The spatial distribution of proteins in cell membranes is crucial for signal transduction, cell communication and membrane trafficking. Members of the Tetraspanin family organize functional protein clusters within the plasma membrane into so-called Tetraspanin-enriched microdomains (TEMs). Direct interactions between Tetraspanins are believed to be important for this organization. However, studies thus far have utilized mainly co-immunoprecipitation methods that cannot distinguish between direct and indirect, through common partners, interactions. Here we study Tetraspanin 8 homointeractions in living cells via quantitative fluorescence microscopy. We demonstrate that Tetraspanin 8 exists in a monomer-dimer equilibrium in the plasma membrane. Tetraspanin 8 dimerization is described by a high dissociation constant (Kd = 14 700 ± 1100 Tspan8/µm2), one of the highest dissociation constants measured for membrane proteins in live cells. We propose that this high dissociation constant, and thus the short lifetime of the Tetraspanin 8 dimer, is critical for Tetraspanin 8 functioning as a master regulator of cell signaling.
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Cover Image
In this issue, Low-Gan and colleagues (pp. 3671–3684) analyzed the binding surface of ACE2 from several important animal species to begin to understand the parameters for the ACE2 recognition by the SARSCoV-2 spike protein receptor binding domain. The residue differences and binding properties between the species’ variants provide a framework for understanding ACE2-RBD binding and virus tropism. The cover image shows the variable residues at the ACE2-RBD interface of individual species. Image courtesy of Vaughn V. Smider.
Quantitative characterization of tetraspanin 8 homointeractions in the plasma membrane
Daniel Wirth, Ece Özdemir, Christopher King, Lena Ahlswede, Dirk Schneider, Kalina Hristova; Quantitative characterization of tetraspanin 8 homointeractions in the plasma membrane. Biochem J 15 October 2021; 478 (19): 3643–3654. doi: https://doi.org/10.1042/BCJ20210459
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