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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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“metastasis (Hemler, 2005) AFT activated accompanied by”
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“, galectins), intracellular proteins (clathrin in clathrin-coated pits), or membrane proteins (tetraspanins [8], caveolins [9, 10], flotillins [11]).”
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“In addition, typical raft resident proteins, like GPI-anchored proteins and caveolin do not associate with tetraspanins [15].”
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Lipid Rafts and Alzheimer’s Disease: Protein-Lipid Interactions and Perturbation of Signaling
Hicks, D. A., Nalivaeva, N. N., & Turner, A. J. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00189 · Cited by 213
“They are involved in a whole range of cellular processes, from cell morphology and motility to signaling pathways (Hemler, 2005).”
BackgroundMonti, E., Bonten, E. J., d’Azzo, A., Bresciani, R., Venerando, B., Borsani, G., Schauer, R., & Tettamanti, G. (2010) · Advances in carbohydrate chemistry and biochemistry · doi:10.1016/s0065-2318(10)64007-3 · Cited by 203
Brazzoli, M., Bianchi, A., Filippini, S., Weiner, A. J., Zhu, Q., Pizza, M., & Crotta, S. (2008) · Journal of Virology · doi:10.1128/jvi.00665-08 · Cited by 200
“serves as a scaffold for signaling processes (6, 27, 33).”
BackgroundJolly, C. L., & Sattentau, Q. J. (2007) · Journal of Virology · doi:10.1128/jvi.01845-06 · Cited by 212
“Since tetraspanins are regulators of actin organization (21), we wished to investigate the existence of physical and/or functional associations between the T-cell actin cytoskeleton and HIV-1 assembly and budding platforms at the plasma membrane.”
BackgroundInfluentialMechanisms of MAVS Regulation at the Mitochondrial Membrane
Jacobs, J. L., & Coyne, C. B. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.10.007 · Cited by 203
“TSPAN6 is a member of the membrane-embedded tetraspanin protein family that has been shown to have many different functions in the cell, including various roles in host immunity [87] Interestingly, TSPAN6 does not promote the ubiquitination of MAVS either directly or indirectly but is itself ubiquitinated in order to…”
BackgroundThe role of claudins in cancer metastasis
Tabariès, S., & Siegel, P. M. (2016) · Oncogene · doi:10.1038/onc.2016.289 · Cited by 198
More than one door – Budding of enveloped viruses through cellular membranes
Welsch, S., Müller, B., & Kräusslich, H. (2007) · FEBS Letters · doi:10.1016/j.febslet.2007.03.060 · Cited by 197
“membrane and some intracellular membranes (reviewed in [65]).”
Tauro, B. J., Mathias, R. A., Greening, D. W., Gopal, S. K., Ji, H. L., Kapp, E. A., Coleman, B. M., Hill, A. F., Kusebauch, U., Hallows, J. L., et al. (2013) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m112.027086 · Cited by 202
“They are reported to function as scaffolding proteins which interact with integrins; many tetraspanins have been implicated in tumour progression [92-94].”
BackgroundMutations in TSPAN12 Cause Autosomal-Dominant Familial Exudative Vitreoretinopathy
Poulter, J. A., Ali, M., Gilmour, D. F., Rice, A., Kondo, H., Hayashi, K., Mackey, D. A., Kearns, L. S., Ruddle, J. B., Craig, J. E., et al. (2010) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2010.01.012 · Cited by 193
“Members of this protein family are characterized by their ability to interact laterally with other tetraspanins and interacting proteins, thereby facilitating the production of large multimolecular membrane complexes, also called tetraspanin webs.(30) Through a number of cellbased assays and genetic interaction screen…”
BackgroundLatysheva, N., Muratov, G., Rajesh, S., Padgett, M., Hotchin, N. A., Overduin, M., & Berditchevski, F. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00849-06 · Cited by 191
“A considerable body of recent work has firmly established that TERM contribute to regulation of the activities of various transmembrane proteins (19, 29).”
BackgroundExtracellular Vesicles and Exosomes: Insights From Exercise Science
Nederveen, J. P., Warnier, G., Carlo, A. D., Nilsson, M. I., & Tarnopolsky, M. A. (2021) · Frontiers in Physiology · doi:10.3389/fphys.2020.604274 · Cited by 200
“…coupling, or other Ca2+-mediated events while later signals such as hormone release (e.g., cortisol), HPA axis activation (e.g., catecholamines), metabolic stress, and/or reactive oxygen species may potentiate the EV response (Savina et al., 2003; Eldh et al., 2010; Hergenreider et al., 2012).”
BackgroundPalmitoylation of membrane proteins (Review)
Charollais, J., & Goot, F. G. V. D. (2008) · Molecular Membrane Biology · doi:10.1080/09687680802620369 · Cited by 191
“TEMs are viewed as signaling microdomains that regulate integrin-dependent adhesion [51,52,56] and their disassembly leads to altered adhesion and cell spreading [54].”
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Yang, X. H., Richardson, A. L., Torres-Arzayus, M. I., Zhou, P., Sharma, C., Kazarov, A. R., Andzelm, M. M., Strominger, J. L., Brown, M., & Hemler, M. E. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-2949 · Cited by 183
“CD151 may link laminin-binding integrins to other proteins within the plasma membrane (38, 39).”
BackgroundSelf-citationThe Norrin/Frizzled4 signaling pathway in retinal vascular development and disease
Ye, X., Wang, Y., & Nathans, J. (2010) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2010.07.003 · Cited by 186
“Members of this family participate in diverse cellular processes, and several of them can organize microdomains in the plasma membrane [34].”
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“These modifications enable organization of tetraspanin-enriched microdomains (TEMs) on the cell membrane that allow interaction with integrin molecules (92).”
BackgroundEbnet, K. (2017) · Physiological Reviews · doi:10.1152/physrev.00004.2017 · Cited by 179
“Tetraspanins assemble protein complexes in the membrane through lateral associations to form tetraspanin-enriched microdomains (83).”
BackgroundStress response signaling and virulence: insights from entomopathogenic fungi
Ortiz‐Urquiza, A., & Keyhani, N. O. (2014) · Current Genetics · doi:10.1007/s00294-014-0439-9 · Cited by 176
Metastasis suppressors genes in cancer
Stafford, L. J., Vaidya, K. S., & Welch, D. R. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.12.016 · Cited by 176
Dornier, E., Coumailleau, F., Ottavi, J., Moretti, J., Boucheix, C., Mauduit, P., Schweisguth, F., & Rubinstein, E. (2012) · The Journal of Cell Biology · doi:10.1083/jcb.201201133 · Cited by 175
“They are expressed in many cell types and have been implicated in various biological processes including cell migration, cell fusion, lymphocyte activation, as well as viral and parasitic infections (Hemler, 2005; Charrin et al., 2009).”
Liver fluke vaccines in ruminants: strategies, progress and future opportunities
Toet, H., Piedrafita, D. M., & Spithill, T. W. (2014) · International Journal for Parasitology · doi:10.1016/j.ijpara.2014.07.011 · Cited by 173
Bacteria-Induced Uroplakin Signaling Mediates Bladder Response to Infection
Thumbikat, P., Berry, R. E., Zhou, G., Billips, B. K., Yaggie, R. E., Zaichuk, T. A., Sun, T., Schaeffer, A. J., & Klumpp, D. J. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000415 · Cited by 173
“Tetraspanins typically function as transmembrane linkers in a complex with other proteins that then transduce signals [48].”
BackgroundMicrovesicles/exosomes as potential novel biomarkers of metabolic diseases
ller, G. M. A. U. (2012) · Diabetes Metabolic Syndrome and Obesity · doi:10.2147/dmso.s32923 · Cited by 178
“Tetraspanins have been implicated in a multitude of biological processes, such as cell adhesion, migration, fusion, and signal transduction through their associated partner molecules.(72,73) Microarray analysis showed that CD9 expression in tumor cells correlated with the down-regulation of several Wnt family genes an…”
BackgroundVicente‐Manzanares, M., & Horwitz, A. R. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-207-6_1 · Cited by 179
Rethinking glomerular basement membrane thickening in diabetic nephropathy: adaptive or pathogenic?
Marshall, C. B. (2016) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00313.2016 · Cited by 179
Deletion of tetraspanin Cd151 results in decreased pathologic angiogenesis in vivo and in vitro
Takeda, Y., Kazarov, A. R., Butterfield, C., Hopkins, B. D., Benjamin, L. E., Kaipainen, A., & Hemler, M. E. (2006) · Blood · doi:10.1182/blood-2006-08-041970 · Cited by 167
Self-citationLaminin-binding integrins and their tetraspanin partners as potential antimetastatic targets
Stipp, C. S. (2010) · Expert Reviews in Molecular Medicine · doi:10.1017/s1462399409001355 · Cited by 165
“and Hemler, M.E. (2003) EWI-2 regulates alpha3beta1 integrin-”
Tabariès, S., Dong, Z., Annis, M. G., Ömeroğlu, A., Pepin, F., Ouellet, V., Russo, C., Hassanain, M. M., Metrakos, P. P., Diaz, Z., et al. (2010) · Oncogene · doi:10.1038/onc.2010.518 · Cited by 165
“In this regard, tetraspanins are essential for adhesion strengthening of integrin-containing complexes and individual tetraspanins have been found in complexes with numerous integrin partners (Hemler, 2005; Lazo, 2007).”
BackgroundBeckmann, J., Scheitza, S., Wernet, P., Fischer, J., & Giebel, B. (2007) · Blood · doi:10.1182/blood-2006-11-055921 · Cited by 160
“However, little is known about their function, though tetraspanins seem to take part in regulating the activation, the motility and the antigen presentation of different leukocytes.(37,38) Interestingly, it has been shown that, in addition to the cell surface, many tetraspanins including CD53 and CD63 are localized on…”
Background
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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