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Life Sci Alliance ; 3(11)2020 11.
Artículo en Inglés | MEDLINE | ID: mdl-32958604

RESUMEN

Tetraspanins are eukaryotic membrane proteins that contribute to a variety of signaling processes by organizing partner-receptor molecules in the plasma membrane. How tetraspanins bind and cluster partner receptors into tetraspanin-enriched microdomains is unknown. Here, we present crystal structures of the large extracellular loop of CD9 bound to nanobodies 4C8 and 4E8 and, the cryo-EM structure of 4C8-bound CD9 in complex with its partner EWI-F. CD9-EWI-F displays a tetrameric arrangement with two central EWI-F molecules, dimerized through their ectodomains, and two CD9 molecules, one bound to each EWI-F transmembrane helix through CD9-helices h3 and h4. In the crystal structures, nanobodies 4C8 and 4E8 bind CD9 at loops C and D, which is in agreement with the 4C8 conformation in the CD9-EWI-F complex. The complex varies from nearly twofold symmetric (with the two CD9 copies nearly anti-parallel) to ca. 50° bent arrangements. This flexible arrangement of CD9-EWI-F with potential CD9 homo-dimerization at either end provides a "concatenation model" for forming short linear or circular assemblies, which may explain the occurrence of tetraspanin-enriched microdomains.


Asunto(s)
Tetraspanina 29/metabolismo , Tetraspanina 29/ultraestructura , Antígenos CD/química , Antígenos CD/metabolismo , Antígenos CD/ultraestructura , Proteínas Portadoras/metabolismo , Línea Celular Tumoral , Membrana Celular/metabolismo , Humanos , Glicoproteínas de Membrana/química , Proteínas de la Membrana/química , Proteínas de la Membrana/metabolismo , Proteínas de la Membrana/ultraestructura , Tetraspanina 28/metabolismo , Tetraspanina 28/ultraestructura , Tetraspanina 29/fisiología , Tetraspaninas/metabolismo , Tetraspaninas/fisiología , Tetraspaninas/ultraestructura , Factores de Transcripción/metabolismo
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