in cell–cell interactions and signalling pathway regulation [53, 54].”
CD9 regulates keratinocyte differentiation and motility by recruiting E-cadherin to the plasma membrane and activating the PI3K/Akt pathway
Jiang, X., Teng, M., Ji, R., Zhang, D., Zhang, Z., Lv, Y., Zhang, Q., Zhang, J., & Huang, Y. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2019.118574 · Cited by 18
Pubertal down-regulation of Tetraspanin 8 in testicular Sertoli cells is crucial for male fertility
Pradhan, B. S., Bhattacharya, I., Sarkar, R. K., & Majumdar, S. S. (2020) · Molecular Human Reproduction · doi:10.1093/molehr/gaaa055 · Cited by 18
An Overview of Exosomes in Cancer Therapy: A Small Solution to a Big Problem
Rodrigues, P., Melim, C., Veiga, F., & Figueiras, A. (2020) · Processes · doi:10.3390/pr8121561 · Cited by 19
“Regarding their lipid composition, exosomes have resemblances with lipid rafts [15,32]—microdomains expressed at the PM with elevated content of sphingolipids, cholesterol, and phospholipids [33].”
Background
CD82 protects against glaucomatous axonal transport deficits via mTORC1 activation in mice
Ye, M., Huang, J., Mou, Q., Luo, J., Hu, Y., Lou, X., Yao, K., Zhao, B., Duan, Q., Li, X., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04445-6 · Cited by 19
A peptide binding to the tetraspanin CD9 reduces cancer metastasis
Suwatthanarak, T., Ito, K., Tanaka, M., Sugiura, K., Hoshino, A., Miyamoto, Y., Miyado, K., & Okochi, M. (2023) · Biomaterials Advances · doi:10.1016/j.bioadv.2023.213283 · Cited by 18
Single‐Cell RNA Transcriptome of the Human Endometrium Reveals Epithelial Characterizations Associated with Recurrent Implantation Failure
Zhang, H., Zhang, C., & Zhang, S. (2023) · Advanced Biology · doi:10.1002/adbi.202300110 · Cited by 18
Microscopic clusters feature the composition of biochemical tetraspanin-assemblies and constitute building-blocks of tetraspanin enriched domains
Schmidt, S. C., Massenberg, A., Homsi, Y., Sons, D., & Lang, T. (2024) · Scientific Reports · doi:10.1038/s41598-024-52615-1 · Cited by 18
Rim formation is not a prerequisite for distribution of cone photoreceptor outer segment proteins
Conley, S. M., Al‐Ubaidi, M. R., Han, Z., & Naash, M. I. (2014) · The FASEB Journal · doi:10.1096/fj.14-251397 · Cited by 18
“A primary role of tetraspanins as a protein family is the organization of functional membrane microdomains (9, 37), and RDS may play a similar role in the photoreceptor.”
Background
Interspecies differences in protein expression do not impact the spatiotemporal regulation of glycoprotein VI mediated activation
Dunster, J. L., Unsworth, A. J., Bye, A. P., Haining, E. J., Sowa, M. A., Di, Y., Sage, T., Pallini, C., Pike, J. A., Hardy, A. T., et al. (2019) · Journal of Thrombosis and Haemostasis · doi:10.1111/jth.14673 · Cited by 18
Expression of CD9 and CD82 in clear cell renal cell carcinoma and its clinical significance
Kwon, H. J., Min, S. Y., Park, M. J., Lee, C., Park, J. H., Chae, J. Y., & Moon, K. C. (2014) · Pathology - Research and Practice · doi:10.1016/j.prp.2014.01.004 · Cited by 18
Differential functions of phospholipid binding and palmitoylation of tumour suppressor EWI2/PGRL
He, B., Zhang, Y. H., Richardson, M. M., Zhang, J. S., Rubinstein, E., & Zhang, X. A. (2011) · Biochemical Journal · doi:10.1042/bj20101381 · Cited by 19
The first transmembrane region of the β-chain stabilizes the tetrameric FcɛRI complex
Singleton, T. E., Platzer, B., Dehlink, E., & Fiebiger, E. (2009) · Molecular Immunology · doi:10.1016/j.molimm.2009.03.023 · Cited by 19
“Alternatively, a truly trimeric FcεRI could reside in tetraspanin-enriched microdomains (Hemler, 2003;Hemler, 2005;Levy and Shoham, 2005b).”
Normal viability of Kai1/Cd82 deficient mice
Risinger, J. I., Custer, M. C., Feigenbaum, L., Simpson, R. J., Hoover, S. B., Webster, J. D., Chandramouli, G. V. R., Tessarollo, L., & Barrett, J. C. (2013) · Molecular Carcinogenesis · doi:10.1002/mc.22009 · Cited by 18
Tetraspan proteins: regulators of renal structure and function
Caplan, M. J., Kamsteeg, E.-J., & Duffield, A. S. (2007) · Current Opinion in Nephrology & Hypertension · doi:10.1097/mnh.0b013e328177b1fa · Cited by 18
Migrasomes, critical players in intercellular communication
Tan, Z., Yang, C., Fu, S., Wu, J., Huang, Y., Li, H., Gong, C., Lv, D., Wang, J., Ding, M., et al. (2025) · Cancer Cell International · doi:10.1186/s12935-025-03754-6 · Cited by 17
“The TSPAN family comprises 33 members, which are ubiquitously expressed in various cell types and possess four transmembrane domains [23, 24].”
Natural Killer Cell Group 7 Sequence in Cytotoxic Cells Optimizes Exocytosis of Lytic Granules Essential for the Perforin-Dependent, but Not Fas Ligand–Dependent, Cytolytic Pathway
Morikawa, Y., Murakami, M., Kondo, H. G., Nemoto, N., Iwabuchi, K., & Eshima, K. (2021) · ImmunoHorizons · doi:10.4049/immunohorizons.2100029 · Cited by 17
Coronaviruses, cholesterol and statins: Involvement and application for Covid-19
Orlowski, S., Mourad, J., Gallo, A., & Bruckert, É. (2021) · Biochimie · doi:10.1016/j.biochi.2021.06.005 · Cited by 18
“This makes sense since these TEM are known to be enriched in cholesterol [48,49].”

Authors: Hemler, M. E.
Affiliations: Harvard University (US)
Corresponding author: Hemler, Martin E.
ORCID: Hemler, Martin E.
Venue: Nature Reviews Molecular Cell Biology
Publisher: Springer Science and Business Media LLC
Published: 2005-10
Volume: 6
Issue: 10
Pages: 801-811
ISSN: 1471-0072 (ISSN-L)
1471-0080
DOI: 10.1038/nrm1736
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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Tetraspanin functions and associated microdomains

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