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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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Tetraspanin 5 (TSPAN5), a Novel Gatekeeper of the Tumor Suppressor DLC1 and Myocardin-Related Transcription Factors (MRTFs), Controls HCC Growth and Senescence
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Targeted next-generation sequencing analysis identifies novel mutations in families with severe familial exudative vitreoretinopathy.
Huang, X., Zhuang, H., Wu, J., Li, J., Hu, F., Zheng, Y., Tellier, L. C. A. M., Zhang, S.-H., Gao, F., Zhang, J., et al. (2017) · PubMed Central · Cited by 14
Upregulation of TSPAN12 is associated with the colorectal cancer growth and metastasis.
Liu, J., Chen, C., Li, G., Chen, D., & Zhou, Q. (2017) · Europe PMC (PubMed Central) · Cited by 14
tANCHOR: A Novel Mammalian Cell Surface Peptide Display System
Ivanusic, D., Madela, K., Burghard, H., Holland, G., Laue, M. M., & Bannert, N. (2020) · BioTechniques · doi:10.2144/btn-2020-0073 · Cited by 14
Molecular characterization of a novel tetraspanin from the oyster, Crassostrea ariakensis: Variation, localization and relationship to oyster host defense
Luo, M., Ye, S., Xu, T., Wu, X., & Yang, P. (2012) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2012.05.009 · Cited by 14
“Some members of the tetraspanin superfamily are mostly expressed on the cell surface, while others are also located in intracellular organelles [45].”
Background
Human Immunodeficiency Virus Type 1 Cellular Entry and Exit in the T Lymphocytic and Monocytic Compartments
Aiamkitsumrit, B., Sullivan, N. T., Nonnemacher, M. R., Pirrone, V., & Wigdahl, B. L. (2015) · Advances in virus research · doi:10.1016/bs.aivir.2015.04.001 · Cited by 14
Proteomic Insights Into Gingival Crevicular Extracellular Vesicles in Periodontitis and Gestational Diabetes: An Exploratory Study
Mizgier, M. L., Nardocci, G., Ramı́rez, V., Bendek, M. J., Hernández, M., Rojas, C., Herrera, D., Kantarcı, A., Kemp, M. W., Illanes, S. E., et al. (2024) · Journal Of Clinical Periodontology · doi:10.1111/jcpe.14083 · Cited by 15
TSPAN12 is overexpressed in NSCLC via p53 inhibition and promotes NSCLC cell growth in vitro and in vivo
Hu, Z., Hou, D., Wang, X., You, Z., & Cao, X. (2018) · OncoTargets and Therapy · doi:10.2147/ott.s155620 · Cited by 13
Hepatitis Viruses Control Host Immune Responses by Modifying the Exosomal Biogenesis Pathway and Cargo
Karamichali, E., Foka, P., Papadopoulou, G., Loukaki-Gkountara, D., Andresaki, K., Koskinas, J. S., & Georgopoulou, U. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810862 · Cited by 14
“It was shown that TEMs, together with tetraspanin CD81, play a key role in sorting target receptors and intracellular components toward exosomes [40].”
Background
Tetraspanin Tspan8 restrains interferon signaling to stabilize intestinal epithelium by directing endocytosis of interferon receptor
Min, J., Yang, S., Cai, Y., Vanderwall, D., Wu, Z., Li, S., Liu, S., Liu, B., Wang, J., Ding, Y., et al. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-023-04803-x · Cited by 13
“As a tetraspanin [10, 11], Tspan8 promote the proliferation, migration, invasion, and metastasis of cancer cells from multiple tissue sources, including glioma, melanoma, hepatocarcinoma, and ovarian, gastric, and colorectal cancers [12–17].”
Background
Rice tetraspanins express in specific domains of diverse tissues and regulate plant architecture and root growth
Qin, S., Li, W., Zeng, J., Huang, Y., & Cai, Q. (2023) · The Plant Journal · doi:10.1111/tpj.16536 · Cited by 13
Extracellular vesicles lay the ground for neuronal plasticity by restoring mitochondrial function, cell metabolism and immune balance
Hermann, D. M., Wang, C., Yusuf, A. M., Herz, J., Doeppner, T. R., & Giebel, B. (2025) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x251325039 · Cited by 15
“Tetraspanins are a family of transmembrane proteins which contain four trans-membrane domains and two extracellular loops, 51 among which are the classical exosomal proteins CD9, CD63 and CD81 (Table 1).”
Disease-associated single amino acid mutation in the calf-1 domain of integrin α3 leads to defects in its processing and cell surface expression
Yamada, M., & Sekiguchi, K. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.11.003 · Cited by 13
Breast Cancer Liver Metastasis
Tabariès, S., & Siegel, P. M. (2011) · Cancer metastasis · doi:10.1007/978-94-007-0292-9_10 · Cited by 13
“Indeed, individual tetraspanins have been found in complexes with numerous integrin partners [147, 148].”
Background
Isolation and characterization of cluster of differentiation 9-positive ependymal cells as potential adult neural stem/progenitor cells in the third ventricle of adult rats
Horiguchi, K., Yoshida, S., Hasegawa, R., Takigami, S., Ohsako, S., Katō, T., & Kato, Y. (2019) · Cell and Tissue Research · doi:10.1007/s00441-019-03132-5 · Cited by 13
“…study that D9-positive cells in the third ventricle were immunopositive for Ki67, Hemler et al. reported that the related tetraspanin, CD81, regulates cell motility and proliferation by facilitating the organization of multimolecular membrane complexes, including CD9 and integrins (Hemler 2005).”
Background
Palmitoylated Proteins in Dendritic Spine Remodeling
Albanesi, J. P., Baryłko, B., Demartino, G., & Jameson, D. M. (2020) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2020.00022 · Cited by 13
“Tetraspanins comprise a family of 33 (in mammals) structurally related proteins that play a role in cell adhesion, migration, and proliferation (Hemler, 2005).”
Background
CD9 knockdown suppresses cell proliferation, adhesion, migration and invasion, while promoting apoptosis and the efficacy of chemotherapeutic drugs and imatinib in Ph+ ALL SUP‑B15 cells
Xing, C., Xu, W., Shi, Y., Zhou, B., Wu, D., Liang, B., Zhou, Y., Gao, S., & Feng, J. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11350 · Cited by 13
“cd9 plays crucial roles in a wide range of physiological processes, including cell motility and fertilization (8).”
Background
Cholesterol plays a decisive role in tetraspanin assemblies during bilayer deformations
Caparotta, M., & Masone, D. (2021) · Biosystems · doi:10.1016/j.biosystems.2021.104505 · Cited by 13
Selection and Validation of Reference Genes for RT-qPCR Analysis of Gene Expression in Nicotiana benthamiana upon Single Infections by 11 Positive-Sense Single-Stranded RNA Viruses from Four Genera
Zhang, G., Zhang, Z., Wan, Q., Zhou, H., Jiao, M., Zheng, H., Lu, Y., Rao, S., Wu, G., Chen, J., et al. (2023) · Plants · doi:10.3390/plants12040857 · Cited by 13
“Tetraspanins are a family of small transmembrane proteins that play crucial roles in intracellular transport, cellular signal transduction, and cell migration [32].”
Background
Differential expression microarrays reveal candidate genes potentially associated with reproductive dysfunction of captive-reared prawn Penaeus monodon
Brady, P., Elizur, A., Cummins, S. F., Nguyen, N. H., Williams, R. R., & Knibb, W. (2013) · Aquaculture · doi:10.1016/j.aquaculture.2013.02.038 · Cited by 13
“(Hemler, 2005).”
Background
Channel catfish (Ictalurus punctatus Rafinesque, 1818) tetraspanin membrane protein family: Identification, characterization and expression analysis of CD63 cDNA
Yeh, H., & Klesius, P. H. (2009) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2009.08.006 · Cited by 13
Prognostic significance of Tspan9 in gastric cancer
Feng, T., Sun, L., Qi, W., Pan, F., Lv, J., Guo, J., Zhao, S., Ding, A., & Qiu, W. (2016) · Molecular and Clinical Oncology · doi:10.3892/mco.2016.961 · Cited by 13
CD151 promotes cell metastasis via activating TGF-β1/Smad signaling in renal cell carcinoma
Yu, Y., Liang, C., Wang, S., Zhu, J., Miao, C., Hua, Y., Bao, M., Cao, Q., Qin, C., Shao, P., et al. (2018) · Oncotarget · doi:10.18632/oncotarget.24028 · Cited by 13
“As one of the most important members of the tetraspanin family, CD151 (also known as GP-27, MER 2, PETA-3, SFA-1 or Tspan24) was observed in different cell types [9].”
Background
Engineering of Surface Proteins in Extracellular Vesicles for Tissue-Specific Targeting
Vogt, S., Stadlmayr, G., Grillari, J., Rüker, F., & Wozniak‐Knopp, G. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.83537 · Cited by 13
Gene expression analysis of human prostate cell lines with and without tumor metastasis suppressor CD82
Dodla, P., Bhoopalan, V., Khoo, S. K., Miranti, C. K., & Sridhar, S. (2020) · BMC Cancer · doi:10.1186/s12885-020-07675-7 · Cited by 13
Therapeutic effect of a TM4SF5-specific monoclonal antibody against colon cancer in a mouse model
Kim, Y.-E., Kwon, S., Wu, G. J., Kim, D., Park, B. K., Park, J.-A., Choi, K., Kim, D., Kwon, H., & Lee, Y. (2014) · Oncotarget · doi:10.18632/oncotarget.2311 · Cited by 13
“Tetraspanins, also known as transmembrane 4 superfamily (TM4SF) members, can associate with various molecules such as integrins, membrane receptors, immunoglobulin superfamily proteins, and other tetraspanins to form a multimolecular tetraspanin web [24,25].”
Background
The frataxin-encoding operon of Caenorhabditis elegans shows complex structure and regulation
Vázquez‐Manrique, R. P., González‐Cabo, P., Ortiz‐Martín, I., Ros, S., Baylis, H. A., & Palau, F. (2006) · Genomics · doi:10.1016/j.ygeno.2006.10.007 · Cited by 13
Functional features and protein network of human sperm-egg interaction
Sabetian, S., Shamsir, M. S., & Naser, M. A. (2014) · Systems Biology in Reproductive Medicine · doi:10.3109/19396368.2014.955896 · Cited by 13
“CD9 is a member of the tetraspanin family (so named as members have four transmembrane domains) [Hemler 2005; Rubinstein 2011].”
Background
Substrate-attached materials are enriched with tetraspanins and are analogous to the structures associated with rear-end retraction in migrating cells
Yamada, M., Mugnai, G., Serada, S., Yagi, Y., Naka, T., & Sekiguchi, K. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.25041 · Cited by 13
Joint features and complementarities of Tspan8 and CD151 revealed in knockdown and knockout models
Yue, S., Zhao, K., Erb, U., Rana, S., & Zöller, M. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160298 · Cited by 13
Gangliosides modulate the secretion of extracellular vesicles and their misfolded protein cargo
Monyror, J., Kadam, V., Morales, L. C., Ordóñez, D., Ibanga, J., Zaidi, A. K., McNamara, E., Pink, D., Stenlund, M. J., Reyes, K., et al. (2025) · Science Advances · doi:10.1126/sciadv.ady5212 · Cited by 12
Single-cell and spatial transcriptomic profiling reveals distinct tumor microenvironment dynamics in cervical adenocarcinoma and squamous cell carcinoma
Wu, Y., Wei, B., Wei, Z., Wang, H., Liu, Y., Xu, D., Li, X., Guo, L., Lu, H., & Shang, H. (2025) · Communications Biology · doi:10.1038/s42003-025-09310-2 · Cited by 13
“3b, Supplementary Data 8), the roles of which were controversial in cancer 11,17 .”
Tetraspanin 7 regulates osteoclast function through association with the RANK/αvβ3 integrin complex
Kim, M., Lin, J., Huh, J., Park, J., Go, M., Lee, H., Hwang, D., Kim, H. S., Kim, T. S., Lee, D., et al. (2021) · Journal of Cellular Physiology · doi:10.1002/jcp.30559 · Cited by 12
“TSPANs also interact with cytoskeletal and signaling proteins through their N‐ and C‐terminal cytoplasmic tails (Hemler, 2005).”
BackgroundInfluential
Site- and Structure-Specific Glycosylation Signatures of Bovine, Caprine, Porcine, and Human Milk-Derived Extracellular Vesicles
Wang, X., Li, H., Wang, Z., Chen, J., Chen, W., Zhou, X., Zhang, L., Xu, S., Gao, X., & Yang, G. (2023) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.3c06439 · Cited by 12
Distinct targeting and uptake of platelet and red blood cell‐derived extracellular vesicles into immune cells
Ilvonen, P., Pusa, R., Härkönen, K., Laitinen, S., & Impola, U. (2024) · Journal of Extracellular Biology · doi:10.1002/jex2.130 · Cited by 12
“Both platelets and more recently RBCs have been studied for their immunological effects and interactions with immune cells (Butler, 1989; Caillon et al., 2022; Ebeyer-Masotta et al., 2022; Hemler, 2005; Kowal et al., 2016; Noris & Galbusera, 2023; Weiss et al., 2018; Yan et al., 2023).”
Background
Uroplakins play conserved roles in egg fertilization and acquired additional urothelial functions during mammalian divergence
Liao, Y., Chang, H.-C., Liang, F., Chung, P.-J., Wei, Y., Nguyen, T.-P., Zhou, G., Talebian, S., Krey, L. C., Deng, F.-M., et al. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-08-0496 · Cited by 12
“Notably, UPIa barely colocalized with GM1, a raft marker, indicating that the uroplakin-containing tetraspanin-enriched microdomains, like that of other tetraspanins (Claas et al., 2001; Le Naour et al., 2006), are distinct from the conventional GM1-positive rafts (Figure 5R) (Hemler, 2003, 2005).”
Background
CellectSeq: In silico discovery of antibodies targeting integral membrane proteins combining in situ selections and next-generation sequencing
Kelil, A., Gallo, E., Banerjee, S., Adams, J., & Sidhu, S. S. (2021) · Communications Biology · doi:10.1038/s42003-021-02066-5 · Cited by 12
TSPAN8 regulates EGFR/AKT pathway to enhance metastasis in gastric cancer
Zhang, L., Xu, Y., Cai, E., Zheng, M., Liu, L., Wang, Q., & Li, S. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08662-4 · Cited by 12
“These interactions ultimately lead to the creation of tetraspaninenriched microdomains (TEMs) [7, 8], which are crucial to facilitating the formation and stability of various functional complexes that impact cellular processes including cell migration, invasion, adhesion, differentiation and signal transduction [9, 10…”
Background
Co-occurrence of tetraspanin and ROS generators
Moribe, H., & Mekada, E. (2013) · Worm · doi:10.4161/worm.23415 · Cited by 12
TM4SF3 and AR: A Nuclear Complex that Stabilizes Both Proteins
Bhansali, M., Zhou, J., & Shemshedini, L. (2015) · Molecular Endocrinology · doi:10.1210/me.2015-1075 · Cited by 12
“The limited studies in these tumors have determined that TM4SF3 has metastasis-promoting activities (40).”
Background
Identification of smut-responsive genes in sugarcane using cDNA-SRAP
Huang, N., Zhang, Y. Y., Xiao, X., Huang, L., Wu, Q., Que, Y., & Xu, L. (2015) · Genetics and Molecular Research · doi:10.4238/2015.june.18.23 · Cited by 12
Tetraspanin 8 is an interactor of the metalloprotease meprin β within tetraspanin-enriched microdomains
Schmidt, F., Müller, M., Prox, J., Arnold, P., Schönherr, C., Tredup, C., Minder, P., Ebsen, H., Janßen, O., Annaert, W. G., et al. (2016) · Biological Chemistry · doi:10.1515/hsz-2016-0126 · Cited by 12
“TEMs represent specialized structures providing a signaling platform by which tetraspanins, also called ‘molecular facilitators’, are involved in a variety of different biological processes (Hemler, 2003, 2005).”
Background

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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